Peptide conformer acidity analysis of protein flexibility monitored by hydrogen exchange.
about
Analysing the visible conformational substates of the FK506-binding protein FKBP12Coarse-Grained Conformational Sampling of Protein Structure Improves the Fit to Experimental Hydrogen-Exchange Data.Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.Protein dynamics viewed by hydrogen exchange.Assessing the native state conformational distribution of ubiquitin by peptide acidityExperimentally assessing molecular dynamics sampling of the protein native state conformational distribution.Protein hydrogen exchange: testing current modelsAssessing the chemical accuracy of protein structures via peptide acidity.Simulated Isotope Exchange Patterns Enable Protein Structure Determination.Ensembles of a small number of conformations with relative populations.
P2860
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P2860
Peptide conformer acidity analysis of protein flexibility monitored by hydrogen exchange.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Peptide conformer acidity analysis of protein flexibility monitored by hydrogen exchange.
@en
type
label
Peptide conformer acidity analysis of protein flexibility monitored by hydrogen exchange.
@en
prefLabel
Peptide conformer acidity analysis of protein flexibility monitored by hydrogen exchange.
@en
P2093
P2860
P356
P1433
P1476
Peptide conformer acidity analysis of protein flexibility monitored by hydrogen exchange.
@en
P2093
David M LeMaster
Griselda Hernández
Janet S Anderson
P2860
P304
P356
10.1021/BI901219X
P407
P577
2009-10-01T00:00:00Z