about
Comparing folding codes in simple heteropolymer models of protein evolutionary landscape: robustness of the superfunnel paradigm.Structural determinants of the rate of protein evolution in yeast.Distribution of genotype network sizes in sequence-to-structure genotype-phenotype maps.Cotranslational protein folding and terminus hydrophobicity.Evolutionary dynamics on protein bi-stability landscapes can potentially resolve adaptive conflicts.Information content of molecular structures.Biophysics of protein evolution and evolutionary protein biophysicsAn information theoretic approach to macromolecular modeling: II. Force fieldsPredicting the tolerance of proteins to random amino acid substitution.SELECTIVE ADVANTAGE OF RECOMBINATION IN EVOLVING PROTEIN POPULATIONS: A LATTICE MODEL STUDY.The amino acid alphabet and the architecture of the protein sequence-structure map. I. Binary alphabetsExhaustive Analysis of a Genotype Space Comprising 10(15 )Central Carbon Metabolisms Reveals an Organization Conducive to Metabolic Innovation.A comparison of genotype-phenotype maps for RNA and proteinsGenetic Correlations Greatly Increase Mutational Robustness and Can Both Reduce and Enhance Evolvability.Comparative modeling and protein-like features of hydrophobic-polar models on a two-dimensional lattice.Funnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution.A tractable genotype-phenotype map modelling the self-assembly of protein quaternary structure.On hydrophobicity and conformational specificity in proteins.The twilight zone between protein order and disorderFoldamer hypothesis for the growth and sequence differentiation of prebiotic polymersShape-dependent designability studies of lattice proteins.The role of protein homochirality in shaping the energy landscape of folding.Adaptive multiscapes: an up-to-date metaphor to visualize molecular adaptation.Classifying proteinlike sequences in arbitrary lattice protein models using LatPack.How Many Protein Sequences Fold to a Given Structure? A Coevolutionary Analysis.Adding levels of complexity enhances robustness and evolvability in a multilevel genotype-phenotype map.Simple model of pH-induced protein denaturation.Coupled folding-binding versus docking: a lattice model study.Exploring protein's optimal HP configurations by self-organizing mapping.Multicanonical chain-growth algorithm.On the networked architecture of genotype spaces and its critical effects on molecular evolution
P2860
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P2860
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Enumerating Designing Sequences in the HP Model
@en
Enumerating Designing Sequences in the HP Model
@nl
type
label
Enumerating Designing Sequences in the HP Model
@en
Enumerating Designing Sequences in the HP Model
@nl
prefLabel
Enumerating Designing Sequences in the HP Model
@en
Enumerating Designing Sequences in the HP Model
@nl
P2860
P356
P1476
Enumerating Designing Sequences in the HP Model
@en
P2093
Anders Irbäck
Carl Troein
P2860
P2888
P356
10.1023/A:1016225010659
P577
2002-03-01T00:00:00Z
P5875
P6179
1039100078