Protein folding pathways of adenylate kinase from E. coli: hydrostatic pressure and stopped-flow studies.
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Watching proteins fold one molecule at a timeStructural dynamics of bio-macromolecules by NMR: the slowly relaxing local structure approachIn the multi-domain protein adenylate kinase, domain insertion facilitates cooperative folding while accommodating function at domain interfaces.Protein folding studied by single-molecule FRET.
P2860
Protein folding pathways of adenylate kinase from E. coli: hydrostatic pressure and stopped-flow studies.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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name
Protein folding pathways of ad ...... sure and stopped-flow studies.
@en
Protein folding pathways of ad ...... sure and stopped-flow studies.
@nl
type
label
Protein folding pathways of ad ...... sure and stopped-flow studies.
@en
Protein folding pathways of ad ...... sure and stopped-flow studies.
@nl
prefLabel
Protein folding pathways of ad ...... sure and stopped-flow studies.
@en
Protein folding pathways of ad ...... sure and stopped-flow studies.
@nl
P2093
P356
P1433
P1476
Protein folding pathways of ad ...... sure and stopped-flow studies.
@en
P2093
P304
14706-14714
P356
10.1021/BI010308I
P407
P577
2001-12-01T00:00:00Z