Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase
about
The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework.A database of macromolecular motionsAssessing local structural perturbations in proteinsStructure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channelThe Structure of Lombricine Kinase: IMPLICATIONS FOR PHOSPHAGEN KINASE CONFORMATIONAL CHANGESStructural characterization of the apo form and NADH binary complex of human lactate dehydrogenaseHot spots in cold adaptation: localized increases in conformational flexibility in lactate dehydrogenase A4 orthologs of Antarctic notothenioid fishesDiversity of function-related conformational changes in proteins: coordinate uncertainty, fragment rigidity, and stabilityUsing least median of squares for structural superposition of flexible proteinsFrom DNA to fitness differences: sequences and structures of adaptive variants of Colias phosphoglucose isomerase (PGI).Induced fit in arginine kinase.Models to Approximate the Motions of Protein Loops.Evolution of oligomeric state through allosteric pathways that mimic ligand bindingReFlexIn: a flexible receptor protein-ligand docking scheme evaluated on HIV-1 proteaseSparse estimation for structural variability.Search for Human Lactate Dehydrogenase A Inhibitors Using Structure-Based Modeling.De novo prediction of polypeptide conformations using dihedral probability grid Monte Carlo methodologyInduced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase.pFlexAna: detecting conformational changes in remotely related proteins.Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.ViewMotions Rainbow: a new method to illustrate molecular motions in proteinsThe importance of slow motions for protein functional loops.Protein flexibility: coordinate uncertainties and interpretation of structural differences.Identification of New Structural Fragments for the Design of Lactate Dehydrogenase A InhibitorsThe pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysisOptimal superpositioning of flexible molecule ensembles.Sequence-, structure-, and dynamics-based comparisons of structurally homologous CheY-like proteins.The flexibility of a distant loop modulates active site motion and product release in ribonuclease A.Structural flexibility and protein adaptation to temperature: Molecular dynamics analysis of malate dehydrogenases of marine molluscs.
P2860
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P2860
Analysis of protein loop closure. Two types of hinges produce one motion in lactate dehydrogenase
description
1991 nî lūn-bûn
@nan
1991 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@ast
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@en
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@nl
type
label
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@ast
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@en
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@nl
prefLabel
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@ast
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@en
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@nl
P1476
Analysis of protein loop closu ...... otion in lactate dehydrogenase
@en
P304
P407
P577
1991-07-05T00:00:00Z