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Native protein sequences are close to optimal for their structures

Native protein sequences are close to optimal for their structures

http://www.wikidata.org/entity/Q24656322

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Computational design of a PDZ domain peptide inhibitor that rescues CFTR activity Analyzing effects of naturally occurring missense mutations Design of a Novel Globular Protein Fold with Atomic-Level Accuracy Computational enzyme design approaches with significant biological outcomes: progress and challenges Computational prediction of native protein ligand-binding and enzyme active site sequences.The 3D profile method for identifying fibril-forming segments of proteins Toward high-resolution homology modeling of antibody Fv regions and application to antibody-antigen docking A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressions Systematic analysis of helical protein interfaces reveals targets for synthetic inhibitors Improved side-chain modeling for protein-protein docking Quantification of helix-helix binding affinities in micelles and lipid bilayers High-resolution structure prediction and the crystallographic phase problem Consistent blind protein structure generation from NMR chemical shift data Homology modeling using parametric alignment ensemble generation with consensus and energy-based model selection RosettaDesign server for protein design Protein-DNA binding specificity predictions with structural models Improvement in protein functional site prediction by distinguishing structural and functional constraints on protein family evolution using computational design.Structural organization and interactions of transmembrane domains in tetraspanin proteins Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics Self-assembling protein nanoparticles in the design of vaccines Stability engineering of the human antibody repertoire Folding and Stabilization of Native-Sequence-Reversed Proteins.In silico prediction of mutant HIV-1 proteases cleaving a target sequence Rapid sampling of molecular motions with prior information constraints BCL::Fold--de novo prediction of complex and large protein topologies by assembly of secondary structure elements Conversion of monomeric protein L to an obligate dimer by computational protein design Crystal structures and increased stabilization of the protein G variants with switched folding pathways NuG1 and NuG2 Local complexity of amino acid interactions in a protein core Structure-based Protocol for Identifying Mutations that Enhance Protein–Protein Binding Affinities High-resolution design of a protein loop Computer-Based Redesign of a β Sandwich Protein Suggests that Extensive Negative Design Is Not Required for De Novo β Sheet Design A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system Alteration of enzyme specificity by computational loop remodeling and design A Correspondence Between Solution-State Dynamics of an Individual Protein and the Sequence and Conformational Diversity of its Family Structural analysis of thermostabilizing mutations of cocaine esterase Computational Design of an Enzyme Catalyst for a Stereoselective Bimolecular Diels-Alder Reaction Computational design of an endo-1,4- -xylanase ligand binding site Computational Design of the Sequence and Structure of a Protein-Binding Peptide Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation Design and Characterization of Epitope-Scaffold Immunogens That Present the Motavizumab Epitope from Respiratory Syncytial Virus

P2860

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P2860

Native protein sequences are close to optimal for their structures

http://www.wikidata.org/entity/Q24656322

description

2000 nî lūn-bûn

@nan

2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

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

name

Native protein sequences are close to optimal for their structures

@ast

Native protein sequences are close to optimal for their structures

@en

Native protein sequences are close to optimal for their structures

@nl

type

label

Native protein sequences are close to optimal for their structures

@ast

Native protein sequences are close to optimal for their structures

@en

Native protein sequences are close to optimal for their structures

@nl

prefLabel

Native protein sequences are close to optimal for their structures

@ast

Native protein sequences are close to optimal for their structures

@en

Native protein sequences are close to optimal for their structures

@nl

P1433

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P3181

P356

PNAS.97.19.10383

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Native protein sequences are close to optimal for their structures

@en

P2093

B Kuhlman

http://www.w3.org/2001/XMLSchema#string

P2860

De novo protein design: fully automated sequence selection

Design, structure and stability of a hyperthermophilic protein variant

High-resolution protein design with backbone freedom

Effective energy function for proteins in solution

Two exposed amino acid residues confer thermostability on a cold shock protein

Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes

Mutagenesis of a buried polar interaction in an SH3 domain: sequence conservation provides the best prediction of stability effects.

The HSSP database of protein structure-sequence alignments and family profiles.

Simplified proteins: minimalist solutions to the 'protein folding problem'.

Energy functions for protein design.

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10383-8

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scholarly article

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639535

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P356

10.1073/PNAS.97.19.10383

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19

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97

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12336849

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P698

10984534

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P921

protein structure

P932

27033

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