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Bruker Corporation aha1 28 335
Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

Journal: Molecules

doi: 10.3390/molecules26071943

Sequence alignment of representative Aha1 homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
Figure Legend Snippet: Sequence alignment of representative Aha1 homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .

Techniques Used: Sequencing, Generated

Structural statistics for the calculated solution structures of Aha1 28−162 and  Aha1 28−335  .
Figure Legend Snippet: Structural statistics for the calculated solution structures of Aha1 28−162 and Aha1 28−335 .

Techniques Used:

Aha1’s C-terminal domain presents unique dynamics behavior and structural features different from Aha1’s N-terminal domain. ( a ) Ribbon representation of the solution structure of human Aha1’s N-terminal domain (Aha1 28−162 ). Aromatic residues (W35, F44, F79, F80, Y81, W83, W89, Y99, H102, Y151 and F159) are highlighted in pink. ( b ) Ribbon representation of the solution structure of human Aha1’s C-terminal domain (Aha1 204−335 , PDB code: 1 × 53). Aromatic residues (F215, Y223, F226, F235, H237, F250, H251, F261, H269, W274, F276, W279, H283, F284, F291, W319, Y322, Y323, F324, F331 and Y333) are highlighted in pink. ( c ) The Tm values of Aha1 28−162 , Aha1 204−335 and Aha1 28−335 were determined. The measured melting temperatures for Aha1 204−335 , Aha1 28−162 and Aha1 28−335 are 72.41 ± 0.14 °C, 54.45 ± 0.18 °C and 54.25 ± 0.09 °C, respectively. ( d ) Reduced spectral density functions of human Aha1’s C-terminal domain (Aha1 204−335 ) in its free state.
Figure Legend Snippet: Aha1’s C-terminal domain presents unique dynamics behavior and structural features different from Aha1’s N-terminal domain. ( a ) Ribbon representation of the solution structure of human Aha1’s N-terminal domain (Aha1 28−162 ). Aromatic residues (W35, F44, F79, F80, Y81, W83, W89, Y99, H102, Y151 and F159) are highlighted in pink. ( b ) Ribbon representation of the solution structure of human Aha1’s C-terminal domain (Aha1 204−335 , PDB code: 1 × 53). Aromatic residues (F215, Y223, F226, F235, H237, F250, H251, F261, H269, W274, F276, W279, H283, F284, F291, W319, Y322, Y323, F324, F331 and Y333) are highlighted in pink. ( c ) The Tm values of Aha1 28−162 , Aha1 204−335 and Aha1 28−335 were determined. The measured melting temperatures for Aha1 204−335 , Aha1 28−162 and Aha1 28−335 are 72.41 ± 0.14 °C, 54.45 ± 0.18 °C and 54.25 ± 0.09 °C, respectively. ( d ) Reduced spectral density functions of human Aha1’s C-terminal domain (Aha1 204−335 ) in its free state.

Techniques Used:

Aha1’s N-terminal domain and C-terminal domain are linked through a long unstructured loop, which confers a low restriction to the relative positioning of these two domains in solution. ( a ) Ribbon representation of the solution structure of human Aha1 28−335 . The N-terminal domain and the C-terminal domain of Aha1 are colored in cyan and golden orange, respectively. ( b ) Reduced spectral density functions of human Aha1 28−335 .
Figure Legend Snippet: Aha1’s N-terminal domain and C-terminal domain are linked through a long unstructured loop, which confers a low restriction to the relative positioning of these two domains in solution. ( a ) Ribbon representation of the solution structure of human Aha1 28−335 . The N-terminal domain and the C-terminal domain of Aha1 are colored in cyan and golden orange, respectively. ( b ) Reduced spectral density functions of human Aha1 28−335 .

