10 residue folded peptide designed by segment statistics.
about
Optimizing pH Response of Affinity between Protein G and IgG Fc: HOW ELECTROSTATIC MODULATIONS AFFECT PROTEIN-PROTEIN INTERACTIONSTracing Primordial Protein Evolution through Structurally Guided Stepwise Segment Elongationβ-hairpin forms by rolling up from C-terminal: topological guidance of early folding dynamicsFixman compensating potential for general branched moleculesProtein thermodynamics can be predicted directly from biological growth ratesAn undergraduate laboratory activity on molecular dynamics simulationsA segment of cold shock protein directs the folding of a combinatorial protein.Structural diversity of protein segments follows a power-law distributionFF12MC: A revised AMBER forcefield and new protein simulation protocol.Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in waterPopulation based reweighting of scaled molecular dynamicsReversible folding simulation by hybrid Hamiltonian replica exchange.Secondary structure propensities in peptide folding simulations: a systematic comparison of molecular mechanics interaction schemes.Stabilizing capping motif for beta-hairpins and sheets.A combined effective fragment potential-fragment molecular orbital method. II. Analytic gradient and application to the geometry optimization of solvated tetraglycine and chignolin.Engineered protein A ligands, derived from a histidine-scanning library, facilitate the affinity purification of IgG under mild acidic conditions.An accurate density functional theory based estimation of pK(a) values of polar residues combined with experimental data: from amino acids to minimal proteins.Universality of thermodynamic constants governing biological growth rates.Temperature and pressure denaturation of chignolin: folding and unfolding simulation by multibaric-multithermal molecular dynamics method.Raising the speed limit for β-hairpin formation.Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Speed of conformational change: comparing explicit and implicit solvent molecular dynamics simulationsShaping up the protein folding funnel by local interaction: lesson from a structure prediction study.Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein AssociationFurther along the Road Less Traveled: AMBER ff15ipq, an Original Protein Force Field Built on a Self-Consistent Physical ModelConvergent evolution in structural elements of proteins investigated using cross profile analysis.Multiple Simulated Annealing-Molecular Dynamics (MSA-MD) for Conformational Space Search of Peptide and Miniprotein.De novo structure prediction and experimental characterization of folded peptoid oligomers.Mutational effects on the folding dynamics of a minimized hairpin.A Miniature Protein Stabilized by a Cation-π Interaction NetworkVery short peptides with stable folds: building on the interrelationship of Trp/Trp, Trp/cation, and Trp/backbone-amide interaction geometries.Use of multiple picosecond high-mass molecular dynamics simulations to predict crystallographic B-factors of folded globular proteins.TIGER2: an improved algorithm for temperature intervals with global exchange of replicas.Exploring energy landscapes: from molecular to mesoscopic systems.Minimization and optimization of designed beta-hairpin foldsSimple, yet powerful methodologies for conformational sampling of proteins.ff14ipq: A Self-Consistent Force Field for Condensed-Phase Simulations of Proteins.Optimized parameter selection reveals trends in Markov state models for protein folding.Transform and relax sampling for highly anisotropic systems: application to protein domain motion and folding.WExplore: hierarchical exploration of high-dimensional spaces using the weighted ensemble algorithm.
P2860
Q27654036-2EF73903-BFD5-4825-AAF0-068A87DCA874Q27680977-2D3B92B7-A19B-4862-96FA-71BB186F5FE8Q28274906-67533C3D-BB10-40E1-B6C9-F64223AB06CBQ28394097-C26564A9-4AFA-44ED-9D83-5C241A7B60B7Q28538355-9A2F871C-27FC-44FA-B1D7-854FE7B3E209Q29575450-FD88AD0C-7D2E-4C7A-ABDB-666A9BF255A5Q30160341-83ADF648-F32B-450C-988E-7999DFB8EDABQ30354608-E9A3A02A-11E2-4E79-8DC0-6D6D3E320DB3Q30389832-EECED008-8EF6-456F-B90E-ED73C78D9221Q30487379-72836E5A-6308-47C2-BD86-5214AE29D074Q30554344-E4AA41D8-4FDE-4B2E-AB4E-9B0992189509Q31154801-CB6EA65A-0178-4D1B-9144-7D0F278FEF8EQ33484480-446532DB-6528-4F9D-A932-3C3F31ED93FEQ33581868-AC42420C-B602-402A-9747-4D672A9EC28AQ33801447-B98CA78C-7E1D-4DE0-B5B5-C1917EC050EAQ33936317-5CD00061-FDBE-4149-950A-F4243CE377A0Q34159924-70467712-B848-4053-9FDD-2DD479B36CE0Q34163806-5A54EB13-72FF-46A7-836C-9632B8D7BDC3Q34284914-0E6F5407-CEBC-46CE-A7FC-C4F0C6135E21Q34371064-98042C56-E14A-4624-95AE-C360F4695E0CQ34457824-CCDB9DA2-E669-47CD-8D87-C79F0FCC55F3Q34466761-055CC5D9-C449-4E6A-A027-8F87703CB2A0Q34480062-009C87FB-69CD-4431-86C1-30747F9F9324Q34503099-8A833EF9-1B1D-4F8B-9884-E68E925B3157Q36072633-1214B81E-92A8-4275-95CE-E8EDB59FEEEEQ36099122-03FC9F6F-FD33-4B41-A9BA-4B5AC26617F5Q36192601-70EB0E80-F022-45B3-AA53-5E838EA90DD8Q36221874-D49965B4-0E63-4AF4-9D9A-E52A2F18838FQ36823550-FB303742-48C7-4BC4-804C-8F44A9C1AD6AQ36901846-4944DE2E-6518-4C2E-8A8F-13DA3B578E0DQ37130581-19C8430D-AAB9-4A3B-8C0D-24FB696C3380Q37280474-133F9EAE-CDD7-4BD1-8980-2E1CFE4EADF4Q37285420-F262A1A9-42EA-480F-9B6F-FD85CD3B6F9DQ38143509-EA3ADC3F-6FA3-4C8F-A2CD-7474DBB4E9D6Q38280257-486D9963-9D59-4400-88A7-AD980AF71AEFQ38346856-35AA91C1-9B23-4BB7-BEE1-CDF26E225817Q39110778-9D97BF9B-F0A3-435A-9092-CC3BDFBBBC2AQ39162913-C80BA17B-278B-4C42-A723-A8C60A12A9D5Q39722452-7FDA3381-43AA-4445-8E3A-A3CEE811EE74Q39825374-9804C9BA-D992-4997-A861-2007F5EFE196
P2860
10 residue folded peptide designed by segment statistics.
description
2004 nî lūn-bûn
@nan
2004 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
10 residue folded peptide designed by segment statistics.
@ast
10 residue folded peptide designed by segment statistics.
@en
type
label
10 residue folded peptide designed by segment statistics.
@ast
10 residue folded peptide designed by segment statistics.
@en
prefLabel
10 residue folded peptide designed by segment statistics.
@ast
10 residue folded peptide designed by segment statistics.
@en
P1433
P1476
10 residue folded peptide designed by segment statistics
@en
P2093
Hisayuki Morii
Yoshito Sawada
P304
P356
10.1016/J.STR.2004.05.022
P577
2004-08-01T00:00:00Z