Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: insights from the quasi-chemical approximation.
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Optimization to low temperature activity in psychrophilic enzymesAn Unstable Head–Rod Junction May Promote Folding into the Compact Off-State Conformation of Regulated MyosinsThe backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homologImplications of aromatic-aromatic interactions: From protein structures to peptide modelsStructural features determining thermal adaptation of esterases.Molecular modelling of the mass density of single proteins.Molecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutationsComparative proteome analysis of psychrophilic versus mesophilic bacterial species: Insights into the molecular basis of cold adaptation of proteinsReduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes.Engineering a large protein by combined rational and random approaches: stabilizing the Clostridium thermocellum cellobiose phosphorylase.Computational tools for rational protein engineering of aldolases.Constraints imposed by non-functional protein-protein interactions on gene expression and proteome size.Psychrophilic enzymes: from folding to function and biotechnology.In Silico Analysis of β-Galactosidases Primary and Secondary Structure in relation to Temperature Adaptation.Thermal compaction of the intrinsically disordered protein tau: entropic, structural, and hydrophobic factors.Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?Unfolding thermodynamics of cysteine-rich proteins and molecular thermal-adaptation of marine ciliates.Massively parallel sampling of lattice proteins reveals foundations of thermal adaptation.Improvement of Bacillus circulans beta-amylase activity attained using the ancestral mutation method.Thermophilic adaptation in prokaryotes is constrained by metabolic costs of proteostasis.Biosynthetic energy cost of potentially highly expressed proteins vary with niche in selected actinobacteria.Stabilizing HIV-1 envelope glycoprotein trimers to induce neutralizing antibodies
P2860
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P2860
Amino-acid interactions in psychrophiles, mesophiles, thermophiles, and hyperthermophiles: insights from the quasi-chemical approximation.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Amino-acid interactions in psy ...... quasi-chemical approximation.
@ast
Amino-acid interactions in psy ...... quasi-chemical approximation.
@en
type
label
Amino-acid interactions in psy ...... quasi-chemical approximation.
@ast
Amino-acid interactions in psy ...... quasi-chemical approximation.
@en
prefLabel
Amino-acid interactions in psy ...... quasi-chemical approximation.
@ast
Amino-acid interactions in psy ...... quasi-chemical approximation.
@en
P2860
P356
P1433
P1476
Amino-acid interactions in psy ...... quasi-chemical approximation.
@en
P2093
Richard A Goldstein
P2860
P304
P356
10.1110/PS.072947007
P577
2007-09-01T00:00:00Z