about
The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysisImportance of Hydrophobic Cavities in Allosteric Regulation of Formylglycinamide Synthetase: Insight from Xenon Trapping and Statistical Coupling AnalysisInsights into the fold organization of TIM barrel from interaction energy based structure networksComparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display.Rapid mapping of protein structure, interactions, and ligand binding by misincorporation proton-alkyl exchange.Searching for folded proteins in vitro and in silico.Amino acid alphabet reduction preserves fold information contained in contact interactions in proteins.Combinatorial approaches to protein stability and structure.In vitro selection and characterization of a stable subdomain of phosphoribosylanthranilate isomerase.Comparative characterization of random-sequence proteins consisting of 5, 12, and 20 kinds of amino acids.Combinatorial mutagenesis to restrict amino acid usage in an enzyme to a reduced setBreaking open a protein barrelStabilizing proteins from sequence statistics: the interplay of conservation and correlation in triosephosphate isomerase stability.An active enzyme constructed from a 9-amino acid alphabet.Deciphering enzymes. Genetic selection as a probe of structure and mechanism.Fast, cheap and out of control--Insights into thermodynamic and informatic constraints on natural protein sequences from de novo protein design.Using diastereopeptides to control metal ion coordination in proteinsClusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Design of thiolate rich metal binding sites within a peptidic framework.A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.Crystal structures of two monomeric triosephosphate isomerase variants identified via a directed-evolution protocol selecting for L-arabinose isomerase activity.Flagellin glycosylation with pseudaminic acid in Campylobacter and Helicobacter: prospects for development of novel therapeutics.Pairwise contact energy statistical potentials can help to find probability of point mutations.Redesigning the type II' β-turn in green fluorescent protein to type I': implications for folding kinetics and stability.The folding pathway of glycosomal triosephosphate isomerase: structural insights into equilibrium intermediates.Structure-based directed evolution of a monomeric triosephosphate isomerase: toward a pentose sugar isomerase.Structural Frameworks Suitable for EngineeringSimplification of complexity in protein molecular systems by grouping amino acids: a view from physics
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Reverse engineering the (beta/alpha )8 barrel fold.
@ast
Reverse engineering the (beta/alpha )8 barrel fold.
@en
type
label
Reverse engineering the (beta/alpha )8 barrel fold.
@ast
Reverse engineering the (beta/alpha )8 barrel fold.
@en
prefLabel
Reverse engineering the (beta/alpha )8 barrel fold.
@ast
Reverse engineering the (beta/alpha )8 barrel fold.
@en
P2093
P2860
P356
P1476
Reverse engineering the (beta/alpha )8 barrel fold.
@en
P2093
Balakrishnan R
Harbury PB
Silverman JA
P2860
P304
P356
10.1073/PNAS.041613598
P407
P577
2001-03-01T00:00:00Z