Techniques Used:

The very N-terminal region and the C-terminal RLF motif of Aha1 present no significant effect on the global fold of the protein. ( a , a I , a II , a III , a IV ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−338 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that underwent resonance shifting upon the absence of Aha1’s very N-terminal fragment (M1-W27). ( b ) The measured Tm values for Aha1 1−338 , Aha1 28−338 and Aha1 28−335 were 55.16 ± 0.11 °C, 53.72 ± 0.05 °C and 53.84 ± 0.04 °C, respectively. ( c , c I ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−335 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance shifting upon the absence of Aha1’s C-terminal RLF motif.
Figure Legend Snippet: The very N-terminal region and the C-terminal RLF motif of Aha1 present no significant effect on the global fold of the protein. ( a , a I , a II , a III , a IV ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−338 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that underwent resonance shifting upon the absence of Aha1’s very N-terminal fragment (M1-W27). ( b ) The measured Tm values for Aha1 1−338 , Aha1 28−338 and Aha1 28−335 were 55.16 ± 0.11 °C, 53.72 ± 0.05 °C and 53.84 ± 0.04 °C, respectively. ( c , c I ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−335 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance shifting upon the absence of Aha1’s C-terminal RLF motif.

Techniques Used: Labeling

Both the N-terminal fragment M1-W27 and the C-terminal RLF motif of Aha1 contribute to the recognition of α-synuclein. ( a , a I , a II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−335 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. ( b , b I , b II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( c , c I , c II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( d ) The ThT data indicates that full-length Aha1 exhibits an inhibition effect on the aggregation process of α-synuclein. Decreased ThT emission was observed when Aha1 1−338 but not Aha1 28−335 was premixed with α-synuclein before the further incubation ( n = 3; ** p < 0.05). ( e ) Inhibitory effect of full-length Aha1 on α-synuclein aggregation. Transmission electron microscopy (120 kV) of α-synuclein fibril (14 μM) incubated with 1.4 μM Aha1 for three days (scale bar: 200 nm).
Figure Legend Snippet: Both the N-terminal fragment M1-W27 and the C-terminal RLF motif of Aha1 contribute to the recognition of α-synuclein. ( a , a I , a II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−335 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. ( b , b I , b II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( c , c I , c II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( d ) The ThT data indicates that full-length Aha1 exhibits an inhibition effect on the aggregation process of α-synuclein. Decreased ThT emission was observed when Aha1 1−338 but not Aha1 28−335 was premixed with α-synuclein before the further incubation ( n = 3; ** p < 0.05). ( e ) Inhibitory effect of full-length Aha1 on α-synuclein aggregation. Transmission electron microscopy (120 kV) of α-synuclein fibril (14 μM) incubated with 1.4 μM Aha1 for three days (scale bar: 200 nm).

Techniques Used: Labeling, Inhibition, Incubation, Transmission Assay, Electron Microscopy

Human Aha1 acts as a holdase-like chaperone and inhibits the aggregation process of α-synuclein in vitro. Part of the presentation was generated by using the reported structure of α-synuclein (PDB code: 6XYO ) and the Open-Source PyMOL 1.8.
Figure Legend Snippet: Human Aha1 acts as a holdase-like chaperone and inhibits the aggregation process of α-synuclein in vitro. Part of the presentation was generated by using the reported structure of α-synuclein (PDB code: 6XYO ) and the Open-Source PyMOL 1.8.

Techniques Used: In Vitro, Generated


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    Bruker Corporation aha1 28 335
    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Thermo Fisher leaf 28 330 331 332 333 334 335 336 337 338 339 340 341 342 343 344 q13
    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Makhteshim Chemical Works Ltd molecular formula c13h16f3n3o4 molecular mass 335 28 structural formula n cf3 no2o2n efsa scientific report
    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Dow AgroSciences molecular formula c13h16f3n3o4 molecular mass 335 28 structural formula n cf3 no2o2n efsa scientific report
    Sequence alignment of representative <t>Aha1</t> homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .
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    Sequence alignment of representative Aha1 homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: Sequence alignment of representative Aha1 homologs from different species. The conserved residues are marked in red. The charged residues and the tryptophan residues in the very N-terminal region of Aha1 are highlighted in purple and green, respectively. The C-terminal RLF motif of Aha1 from higher eukaryotes is highlighted in blue. The sequence alignment result was generated by using CLUSTALW and ESPript 3.0 .

