Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.
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Mechanism of prion propagation: amyloid growth occurs by monomer additionSolution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritimaExamination of the folding of E. coli CspA through tryptophan substitutionsFolding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex.Cloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima.Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxideFolding simulations for proteins with diverse topologies are accessible in days with a physics-based force field and implicit solventProtein folding and unfolding on a complex energy landscape.Integrase-directed recovery of functional genes from genomic librariesWW domain folding complexity revealed by infrared spectroscopy.Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Dynamics of an ultrafast folding subdomain in the context of a larger protein fold.Nonglassy kinetics in the folding of a simple single-domain protein.The effect of context on the folding of β-hairpins.The Role of Electrostatic Interactions in Folding of β-ProteinsStructure and function of cold shock proteins in archaea.BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.Single-domain antibody fragments with high conformational stability.Dynameomics: a consensus view of the protein unfolding/folding transition state ensemble across a diverse set of protein folds.The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo.Identification and transcriptional control of Caulobacter crescentus genes encoding proteins containing a cold shock domain.WW: An isolated three-stranded antiparallel beta-sheet domain that unfolds and refolds reversibly; evidence for a structured hydrophobic cluster in urea and GdnHCl and a disordered thermal unfolded stateUrea impedes the hydrophobic collapse of partially unfolded proteinsContact order revisited: influence of protein size on the folding rate.Is there an en route folding intermediate for Cold shock proteins?Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA.Role of a solvent-exposed aromatic cluster in the folding of Escherichia coli CspA.The entropic nature of protein thermal stabilization.Correspondence between anomalous m- and DeltaCp-values in protein folding.Heat stable ssDNA/RNA-binding activity of a wheat cold shock domain protein.
P2860
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P2860
Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.
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
Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.
@en
type
label
Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.
@en
prefLabel
Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.
@en
P2093
P2860
P356
P1433
P1476
Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA.
@en
P2093
B J Hillier
H M Rodriguez
L M Gregoret
P2860
P304
P356
10.1002/PRO.5560070228
P577
1998-02-01T00:00:00Z