Principles of protein folding--a perspective from simple exact models.
about
Directed evolution of a model primordial enzyme provides insights into the development of the genetic codeOn the characterization and software implementation of general protein lattice modelsHow are model protein structures distributed in sequence space?Thermodynamic prediction of protein neutralityCoarse-grained modeling of mucus barrier propertiesPolymer principles and protein foldingIs the molten globule a third phase of proteins?Knotted proteins: A tangled tale of Structural BiologyProtein design: toward functional metalloenzymesRelative entropy as a universal metric for multiscale errorsStructural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein foldingInterplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assemblyTheoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingA small engineered protein lacks structural uniqueness by increasing the side-chain conformational entropyWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesThe protein folding problemA self-consistent knowledge-based approach to protein designMolecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: relative stabilities in experiment and simulationsWhy reversing the sequence of the alpha domain of human metallothionein-2 does not change its metal-binding and folding characteristicsA molecular interpretation of 2D IR protein folding experiments with Markov state modelsA simple model predicts experimental folding rates and a hub-like topologyAn Improved Ant Colony Optimisation Algorithm for the 2D HP Protein Folding ProblemA minimal physically realistic protein-like lattice model: designing an energy landscape that ensures all-or-none folding to a unique native stateNon-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.Thermodynamics of protein folding: a statistical mechanical study of a small all-beta protein.Robustness of protein folding kinetics to surface hydrophobic substitutions.Folding funnels and frustration in off-lattice minimalist protein landscapes.On the polymer physics origins of protein folding thermodynamics.Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.The elastic net algorithm and protein structure prediction.Nonatomic solvent-driven Voronoi tessellation of proteins: an open tool to analyze protein folds.Comparing folding codes in simple heteropolymer models of protein evolutionary landscape: robustness of the superfunnel paradigm.Divergence, recombination and retention of functionality during protein evolution.Sequence determinants of a conformational switch in a protein structure.Proteins with highly similar native folds can show vastly dissimilar folding behavior when desolvated.Codability criterion for picking proteinlike structures from random three-dimensional configurations.Reconstructing protein structure from solvent exposure using tabu search.An effective evolutionary algorithm for protein folding on 3D FCC HP model by lattice rotation and generalized move sets.A firefly-inspired method for protein structure prediction in lattice models.Lattice model simulation of interchain protein interactions and the folding dynamics and dimerization of the GCN4 Leucine zipper.
P2860
Q21092411-635F389F-86B0-4774-8E3B-71ACA830423EQ21133612-4CE0E7D0-2E8A-4D52-879C-1A10FAEEBD88Q24532911-69FF1E09-C777-4910-B725-72223A194C4FQ24557480-BE929007-859C-4A69-8EC9-0B37BD642467Q24606537-8707E29A-464C-4DE3-B6E9-BCCD911ACE6DQ24672635-4515D3BC-84B8-4A26-AE02-9D9925FC4A4CQ24681756-95925250-447F-42F9-BB4E-E700906116A0Q26783791-A8AC709E-7AF5-474F-99AE-EE0BD1D00582Q26866201-F91EC5E8-AB8F-4C9E-8FC3-F2FF2B4A271BQ27444470-B1F87159-4130-483F-A4EB-5AFCBDB268A5Q27618349-B7121840-7F74-43AE-ADB8-D1EF7F0D4A47Q27650994-7A14A8D7-4A07-4B5D-8BC6-ED1644CBB3C2Q27651198-170411FB-5032-44F9-9AD5-A7342E72029FQ27734034-A3F15BE6-B03A-4077-9CDC-B6317A459D86Q28080003-A90AB43F-107D-4F54-80C0-38901357A7F2Q28284812-AB2FE1AE-BB25-4E52-A7CB-D0D85FE55C6EQ28346250-E4CB339D-3DD1-4F65-8AD9-A50FBBFEBFD7Q28361327-DB7304F8-1AB4-4C90-A173-13B2CAF877A2Q28646226-3C9C3CF2-2973-406F-AEE6-2B7C934015B2Q28660159-30C32B6C-5AA8-4911-98F3-99AAD4BE64E7Q28728370-861FF069-0CB7-482B-A5EC-DCAD099F05AAQ29396450-F8DCF9A2-B71B-4796-85AE-7CB8FD1985B4Q30164862-A7EB7F60-75C7-48CF-ADA6-244DB97CD06EQ30165223-3D655336-82A8-49D2-987C-DD11BA78B2FAQ30168891-00D7E53B-48DA-4FEF-9F44-DE9D2E61A5B7Q30175271-0713C347-6118-4D5C-844D-205656A54A41Q30176183-9959EB25-D8AC-451A-8FA0-BCAC71491737Q30313760-AD89C5DE-FD30-4977-A87A-BA3A3D78C106Q30323021-1237D71D-7A95-4D72-A569-39527AFA1F8BQ30330025-48418EC2-1CDA-4BB1-ACD2-2082010166BEQ30332169-C873A18E-A1F1-4A72-8A81-88C364E45366Q30344005-AA2B6E4B-EA15-438F-BFD9-FC71F43BFE1FQ30351513-E0835CEC-8EE6-4B16-A668-BDE6AF22FC25Q30352170-47C3D231-B3E5-4CD6-9A0E-DBCD9CD04AAFQ30355839-F5FB472D-4035-4907-8824-81011B95443DQ30357262-274EAF76-09D4-4286-A602-C5D1C055C0EFQ30357690-9698B93F-6474-4532-816D-CCCD80E3D3F8Q30359394-3BDA8F31-F5F2-4AE4-A233-FE77D83D7CDCQ30364027-01366D71-9686-4497-995C-2FC7949E7507Q30367572-902E2117-C8BD-4766-ADC4-F0C712B009B1
P2860
Principles of protein folding--a perspective from simple exact models.
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Principles of protein folding--a perspective from simple exact models.
@ast
Principles of protein folding--a perspective from simple exact models.
@en
type
label
Principles of protein folding--a perspective from simple exact models.
@ast
Principles of protein folding--a perspective from simple exact models.
@en
prefLabel
Principles of protein folding--a perspective from simple exact models.
@ast
Principles of protein folding--a perspective from simple exact models.
@en
P2093
P2860
P356
P1433
P1476
Principles of protein folding--a perspective from simple exact models
@en
P2093
P2860
P304
P356
10.1002/PRO.5560040401
P577
1995-04-01T00:00:00Z