Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains.
about
A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressionsImproved prediction of protein side-chain conformations with SCWRL4Computational design of Candida boidinii xylose reductase for altered cofactor specificityStructures of N-termini of helices in proteinsComputational methods in drug discoveryComputational design and experimental study of tighter binding peptides to an inactivated mutant of HIV-1 proteaseGetting specificity from simplicity in putative proteins from the prebiotic EarthRosetta in CASP4: progress in ab initio protein structure predictionStructural Studies of the HIV-1 Integrase Protein: Compound Screening and Characterization of a DNA-Binding InhibitorAutoDockFR: Advances in Protein-Ligand Docking with Explicitly Specified Binding Site FlexibilityA graph-theory algorithm for rapid protein side-chain predictionPhysics-based method to validate and repair flaws in protein structuresDe novo design of helical bundles as models for understanding protein folding and function.New insights into the interdependence between amino acid stereochemistry and protein structureProtein side-chain modeling with a protein-dependent optimized rotamer library.Predicting the side-chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models.3d interaction homology: The structurally known rotamers of tyrosine derive from a surprisingly limited set of information-rich hydropathic interaction environments described by maps.Constant time clash detection in protein folding.Equilibrium transitions between side-chain conformations in leucine and isoleucine.PROTDES: CHARMM toolbox for computational protein design.Conformation dependence of backbone geometry in proteins.Fine grained sampling of residue characteristics using molecular dynamics simulation.Integration of Diverse Research Methods to Analyze and Engineer Ca-Binding Proteins: From Prediction to ProductionA quality metric for homology modeling: the H-factor.Uncluttered Single-Image Visualization of Vascular Structures Using GPU and Integer ProgrammingA protein-dependent side-chain rotamer library.Computational method to reduce the search space for directed protein evolution.Factors governing loss and rescue of DNA binding upon single and double mutations in the p53 core domain.A fast method for predicting amino acid mutations that lead to unfolding.A stochastic algorithm for global optimization and for best populations: a test case of side chains in proteins.Role of cysteine residues in structural stability and function of a transmembrane helix bundle.New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.Asparagine and glutamine rotamers: B-factor cutoff and correction of amide flips yield distinct clusteringExtending Iterative Protein Redesign and Optimization (IPRO) in protein library design for ligand specificity.Structural principles for computational and de novo design of 4Fe-4S metalloproteins.Application of evolutionary algorithm methods to polypeptide folding: comparison with experimental results for unsolvated Ac-(Ala-Gly-Gly)5-LysH+Differences in hydration structure near hydrophobic and hydrophilic amino acids.SIDEpro: a novel machine learning approach for the fast and accurate prediction of side-chain conformations.Hotspot-centric de novo design of protein binders.Exploration of the structural features defining the conduction properties of a synthetic ion channel.
P2860
Q24610334-8FD38C9B-010C-47D7-968A-59DDA26393CAQ24634442-8D082C17-502F-4919-9F50-D7D3969D9FB5Q24647217-F0251920-CB61-4EB8-A97C-1458D5878F6DQ24673742-7F8D4CDE-6778-4D5E-A1CE-1DFB7D5B9F47Q26997089-A347CC8F-4963-476A-BCD4-E8CD33D2247CQ27647665-B8F754D3-5422-4134-A639-CF153A129CECQ27648142-EA51AD37-4466-44B6-9170-429CD391E58EQ28218074-4299BEAB-6A5E-4C2F-B438-4E248C9A0685Q28547968-9966A836-6813-4F39-B23F-B8EE7BCB8389Q28551247-8E935B36-5316-4E1E-A73F-C89A45FF71D0Q29619249-AEEABEB8-B5D1-4BF2-8FA8-7A01C6922F38Q29863696-3A583C6B-CED1-41E0-87A7-894DEB7C7394Q30327505-9D171919-BF31-4714-BD5D-1D7827EE29A2Q30355923-4B0411D5-08F4-44C3-B2A9-C7EEB0A07D7DQ30360147-7E5DFAF3-7752-420E-A977-CE52EF22901EQ30363422-8B3382B6-E3BE-4324-9FD9-9F9F1A046CB3Q30374011-BBB41214-643A-43DF-BD5D-8CB4C818761DQ30375011-B81AF64F-CF31-446B-A059-56238E64E940Q30375057-1434F50C-AFED-4EDB-9134-0C52DDDD695EQ30378590-286B2529-6070-4E35-ADDF-A655F25431B3Q30381729-2B958465-D8BC-4138-9FEF-EB9DC34D3AC3Q30391276-2BAC4C85-FCF0-441C-901F-FC687698EF5AQ30393133-4FCDFA06-8FF4-4806-8D66-A65497433A6FQ30399307-79B2AC3B-F038-4DC8-A6ED-9205290EC0F8Q30412362-5110FB12-9E7B-49A0-BA47-0452CD91D433Q30413617-E4355FE6-6045-4281-897F-D355A63F998CQ30660873-B812FA69-1603-4939-87D7-7C826C5F782CQ30682940-7B12323E-15A0-4D36-9CDF-3378313F2E55Q30704432-A29ED163-420D-47DD-B583-D153FB862DD8Q30797846-7C9F526F-CBEE-4431-B85B-DD93EB25BED2Q30998001-565AA144-92D8-44CD-A013-427A31F8B3FEQ31035956-9C46155D-6E0C-4EE0-AC09-8C4CF0BFB1FDQ31932109-AA3099B2-2C1B-405D-BF80-CA558210D8F1Q33268494-4ECA6D1B-2E72-4375-9F80-836400D794ADQ33558989-766FE247-3FAA-44B4-82CD-3875BC4BF8FBQ33903982-08A7B2B7-7DBD-461C-9ED9-B34ABE06149FQ33907640-E9C2AA05-91C1-4551-A40A-32BBA71F764BQ34071261-964D05C4-066D-4960-AAD1-28DEA93DB93DQ34087555-EDF5927F-7571-423D-AEDB-1EC929C7D48BQ34169778-0F2EE5D7-A727-4717-8F98-F76427AC827C
P2860
Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains.
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Conformational analysis of the ...... erences of protein sidechains.
@ast
Conformational analysis of the ...... erences of protein sidechains.
@en
Conformational analysis of the ...... erences of protein sidechains.
@nl
type
label
Conformational analysis of the ...... erences of protein sidechains.
@ast
Conformational analysis of the ...... erences of protein sidechains.
@en
Conformational analysis of the ...... erences of protein sidechains.
@nl
prefLabel
Conformational analysis of the ...... erences of protein sidechains.
@ast
Conformational analysis of the ...... erences of protein sidechains.
@en
Conformational analysis of the ...... erences of protein sidechains.
@nl
P2860
P356
P1476
Conformational analysis of the ...... erences of protein sidechains.
@en
P2093
P2860
P304
P356
10.1038/NSB0594-334
P577
1994-05-01T00:00:00Z