Determining denaturation midpoints in multiprobe equilibrium protein folding experiments.
about
Protein sectors: evolutionary units of three-dimensional structureSlow proton transfer coupled to unfolding explains the puzzling results of single-molecule experiments on BBL, a paradigmatic downhill folding proteinUnderstanding protein folding cooperativity based on topological consideration.Slowing down downhill folding: a three-probe study.Mapping fast protein folding with multiple-site fluorescent probesInteraction Networks in Protein Folding via Atomic-Resolution Experiments and Long-Time-Scale Molecular Dynamics SimulationsEvolution under Drug Pressure Remodels the Folding Free-Energy Landscape of Mature HIV-1 ProteaseCrowding effects on the small, fast-folding protein lambda6-85.Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.The effect of electrostatics on the marginal cooperativity of an ultrafast folding protein.Exploiting the downhill folding regime via experiment.A one-dimensional free energy surface does not account for two-probe folding kinetics of protein alpha(3)D.The Surface of Protein λ6-85 Can Act as a Template for Recurring Poly(ethylene glycol) Structure.
P2860
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P2860
Determining denaturation midpoints in multiprobe equilibrium protein folding experiments.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Determining denaturation midpoints in multiprobe equilibrium protein folding experiments.
@en
type
label
Determining denaturation midpoints in multiprobe equilibrium protein folding experiments.
@en
prefLabel
Determining denaturation midpoints in multiprobe equilibrium protein folding experiments.
@en
P356
P1433
P1476
Determining denaturation midpoints in multiprobe equilibrium protein folding experiments.
@en
P2093
Victor Muñoz
P304
P356
10.1021/BI800336X
P407
P577
2008-06-10T00:00:00Z