about
The interactome: Predicting the protein-protein interactions in cellsContribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1Crystal Structure of a"Nonfoldable"Insulin: IMPAIRED FOLDING EFFICIENCY DESPITE NATIVE ACTIVITYNMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiationCombining structural modeling with ensemble machine learning to accurately predict protein fold stability and binding affinity effects upon mutationThe identification of conserved interactions within the SH3 domain by alignment of sequences and structures.Structural events during the refolding of an all beta-sheet protein.A theoretical search for folding/unfolding nuclei in three-dimensional protein structuresConserved key amino acid positions (CKAAPs) derived from the analysis of common substructures in proteins.Persistently conserved positions in structurally similar, sequence dissimilar proteins: roles in preserving protein fold and function.Imprint of evolution on protein structures.Prediction of protein structural features from sequence data based on Shannon entropy and Kolmogorov complexity.Fold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Comparison of translation loads for standard and alternative genetic codesA protein evolution model with independent sites that reproduces site-specific amino acid distributions from the Protein Data Bank.A first-principles model of early evolution: emergence of gene families, species, and preferred protein folds.Mutation bias favors protein folding stability in the evolution of small populationsSearching for "downhill scenarios" in protein folding.Towards understanding the mechanisms of molecular recognition by computer simulations of ligand-protein interactions.Deciphering the hidden informational content of protein sequences: foldability of proinsulin hinges on a flexible arm that is dispensable in the mature hormoneSequence evolution and the mechanism of protein foldingStability and the evolvability of function in a model proteinThe influence of selection for protein stability on dN/dS estimationsFractal globules: a new approach to artificial molecular machinesIdentification of the minimal protein-folding nucleus through loop-entropy perturbationsComparative modeling and protein-like features of hydrophobic-polar models on a two-dimensional lattice.Robust protein protein interactions in crowded cellular environments.Packing regularities in biological structures relate to their dynamics.Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.Solvent-amino acid interaction energies in three-dimensional-lattice Monte Carlo simulations of a model 27-mer protein: Folding thermodynamics and kineticsDiabetes mellitus due to the toxic misfolding of proinsulin variants.Uncovering the properties of energy-weighted conformation space networks with a hydrophobic-hydrophilic modelFunnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution.Origination of the Protein Fold Repertoire from Oily Pluripotent Peptides.Detecting selection on protein stability through statistical mechanical models of folding and evolutionEarly Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.Maximum-Likelihood Phylogenetic Inference with Selection on Protein Folding Stability.Protein sequence entropy is closely related to packing density and hydrophobicity.An implicit solvent coarse-grained lipid model with correct stress profile.Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module.
P2860
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P2860
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
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
name
How evolution makes proteins fold quickly
@ast
How evolution makes proteins fold quickly
@en
type
label
How evolution makes proteins fold quickly
@ast
How evolution makes proteins fold quickly
@en
prefLabel
How evolution makes proteins fold quickly
@ast
How evolution makes proteins fold quickly
@en
P2093
P2860
P356
P1476
How evolution makes proteins fold quickly
@en
P2093
E I Shakhnovich
V I Abkevich
P2860
P304
P356
10.1073/PNAS.95.9.4976
P407
P577
1998-04-01T00:00:00Z