Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.
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Deciphering Modern Glucocorticoid Cross-pharmacology Using Ancestral Corticosteroid ReceptorsBridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59Phenotypic comparisons of consensus variants versus laboratory resurrections of Precambrian proteinsSelection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean LifeSingle-molecule paleoenzymology probes the chemistry of resurrected enzymesA computational-experimental approach identifies mutations that enhance surface expression of an oseltamivir-resistant influenza neuraminidase.Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability.Inferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.Role of conservative mutations in protein multi-property adaptationHighly anomalous energetics of protein cold denaturation linked to folding-unfolding kineticsBiophysics of protein evolution and evolutionary protein biophysicsEvolutionary biochemistry: revealing the historical and physical causes of protein properties.Evolutionary trend toward kinetic stability in the folding trajectory of RNases H.Irreversible denaturation of maltodextrin glucosidase studied by differential scanning calorimetry, circular dichroism, and turbidity measurementsMutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history.Changing folding and binding stability in a viral coat protein: a comparison between substitutions accessible through mutation and those fixed by natural selection.In silico Evaluation of Crosslinking Effects on Denaturant m(eq) values and ΔCp upon Protein UnfoldingModulating protein stability - directed evolution strategies for improved protein function.Effect of mutations on the thermostability of Aspergillus aculeatus β-1,4-galactanase.Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis.Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53.Evidence for the principle of minimal frustration in the evolution of protein folding landscapes.Reply to Candel et al.: Evidence for evolutionary conservation of folding kinetics in the thioredoxin protein family.Fast folding and slow unfolding of a resurrected Precambrian protein.The burst-phase folding intermediate of ribonuclease H changes conformation over evolutionary history.Effects of point mutations on the thermostability of B. subtilis lipase: investigating nonadditivity.On the Potential Origins of the High Stability of Reconstructed Ancestral Proteins.Recognition between a short unstructured peptide and a partially folded fragment leads to the thioredoxin fold sharing native-like dynamics.Structure and energy based quantitative missense variant effect analysis provides insights into drug resistance mechanisms of anaplastic lymphoma kinase mutations.
P2860
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P2860
Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Natural selection for kinetic ...... rences in sequence alignments.
@en
Natural selection for kinetic ...... rences in sequence alignments.
@nl
type
label
Natural selection for kinetic ...... rences in sequence alignments.
@en
Natural selection for kinetic ...... rences in sequence alignments.
@nl
prefLabel
Natural selection for kinetic ...... rences in sequence alignments.
@en
Natural selection for kinetic ...... rences in sequence alignments.
@nl
P2093
P50
P1476
Natural selection for kinetic ...... rences in sequence alignments.
@en
P2093
Beatriz Ibarra-Molero
Fernando Ariza
Jose M Sanchez-Ruiz
P304
P356
10.1016/J.JMB.2006.07.065
P407
P577
2006-07-31T00:00:00Z