Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
about
Long-range correlation properties of coding and noncoding DNA sequences: GenBank analysis.Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: A structural clue to amyloid assemblyFolding funnels and frustration in off-lattice minimalist protein landscapes.Underlying hydrophobic sequence periodicity of protein tertiary structure.The Shannon information entropy of protein sequences.Screening for peptide drugs from the natural repertoire of biodiverse protein folds.Time-dependent ARMA modeling of genomic sequences.The distribution of CTL epitopes in HIV-1 appears to be random, and similar to that of other proteomes.An analysis of single amino acid repeats as use case for application specific background modelsDo natural proteins differ from random sequences polypeptides? Natural vs. random proteins classification using an evolutionary neural network.Simulation of biomimetic recognition between polymers and surfaces.Thermodynamic procedure to synthesize heteropolymers that can renature to recognize a given target molecule.Randomness in Sequence Evolution Increases over TimeChemical physics of protein folding.On the thermodynamic hypothesis of protein foldingA coarse-grained protein model in a water-like solvent.Self-organization and entropy reduction in a living cell.Natural protein sequences are more intrinsically disordered than random sequencesEvidence for nonrandom hydrophobicity structures in protein chains.On hydrophobicity correlations in protein chains.Statistical mechanics of simple models of protein folding and design.Information-theoretic analysis and prediction of protein atomic burials: on the search for an informational intermediate between sequence and structure.Phase diagram of random heteropolymers.Information and redundancy in the burial folding code of globular proteins within a wide range of shapes and sizes.Random sequences with power-law correlations exhibit proteinlike behavior.Clustering of protein structures using hydrophobic free energy and solvent accessibility of proteins.Multifractal and correlation analyses of protein sequences from complete genomes.On the transition coordinate for protein folding
P2860
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P2860
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
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1994年學術文章
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1994年學術文章
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name
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@ast
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@en
type
label
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@ast
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@en
prefLabel
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@ast
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@en
P2860
P356
P1476
Nonrandomness in protein sequences: evidence for a physically driven stage of evolution?
@en
P2093
P2860
P304
12972-12975
P356
10.1073/PNAS.91.26.12972
P407
P577
1994-12-01T00:00:00Z