about
Teaching computers to fold proteinsFrom residue coevolution to protein conformational ensembles and functional dynamics.Phase diagrams describing fibrillization by polyalanine peptides.Spontaneous fibril formation by polyalanines; discontinuous molecular dynamics simulationsMultiscale coarse-graining of the protein energy landscapeRole of Backbone Dipole Interactions in the Formation of Secondary and Supersecondary Structures of Proteins.A coarse-grained approach to protein design: learning from design to understand folding.A structure-based method for derivation of all-atom potentials for protein foldingThe ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation.alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model.A systematically coarse-grained solvent-free model for quantitative phospholipid bilayer simulationsUnfolding of globular proteins: monte carlo dynamics of a realistic reduced model.A structural model of polyglutamine determined from a host-guest method combining experiments and landscape theory.A directed essential dynamics simulation of peptide folding.Generalized simulated tempering for exploring strong phase transitions.PRIMO: A Transferable Coarse-grained Force Field for Proteins.Recent advances in transferable coarse-grained modeling of proteins.Perspective: Coarse-grained models for biomolecular systems.Efficient Parameter Estimation of Generalizable Coarse-Grained Protein Force Fields Using Contrastive Divergence: A Maximum Likelihood Approach.Two-state folding over a weak free-energy barrier.Thermodynamics of alpha- and beta-structure formation in proteins.Coupled folding-binding in a hydrophobic/polar protein model: impact of synergistic folding and disordered flanks.The role of directional interactions in the designability of generalized heteropolymers.Hydrogen bonds, hydrophobicity forces and the character of the collapse transitionGeneric coarse-grained model for protein folding and aggregation.Solvent effects on the conformational transition of a model polyalanine peptide.Chevron behavior and isostable enthalpic barriers in protein folding: successes and limitations of simple Gō-like modeling.A multi-state coarse grained modeling approach for an intrinsically disordered peptide.Two Perturbations for Geometry Optimization of Off-lattice Bead Protein Models.The effect of surface adsorption on tertiary structure formation in helical polymers.Construction of an intermediate-resolution lattice model and re-examination of the helix-coil transition: a dynamic Monte Carlo simulation.Significance of bending restraints for the stability of helical polymer conformations.Effects of hydrophobic and dipole-dipole interactions on the conformational transitions of a model polypeptide.Folding 19 proteins to their native state and stability of large proteins from a coarse-grained model.Folding of a small helical protein using hydrogen bonds and hydrophobicity forces
P2860
Q21686181-0836C07C-5164-4DB2-A815-21109449920BQ27321788-7C0298C9-C2C5-4E05-8433-E510F7C0AE41Q28386736-8F8B3601-4D81-4B00-A91A-211802057679Q28393682-A249DA19-DA32-4EE8-B4DC-D677D244F0E1Q33619186-90DF92A1-7C80-4FF1-A6F7-3B41D3A235B3Q33739133-9D4BE135-9B74-4E57-AA94-48EB986FF3FCQ33958000-35D1A5FA-9DAA-49F3-8FDD-B5E3665EA389Q34024626-DDBADA1E-CC5C-4541-B215-6204C08FDA4EQ34037348-70A4A035-6E27-449E-9836-CB2AC0363C98Q34084053-C893A79E-366F-4A75-8F30-80B487EEF6B3Q34085742-1A246869-38E7-43E5-841B-7279B57BE0D1Q34183629-0CA8123C-7C91-401A-AF3B-DE758C00EB8DQ34187126-D442647C-5077-4B37-837F-3DCAA73D6EDBQ34190165-CDA36E25-A190-40D9-A5E1-16D30164EA0DQ34279694-E2160B15-D486-4814-A44D-1F978BDA37CBQ37127872-603DC13A-28A5-4C32-8251-84A66157EDC6Q37721126-99C68D2E-803F-47F9-B125-50E247457080Q38136697-49DBA69F-03C2-40FC-83E1-8BEB3AFD7C67Q38526771-3733B193-C473-4490-A785-E993A2E840AFQ40251257-362BE06B-1038-41EC-8236-53FAEE700044Q40251298-A1832EB4-33C4-43A5-9F84-FE595EF41F96Q40929494-82585502-FB23-48D7-A6C2-5AC22B00B5E0Q40973968-33C29AC2-79DF-421D-814D-847BC228923EQ41833620-D8D4495F-065A-4C38-BF54-D5D3843D68D2Q41906347-82FD45AF-4C9A-4CEC-9D1E-F26835B92B22Q42037889-E172281A-FDA8-4491-8CD0-90E63F29EF69Q42090270-AD8B53ED-3AD3-463C-9737-D86866C115C5Q47697536-35D29569-B7D3-4EC5-903C-432D45191715Q47868654-F6D0D444-DF2D-4AE0-A1FE-1651D78AA8C0Q47920788-FEB7B0DF-445C-47F0-94CE-1CA5349DCD36Q50927969-7E33F243-F4E5-4E4C-926A-BC64A3F794E3Q51642157-4FF92DDE-86C9-4032-80C1-262F0B377129Q53027596-0E6F97FC-3B6A-4950-AAC9-2EC4DC77527EQ54784061-23D559BE-E51F-45A2-9D6E-0BB55D765423Q57953582-D791DA67-8937-4390-9F1E-D98947C3C774
P2860
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
Three-helix-bundle protein in a Ramachandran model.
@ast
Three-helix-bundle protein in a Ramachandran model.
@en
type
label
Three-helix-bundle protein in a Ramachandran model.
@ast
Three-helix-bundle protein in a Ramachandran model.
@en
prefLabel
Three-helix-bundle protein in a Ramachandran model.
@ast
Three-helix-bundle protein in a Ramachandran model.
@en
P2093
P2860
P356
P1476
Three-helix-bundle protein in a Ramachandran model.
@en
P2093
P2860
P304
13614-13618
P356
10.1073/PNAS.240245297
P407
P577
2000-12-01T00:00:00Z
P5875
P698
P818
cond-mat/0011079