about
Unfolded-state dynamics and structure of protein L characterized by simulation and experimentTaming the complexity of protein foldingFast protein folding kineticsProtein folded states are kinetic hubs.Extremely slow intramolecular diffusion in unfolded protein LComplex pathways in folding of protein G explored by simulation and experiment.Microfluidic mixers for studying protein folding.Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state.Direct observation of downhill folding of lambda-repressor in a microfluidic mixer.How, when and why proteins collapse: the relation to folding.How cooperative are protein folding and unfolding transitions?Ultrafast microfluidic mixer with three-dimensional flow focusing for studies of biochemical kinetics.Right- and left-handed three-helix proteins. II. Similarity and differences in mechanical unfolding of proteins.Site-specific time-resolved FRET reveals local variations in the unfolding mechanism in an apparently two-state protein unfolding transition.Equilibrium and nonequilibrium effects in the collapse of a model polypeptide.
P2860
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P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Ruggedness in the folding landscape of protein L.
@en
Ruggedness in the folding landscape of protein L.
@nl
type
label
Ruggedness in the folding landscape of protein L.
@en
Ruggedness in the folding landscape of protein L.
@nl
prefLabel
Ruggedness in the folding landscape of protein L.
@en
Ruggedness in the folding landscape of protein L.
@nl
P2093
P2860
P50
P356
P1476
Ruggedness in the folding landscape of protein L.
@en
P2093
Lisa J Lapidus
Marcus Jäger
Michaela Kopka
Olgica Bakajin
Steven A Waldauer
Terry Ball
Vijay R Singh
William J Wedemeyer
Yujie Chen
P2860
P304
P356
10.2976/1.3013702
P577
2008-11-14T00:00:00Z