about
The effect of tryptophanyl substitution on folding and structure of myoglobin.Photolytic Cross-Linking to Probe Protein-Protein and Protein-Matrix Interactions in Lyophilized PowdersExperimental evaluation of topological parameters determining protein-folding rates.Primary folding dynamics of sperm whale apomyoglobin: core formationCollapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.One-dimensional barrier-preserving free-energy projections of a beta-sheet miniprotein: new insights into the folding process.Tryptophanyl substitutions in apomyoglobin determine protein aggregation and amyloid-like fibril formation at physiological pH.Diffusion-collision model study of misfolding in a four-helix bundle protein.Photolytic labeling to probe molecular interactions in lyophilized powders.Hydrogen bond networks determine emergent mechanical and thermodynamic properties across a protein familyDynamics of the minimally frustrated helices determine the hierarchical folding of small helical proteins.Common folding processes of mini-proteins: Partial formations of secondary structures initiate the immediate protein folding.
P2860
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P2860
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
The early folding kinetics of apomyoglobin.
@en
The early folding kinetics of apomyoglobin.
@nl
type
label
The early folding kinetics of apomyoglobin.
@en
The early folding kinetics of apomyoglobin.
@nl
prefLabel
The early folding kinetics of apomyoglobin.
@en
The early folding kinetics of apomyoglobin.
@nl
P2860
P356
P1433
P1476
The early folding kinetics of apomyoglobin.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560070229
P577
1998-02-01T00:00:00Z