Conformational plasticity of an enzyme during catalysis: intricate coupling between cyclophilin A dynamics and substrate turnover.
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Full Atom Simulations of Spin Label ConformationsKeep on moving: discovering and perturbing the conformational dynamics of enzymesComparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.Dynamical network of residue-residue contacts reveals coupled allosteric effects in recognition, catalysis, and mutation.Cyclophilin40 isomerase activity is regulated by a temperature-dependent allosteric interaction with Hsp90.Isolation and purification of Bacillus thuringiensis var. israelensis IМV В-7465 peptidase with specificity toward elastin and collagen.Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis.Application of quantum mechanics/molecular mechanics methods in the study of enzymatic reaction mechanismsIn Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function
P2860
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P2860
Conformational plasticity of an enzyme during catalysis: intricate coupling between cyclophilin A dynamics and substrate turnover.
description
2013 nî lūn-bûn
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2013年の論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年論文
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2013年论文
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name
Conformational plasticity of a ...... namics and substrate turnover.
@ast
Conformational plasticity of a ...... namics and substrate turnover.
@en
type
label
Conformational plasticity of a ...... namics and substrate turnover.
@ast
Conformational plasticity of a ...... namics and substrate turnover.
@en
prefLabel
Conformational plasticity of a ...... namics and substrate turnover.
@ast
Conformational plasticity of a ...... namics and substrate turnover.
@en
P2860
P1433
P1476
Conformational plasticity of a ...... namics and substrate turnover.
@en
P2093
Donald Hamelberg
Lauren C McGowan
P2860
P304
P356
10.1016/J.BPJ.2012.11.3815
P407
P577
2013-01-08T00:00:00Z