A new approach to the design of uniquely folded thermally stable proteins.
about
Computational design of a PDZ domain peptide inhibitor that rescues CFTR activityDesign, synthesis, and characterization of a novel hemoproteinProtein thermodynamics can be predicted directly from biological growth ratesEffects of Non-Natural Amino Acid Incorporation into the Enzyme Core Region on Enzyme Structure and Function.Rotamer optimization for protein design through MAP estimation and problem-size reduction.OptGraft: A computational procedure for transferring a binding site onto an existing protein scaffold.Computational approaches for de novo design and redesign of metal-binding sites on proteinsExtending Iterative Protein Redesign and Optimization (IPRO) in protein library design for ligand specificity.Combinatorial design of protein sequences with applications to lattice and real proteins.Universality of thermodynamic constants governing biological growth rates.Designing proteins from the inside out.A critical analysis of computational protein design with sparse residue interaction graphs.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.BWM*: A Novel, Provable, Ensemble-based Dynamic Programming Algorithm for Sparse Approximations of Computational Protein Design.Expanded explorations into the optimization of an energy function for protein design.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersDevelopment of a cytokine analog with enhanced stability using computational ultrahigh throughput screeningIncreasing protein stability using a rational approach combining sequence homology and structural alignment: Stabilizing the WW domain.OSPREY Predicts Resistance Mutations Using Positive and Negative Computational Protein Design.Action-at-a-distance interactions enhance protein binding affinity.Protein aggregation determinants from a simplified model: cooperative folders resist aggregation.Genetic algorithms as a tool for helix design--computational and experimental studies on prion protein helix 1.7 Computational protein design and discovery
P2860
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P2860
A new approach to the design of uniquely folded thermally stable proteins.
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 new approach to the design of uniquely folded thermally stable proteins.
@en
A new approach to the design of uniquely folded thermally stable proteins.
@nl
type
label
A new approach to the design of uniquely folded thermally stable proteins.
@en
A new approach to the design of uniquely folded thermally stable proteins.
@nl
prefLabel
A new approach to the design of uniquely folded thermally stable proteins.
@en
A new approach to the design of uniquely folded thermally stable proteins.
@nl
P2093
P2860
P356
P1433
P1476
A new approach to the design of uniquely folded thermally stable proteins.
@en
P2093
P2860
P304
P356
10.1110/PS.9.2.403
P577
2000-02-01T00:00:00Z