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques: Sequencing, Generated

    Structural statistics for the calculated solution structures of Aha1 28−162 and  Aha1 28−335  .

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: Structural statistics for the calculated solution structures of Aha1 28−162 and Aha1 28−335 .

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques:

    Aha1’s C-terminal domain presents unique dynamics behavior and structural features different from Aha1’s N-terminal domain. ( a ) Ribbon representation of the solution structure of human Aha1’s N-terminal domain (Aha1 28−162 ). Aromatic residues (W35, F44, F79, F80, Y81, W83, W89, Y99, H102, Y151 and F159) are highlighted in pink. ( b ) Ribbon representation of the solution structure of human Aha1’s C-terminal domain (Aha1 204−335 , PDB code: 1 × 53). Aromatic residues (F215, Y223, F226, F235, H237, F250, H251, F261, H269, W274, F276, W279, H283, F284, F291, W319, Y322, Y323, F324, F331 and Y333) are highlighted in pink. ( c ) The Tm values of Aha1 28−162 , Aha1 204−335 and Aha1 28−335 were determined. The measured melting temperatures for Aha1 204−335 , Aha1 28−162 and Aha1 28−335 are 72.41 ± 0.14 °C, 54.45 ± 0.18 °C and 54.25 ± 0.09 °C, respectively. ( d ) Reduced spectral density functions of human Aha1’s C-terminal domain (Aha1 204−335 ) in its free state.

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: Aha1’s C-terminal domain presents unique dynamics behavior and structural features different from Aha1’s N-terminal domain. ( a ) Ribbon representation of the solution structure of human Aha1’s N-terminal domain (Aha1 28−162 ). Aromatic residues (W35, F44, F79, F80, Y81, W83, W89, Y99, H102, Y151 and F159) are highlighted in pink. ( b ) Ribbon representation of the solution structure of human Aha1’s C-terminal domain (Aha1 204−335 , PDB code: 1 × 53). Aromatic residues (F215, Y223, F226, F235, H237, F250, H251, F261, H269, W274, F276, W279, H283, F284, F291, W319, Y322, Y323, F324, F331 and Y333) are highlighted in pink. ( c ) The Tm values of Aha1 28−162 , Aha1 204−335 and Aha1 28−335 were determined. The measured melting temperatures for Aha1 204−335 , Aha1 28−162 and Aha1 28−335 are 72.41 ± 0.14 °C, 54.45 ± 0.18 °C and 54.25 ± 0.09 °C, respectively. ( d ) Reduced spectral density functions of human Aha1’s C-terminal domain (Aha1 204−335 ) in its free state.

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques:

    Aha1’s N-terminal domain and C-terminal domain are linked through a long unstructured loop, which confers a low restriction to the relative positioning of these two domains in solution. ( a ) Ribbon representation of the solution structure of human Aha1 28−335 . The N-terminal domain and the C-terminal domain of Aha1 are colored in cyan and golden orange, respectively. ( b ) Reduced spectral density functions of human Aha1 28−335 .

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: Aha1’s N-terminal domain and C-terminal domain are linked through a long unstructured loop, which confers a low restriction to the relative positioning of these two domains in solution. ( a ) Ribbon representation of the solution structure of human Aha1 28−335 . The N-terminal domain and the C-terminal domain of Aha1 are colored in cyan and golden orange, respectively. ( b ) Reduced spectral density functions of human Aha1 28−335 .

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques:

    The very N-terminal region and the C-terminal RLF motif of Aha1 present no significant effect on the global fold of the protein. ( a , a I , a II , a III , a IV ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−338 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that underwent resonance shifting upon the absence of Aha1’s very N-terminal fragment (M1-W27). ( b ) The measured Tm values for Aha1 1−338 , Aha1 28−338 and Aha1 28−335 were 55.16 ± 0.11 °C, 53.72 ± 0.05 °C and 53.84 ± 0.04 °C, respectively. ( c , c I ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−335 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance shifting upon the absence of Aha1’s C-terminal RLF motif.

