Nonnative interactions regulate folding and switching of myristoylated protein.
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The roles of conditional disorder in redox proteinsHow well does a funneled energy landscape capture the folding mechanism of spectrin domains?Quantifying the Sources of Kinetic Frustration in Folding Simulations of Small Proteins.Understanding the folding-function tradeoff in proteins.Native contact density and nonnative hydrophobic effects in the folding of bacterial immunity proteins.Protein unfolding rates correlate as strongly as folding rates with native structure.Spatial ranges of driving forces are a key determinant of protein folding cooperativity and rate diversity.Right- and left-handed three-helix proteins. I. Experimental and simulation analysis of differences in folding and structure.The low populated folding intermediate of a mutant of the Fyn SH3 domain identified by a simple model.Analyzing the effect of homogeneous frustration in protein folding.
P2860
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P2860
Nonnative interactions regulate folding and switching of myristoylated protein.
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2012 nî lūn-bûn
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2012年の論文
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2012年学术文章
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2012年学术文章
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2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
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2012年學術文章
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2012年學術文章
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name
Nonnative interactions regulate folding and switching of myristoylated protein.
@ast
Nonnative interactions regulate folding and switching of myristoylated protein.
@en
type
label
Nonnative interactions regulate folding and switching of myristoylated protein.
@ast
Nonnative interactions regulate folding and switching of myristoylated protein.
@en
prefLabel
Nonnative interactions regulate folding and switching of myristoylated protein.
@ast
Nonnative interactions regulate folding and switching of myristoylated protein.
@en
P2093
P2860
P356
P1476
Nonnative interactions regulate folding and switching of myristoylated protein.
@en
P2093
Amir Marcovitz
Aron Broom
Dalit Shental-Bechor
Duncan Mackenzie
Elizabeth M Meiering
Fadila Ghashut
Fernando Bralha
Martin T J Smith
Yaakov Levy
P2860
P304
17839-17844
P356
10.1073/PNAS.1201803109
P407
P577
2012-07-30T00:00:00Z