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amicon ultra-15 centrifugal filter units  (Millipore)
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Millipore amicon ultra-15 centrifugal filter units
Amicon Ultra 15 Centrifugal Filter Units, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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amicon ultra-15 centrifugal filter units - by Bioz Stars, 2026-03
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program pymol  (DeLano Scientific)
90
DeLano Scientific program pymol
(A) This figure depicts the structure of Cp14ε which is a conventional 14-3-3 dimer in every respect, from structure to peptide-binding to dimerization interface. One subunit is in red while the other is in gray. The peptide RAI(pS)LP is bound in each binding groove. The Arg-Arg-Tyr triad is shown in the gray subunit. This and subsequent figures of protein structures were rendered using the program <t>PyMol</t> <t>(Delano</t> Scientific, Palo Alto, CA, USA). (B) Dimerization interface between the two subunits of Cp14ε features the same Arg-Glu salt bridges previously identified in human 14-3-3 proteins.
Program Pymol, supplied by DeLano Scientific, 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/result/program pymol/product/DeLano Scientific
Average 90 stars, based on 1 article reviews
program pymol - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


(A) This figure depicts the structure of Cp14ε which is a conventional 14-3-3 dimer in every respect, from structure to peptide-binding to dimerization interface. One subunit is in red while the other is in gray. The peptide RAI(pS)LP is bound in each binding groove. The Arg-Arg-Tyr triad is shown in the gray subunit. This and subsequent figures of protein structures were rendered using the program PyMol (Delano Scientific, Palo Alto, CA, USA). (B) Dimerization interface between the two subunits of Cp14ε features the same Arg-Glu salt bridges previously identified in human 14-3-3 proteins.

Journal: PLoS ONE

Article Title: Characterization of 14-3-3 Proteins from Cryptosporidium parvum

doi: 10.1371/journal.pone.0014827

Figure Lengend Snippet: (A) This figure depicts the structure of Cp14ε which is a conventional 14-3-3 dimer in every respect, from structure to peptide-binding to dimerization interface. One subunit is in red while the other is in gray. The peptide RAI(pS)LP is bound in each binding groove. The Arg-Arg-Tyr triad is shown in the gray subunit. This and subsequent figures of protein structures were rendered using the program PyMol (Delano Scientific, Palo Alto, CA, USA). (B) Dimerization interface between the two subunits of Cp14ε features the same Arg-Glu salt bridges previously identified in human 14-3-3 proteins.

Article Snippet: With Cp14ε being close to or over 60% identical to most human 14-3-3 proteins, its structure is expectedly congruent to the human homologues (see ), deviating from the 14-3-3ε (2BR9), η (2C74), σ (1YWT), γ (2B05), ζ (1QJA), τ/θ (2BTP) and β (2C23), structures by root mean square (RMS) values of 0.9, 1.1, 1.2, 1.2, 1.5, 1.6 and 1.9 Å respectively, as measured in the program Pymol (Delano Scientific, CA).

Techniques: Binding Assay