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: The very N-terminal region and the C-terminal RLF motif of Aha1 present no significant effect on the global fold of the protein. ( a , a I , a II , a III , a IV ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−338 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that underwent resonance shifting upon the absence of Aha1’s very N-terminal fragment (M1-W27). ( b ) The measured Tm values for Aha1 1−338 , Aha1 28−338 and Aha1 28−335 were 55.16 ± 0.11 °C, 53.72 ± 0.05 °C and 53.84 ± 0.04 °C, respectively. ( c , c I ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 (colored in black) and 15 N-labeled Aha1 28−335 (colored in red). Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance shifting upon the absence of Aha1’s C-terminal RLF motif.

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques: Labeling

    Both the N-terminal fragment M1-W27 and the C-terminal RLF motif of Aha1 contribute to the recognition of α-synuclein. ( a , a I , a II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−335 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. ( b , b I , b II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( c , c I , c II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( d ) The ThT data indicates that full-length Aha1 exhibits an inhibition effect on the aggregation process of α-synuclein. Decreased ThT emission was observed when Aha1 1−338 but not Aha1 28−335 was premixed with α-synuclein before the further incubation ( n = 3; ** p < 0.05). ( e ) Inhibitory effect of full-length Aha1 on α-synuclein aggregation. Transmission electron microscopy (120 kV) of α-synuclein fibril (14 μM) incubated with 1.4 μM Aha1 for three days (scale bar: 200 nm).

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: Both the N-terminal fragment M1-W27 and the C-terminal RLF motif of Aha1 contribute to the recognition of α-synuclein. ( a , a I , a II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−335 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. ( b , b I , b II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 28−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( c , c I , c II ) Superposition of 1 H- 15 N-HSQC spectra recorded on 15 N-labeled Aha1 1−338 without (colored in black) or with (colored in red) the addition of 10-fold molar excess of unlabeled α-synuclein. Selected 1 H- 15 N-HSQC spectra regions are expanded to view representative residues that undergo resonance attenuations upon the presence of α-synuclein. ( d ) The ThT data indicates that full-length Aha1 exhibits an inhibition effect on the aggregation process of α-synuclein. Decreased ThT emission was observed when Aha1 1−338 but not Aha1 28−335 was premixed with α-synuclein before the further incubation ( n = 3; ** p < 0.05). ( e ) Inhibitory effect of full-length Aha1 on α-synuclein aggregation. Transmission electron microscopy (120 kV) of α-synuclein fibril (14 μM) incubated with 1.4 μM Aha1 for three days (scale bar: 200 nm).

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques: Labeling, Inhibition, Incubation, Transmission Assay, Electron Microscopy

    Human Aha1 acts as a holdase-like chaperone and inhibits the aggregation process of α-synuclein in vitro. Part of the presentation was generated by using the reported structure of α-synuclein (PDB code: 6XYO ) and the Open-Source PyMOL 1.8.

    Journal: Molecules

    Article Title: Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity

    doi: 10.3390/molecules26071943

    Figure Lengend Snippet: Human Aha1 acts as a holdase-like chaperone and inhibits the aggregation process of α-synuclein in vitro. Part of the presentation was generated by using the reported structure of α-synuclein (PDB code: 6XYO ) and the Open-Source PyMOL 1.8.

    Article Snippet: Meanwhile, 1 H- 15 N-HSQC, 15 N-IPAP-HSQC, HNCO, HN(CA)CO, HNCA, HNCACB, CBCA(CO)NH, HBHA(CO)NH, H(CC)(CO)NH and 15 N-NOESY-HSQC spectra were acquired on Bruker 600 MHz or 900 MHz NMR spectrometers equipped with TCI cryoprobe at 25 °C for solution structure determination of Aha1 28−335 .

    Techniques: In Vitro, Generated