Statistical mechanics of simple models of protein folding and design.
about
Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.Statistical significance of protein structure prediction by threading.Improved recognition of native-like protein structures using a family of designed sequencesProtein topology and stability define the space of allowed sequences.Sequence variations within protein families are linearly related to structural variations.Imprint of evolution on protein structures.Comparing folding codes in simple heteropolymer models of protein evolutionary landscape: robustness of the superfunnel paradigm.Evolution, energy landscapes and the paradoxes of protein folding.Fast optimization of statistical potentials for structurally constrained phylogenetic models.Buffed energy landscapes: another solution to the kinetic paradoxes of protein folding.Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregationCoevolutionary information, protein folding landscapes, and the thermodynamics of natural selection.Folding Trp-cage to NMR resolution native structure using a coarse-grained protein modelOn the role of frustration in the energy landscapes of allosteric proteins.Protein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.Folding protein models with a simple hydrophobic energy function: the fundamental importance of monomer inside/outside segregation.Evaluating and optimizing computational protein design force fields using fixed composition-based negative designConnecting the Sequence-Space of Bacterial Signaling Proteins to Phenotypes Using Coevolutionary Landscapes.Thoroughly sampling sequence space: large-scale protein design of structural ensembles.Biomolecular information gained through in vitro evolution.Massively parallel sampling of lattice proteins reveals foundations of thermal adaptation.The twilight zone between protein order and disorderEvolution of functionality in lattice proteins.Optimising minimal building blocks for addressable self-assembly.Information and redundancy in the burial folding code of globular proteins within a wide range of shapes and sizes.Freezing and folding behavior in simple off-lattice heteropolymers.Coarse-grained lattice model for investigating the role of cooperativity in molecular recognition.Random sequences with power-law correlations exhibit proteinlike behavior.Random heteropolymer dynamics.Folding Lennard-Jones proteins by a contact potential.Unlocking of interlocked heteropolymer gel by light: photoinduced volume phase transition in an ionic liquid from a metastable state to an equilibrium phase.Designing specificity of protein-substrate interactionsDesigning refoldable model moleculesEnergetic Components of Cooperative Protein Folding
P2860
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P2860
Statistical mechanics of simple models of protein folding and design.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Statistical mechanics of simple models of protein folding and design.
@en
type
label
Statistical mechanics of simple models of protein folding and design.
@en
prefLabel
Statistical mechanics of simple models of protein folding and design.
@en
P2093
P2860
P921
P1433
P1476
Statistical mechanics of simple models of protein folding and design.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(97)78345-0
P407
P577
1997-12-01T00:00:00Z