The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
about
A thermodynamic ligand binding study of the third PDZ domain (PDZ3) from the mammalian neuronal protein PSD-95Hydrogen bonding in water using synthetic receptorsInteratomic potentials and solvation parameters from protein engineering data for buried residuesThermodynamic stability of wild-type and mutant p53 core domainCharacterization of protein-folding pathways by reduced-space modelingTranslating Koch's postulates to identify matrix metalloproteinase roles in postmyocardial infarction remodeling: cardiac metalloproteinase actions (CarMA) postulatesSolvation in protein folding analysis: Combination of theoretical and experimental approachesStructural Alterations within Native Amyloidogenic Immunoglobulin Light ChainsStabilising the DNA-binding domain of p53 by rational design of its hydrophobic coreStructural basis for the enhanced stability of highly fluorinated proteinsX-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamaseThermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core proteinContribution of hydrogen bonds to protein stabilityTrimeric domain-swapped barnaseA self-consistent knowledge-based approach to protein designCharacterisation of the SUMO-like domains of Schizosaccharomyces pombe Rad60Computational studies on mutant protein stability: The correlation between surface thermal expansion and protein stability.Design of highly stable functional GroEL minichaperones.Effect of protein structure on mitochondrial import.Energetics of aliphatic deletions in protein coresDesolvation and development of specific hydrophobic core packing during Im7 folding.Mathematics, thermodynamics, and modeling to address ten common misconceptions about protein structure, folding, and stability.Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.A method to rationally increase protein stability based on the charge-charge interaction, with application to lipase LipK107.Structural and dynamic properties that govern the stability of an engineered fibronectin type III domainMolecular simulations of cotranslational protein folding: fragment stabilities, folding cooperativity, and trapping in the ribosome."Hot cores" in proteins: comparative analysis of the apolar contact area in structures from hyper/thermophilic and mesophilic organisms.Betaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins.Protein thermostability calculations using alchemical free energy simulationsThe conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function.Engineering an artificial zymogen by alternate frame protein foldingDetermination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein.Hydrogen bonding stabilizes globular proteins.Determination of cancer risk associated with germ line BRCA1 missense variants by functional analysis.Conferring thermostability to mesophilic proteins through optimized electrostatic surfaces.The folding of GroEL-bound barnase as a model for chaperonin-mediated protein folding.Phi-value analysis and the nature of protein-folding transition statesSurfing on protein folding energy landscapes.Urea unfolding of peptide helices as a model for interpreting protein unfolding.
P2860
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P2860
The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
The folding of an enzyme. II. ...... eractions to protein stability
@ast
The folding of an enzyme. II. ...... eractions to protein stability
@en
The folding of an enzyme. II. ...... eractions to protein stability
@nl
type
label
The folding of an enzyme. II. ...... eractions to protein stability
@ast
The folding of an enzyme. II. ...... eractions to protein stability
@en
The folding of an enzyme. II. ...... eractions to protein stability
@nl
prefLabel
The folding of an enzyme. II. ...... eractions to protein stability
@ast
The folding of an enzyme. II. ...... eractions to protein stability
@en
The folding of an enzyme. II. ...... eractions to protein stability
@nl
P2093
P1476
The folding of an enzyme. II. ...... eractions to protein stability
@en
P2093
P304
P356
10.1016/0022-2836(92)90562-X
P407
P577
1992-04-01T00:00:00Z