A statistical mechanical method to optimize energy functions for protein folding.
about
Teaching computers to fold proteinsReductive genome evolution in Buchnera aphidicolaStatistical potential for assessment and prediction of protein structuresOptimized distance-dependent atom-pair-based potential DOOP for protein structure prediction.Statistical potentials for improved structurally constrained evolutionary models.Protein side chain modeling with orientation-dependent atomic force fields derived by series expansionsStatistical mechanics-based method to extract atomic distance-dependent potentials from protein structures.Distance dependency and minimum amino acid alphabets for decoy scoring potentials.How to guarantee optimal stability for most representative structures in the Protein Data Bank.Molecular and Functional Bases of Selection against a Mutation Bias in an RNA Virus.On simplified global nonlinear function for fitness landscape: a case study of inverse protein folding.Statistical potential for modeling and ranking of protein-ligand interactionsWhy should we care about molecular coevolution?Detecting selection on protein stability through statistical mechanical models of folding and evolutiontoyLIFE: a computational framework to study the multi-level organisation of the genotype-phenotype map.Assessment of the quality of energy functions for protein folding by using a criterion derived with the help of the noisy go model.Substitution rates predicted by stability-constrained models of protein evolution are not consistent with empirical data.A new parameter-rich structure-aware mechanistic model for amino acid substitution during evolution.Sequence determinants of protein folding rates: positive correlation between contact energy and contact range indicates selection for fast folding.Recurrent oligomers in proteins: an optimal scheme reconciling accurate and concise backbone representations in automated folding and design studies.Lack of self-averaging in neutral evolution of proteinsInfluence of mutation bias and hydrophobicity on the substitution rates and sequence entropies of protein evolutionFolding of a small helical protein using hydrogen bonds and hydrophobicity forces
P2860
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P2860
A statistical mechanical method to optimize energy functions for protein folding.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
A statistical mechanical method to optimize energy functions for protein folding.
@ast
A statistical mechanical method to optimize energy functions for protein folding.
@en
type
label
A statistical mechanical method to optimize energy functions for protein folding.
@ast
A statistical mechanical method to optimize energy functions for protein folding.
@en
prefLabel
A statistical mechanical method to optimize energy functions for protein folding.
@ast
A statistical mechanical method to optimize energy functions for protein folding.
@en
P2093
P2860
P356
P1476
A statistical mechanical method to optimize energy functions for protein folding.
@en
P2093
Bastolla U
Vendruscolo M
P2860
P304
P356
10.1073/PNAS.97.8.3977
P407
P577
2000-04-01T00:00:00Z