Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
about
Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.Relaxation dispersion NMR spectroscopy as a tool for detailed studies of protein folding.Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.Partially folded states of staphylococcal nuclease highlight the conserved structural hierarchy of OB-fold proteins.Protein folding and misfolding: mechanism and principles.Visualizing transient dark states by NMR spectroscopy.Characterization of a transient unfolding intermediate in a core mutant of γS-crystallin.Protein folding: independent unrelated pathways or predetermined pathway with optional errorsCytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway.Characterizing and controlling the inherent dynamics of cyclophilin-A.Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy.NMR spectroscopy brings invisible protein states into focus.What lessons can be learned from studying the folding of homologous proteins?An exact solution for R2,eff in CPMG experiments in the case of two site chemical exchangeStable folding intermediates prevent fast interconversion between the closed and open states of Mad2 through its denatured state.
P2860
Q30156869-5728D523-6BC9-49A7-B132-71FC51DBFAF4Q30157327-B98AF311-1512-44EC-B44F-49AFCAF188C8Q30157745-407D7338-0281-41B5-9C04-0153D6E5637CQ30157912-0D814656-4CC0-41B3-B7BE-8B5ECDBD58D7Q30368801-E8D5BFCC-C25F-4907-8724-A23AF1F23E7BQ34464287-82CDDBC9-F096-48C7-A924-06F690BD4589Q35173750-B73FE8FD-54B2-4574-A18E-9B4AF3BAF3B9Q36734703-030F7E16-FC47-422C-8C77-65FCF9251800Q36802526-1357ECB5-8336-4ADF-BF02-19EFC696CFCDQ37388911-9086B1E7-035B-4AE8-8A06-35F73FF97126Q37401352-DFEFFA91-F7D4-4299-A727-14772C7AF827Q37617946-DC3DB51C-340C-4319-890F-5DF60AECB3BEQ37767065-CEDF3565-5356-48A1-9AC3-538D0AA99512Q41044009-4B37D448-EDD0-4FAE-B7D9-C7CB91DD3776Q55059374-1BAC7B81-53D1-44F8-B8A4-6EE36FB75937
P2860
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
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2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
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name
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@ast
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@en
type
label
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@ast
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@en
prefLabel
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@ast
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@en
P50
P356
P1433
P1476
Abp1p and Fyn SH3 domains fold through similar low-populated intermediate states.
@en
P2093
Alan R Davidson
Dmitry M Korzhnev
P304
10175-10183
P356
10.1021/BI0611560
P407
P577
2006-08-01T00:00:00Z