compex Search Results


krf excimer laser  (Coherent Corp)
97
Coherent Corp krf excimer laser
Krf Excimer Laser, supplied by Coherent Corp, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/COMPEX/arxiv__2107__05591-64-3-7
Average 97 stars, based on 1 article reviews
krf excimer laser - by Bioz Stars, 2026-10
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atpase domain of dnak  (Compex Inc)
90
Compex Inc atpase domain of dnak
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Atpase Domain Of Dnak, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/atpase+domain+of+dnak/pmc02773841-91-34-31
Average 90 stars, based on 1 article reviews
atpase domain of dnak - by Bioz Stars, 2026-10
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pd(tfa)2  (Compex Inc)
90
Compex Inc pd(tfa)2
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Pd(tfa)2, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/pd+tfa+2/us09809596-111-1-1
Average 90 stars, based on 1 article reviews
pd(tfa)2 - by Bioz Stars, 2026-10
90/100 stars
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vehicle's wifi  (Compex Inc)
90
Compex Inc vehicle's wifi
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Vehicle's Wifi, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/vehicle+s+wifi/us12177766-74-10-15
Average 90 stars, based on 1 article reviews
vehicle's wifi - by Bioz Stars, 2026-10
90/100 stars
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compex® rehab unit  (Compex Inc)
90
Compex Inc compex® rehab unit
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Compex® Rehab Unit, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/compex++rehab+unit/10__1590_slash_s1679___45082015rw3140-406-52-58
Average 90 stars, based on 1 article reviews
compex® rehab unit - by Bioz Stars, 2026-10
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self-adhesive electrodes 50mm 50mm  (Compex Inc)
90
Compex Inc self-adhesive electrodes 50mm 50mm
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Self Adhesive Electrodes 50mm 50mm, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/self+adhesive+electrodes+50mm+50mm/pm15289804-69-6-11
Average 90 stars, based on 1 article reviews
self-adhesive electrodes 50mm 50mm - by Bioz Stars, 2026-10
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self-adhesive surface electrodes compex dura-stick plus  (Compex Inc)
90
Compex Inc self-adhesive surface electrodes compex dura-stick plus
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Self Adhesive Surface Electrodes Compex Dura Stick Plus, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/self+adhesive+gel+electrodes+performance/pm40122808-75-5-7
Average 90 stars, based on 1 article reviews
self-adhesive surface electrodes compex dura-stick plus - by Bioz Stars, 2026-10
90/100 stars
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motor point pen electrode  (Compex Inc)
90
Compex Inc motor point pen electrode
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Motor Point Pen Electrode, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/small+pen+electrode+motor+point+pen/pm26849999-72-1-6
Average 90 stars, based on 1 article reviews
motor point pen electrode - by Bioz Stars, 2026-10
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krf excimer laser coherent compex pro 201f  (Compex Inc)
90
Compex Inc krf excimer laser coherent compex pro 201f
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Krf Excimer Laser Coherent Compex Pro 201f, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/krf+excimer+laser/pmc08788136-73-7-11
Average 90 stars, based on 1 article reviews
krf excimer laser coherent compex pro 201f - by Bioz Stars, 2026-10
90/100 stars
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pulsed laser deposition system krf excimer laser compex pro 205  (Compex Inc)
90
Compex Inc pulsed laser deposition system krf excimer laser compex pro 205
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
Pulsed Laser Deposition System Krf Excimer Laser Compex Pro 205, supplied by Compex Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/compex/coherent+compex+pro+201+f+krf+excimer+laser/10__1002_slash_ente__201600117-172-13-21
Average 90 stars, based on 1 article reviews
pulsed laser deposition system krf excimer laser compex pro 205 - by Bioz Stars, 2026-10
90/100 stars
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xecl excimer laser  (Compex Inc)
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Compex Inc xecl excimer laser
Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
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Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) <t>ATPase</t> domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b <t>)</t> <t>Compex</t> of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).
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Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) ATPase domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b ) Compex of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).

Journal: Cellular and Molecular Life Sciences

Article Title: Hsp70 chaperones: Cellular functions and molecular mechanism

doi: 10.1007/s00018-004-4464-6

Figure Lengend Snippet: Structural aspects of Hsp70 chaperones and their interaction with co-chaperones and substrates. ( a ) ATPase domain of bovine Hsc70 . Secondary structure representation of the ATPase domain of bovine Hsc70 in complex with ADP, inorganic phosphate and two potassium ions. To emphasized the flexibility and shearing motion of the ATPase domain an overlay of the x-ray structure (cyan; PDB entry code 1BUP; ) and a model derived by NMR using the method of residual dipolar coupling (dark blue; ) is shown. The two structures were aligned in the program WeblabViewer (Accelrys, San Diego) using tethers in subdomain IA only. ( b ) Compex of the ATPase domain of DnaK with a dimer of GrpE X-ray structure of the complex of the DnaK ATPase domain (blue) and the GrpE dimer (orange and yellow; PDB entry code 1DKG; ). In ball-and-stick and transparent surface representation are indicated the interacting residues. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1. X-ray structure of the complex of the human Hsc70 ATPase domain (green) and a fragment of Bag-1 (magenta; PDB entry code 1HX1; ). The interacting residues and the potential salt bridge (K56-E268) are indicated. The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( d ) Model of the structure of the substrate binding domain. Ribbon representation of the structure of the substrate binding domain of E. coli DnaK (PDB entry code 1DKX; ) with bound peptide substrate (as stick model). Indicated are residues that contact the substrate in space-filling representation and residues that form the so-called latch of H-bonds and a salt bridge in ball-and-stick representation. (e) Interaction of E. coli DnaK with a peptide substrate. X-ray structure of the β -sheet domain of E. coli DnaK (PDB entry code 1DKX; ) in ribbon representation in complex with the peptide NRLLLTG in stick representation. Orientation as indicated in the inset with a -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. ( f ) Interaction of E. coli HscA with a peptide substrate. X-ray structure of the β -sheet domain of E. coli HscA (PDB entry code 1U00; in ribbon representation in complex with the peptide ELPPVKIHC in stick representation. Orientation as indicated in the inset of panel ( e ) with α -helices cut away along the dashed line and rotated by 90°. H-bonds to the backbone of the substrate are indicated as dotted lines. Note the inverse orientation as compared to the peptide in ( e ).

Article Snippet: The ATPase domain is rotated by about 90° as compared to the representation shown in ( a ) as indicated at the bottom of panel ( a ). ( c ) Compex of the ATPase domain of Hsc70 with the Bag-domain fragment of Bag-1.

Techniques: Derivative Assay, Binding Assay