Sequence-similar, structure-dissimilar protein pairs in the PDB.
about
Solving nucleic acid structures by molecular replacement: examples from group II intron studiesRedundancy-weighting for better inference of protein structural features.SSpro/ACCpro 5: almost perfect prediction of protein secondary structure and relative solvent accessibility using profiles, machine learning and structural similarity.Low complexity and disordered regions of proteins have different structural and amino acid preferences.Global distribution of conformational states derived from redundant models in the PDB points to non-uniqueness of the protein structure.FragBag, an accurate representation of protein structure, retrieves structural neighbors from the entire PDB quickly and accurately.Ensemble-based evaluation for protein structure models.Multi-view methods for protein structure comparison using latent dirichlet allocation.A novel method to compare protein structures using local descriptors.PocketAnnotate: towards site-based function annotation.GSAFold: a new application of GSA to protein structure prediction.Compressive genomics for protein databases.A closer look into the α-helix basin.PLoS Computational Biology conference postcards from ISMB 2010CFP: a web-server for constructing sequence-based protein conformational flexibility profiles.Biochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1AFINDSITE(X): a structure-based, small molecule virtual screening approach with application to all identified human GPCRs.Improving computational protein design by using structure-derived sequence profile.GOSSIP: a method for fast and accurate global alignment of protein structuresQuantitative modeling of transcription factor binding specificities using DNA shape.Fold-specific sequence scoring improves protein sequence matching.Nonlinearities in protein space limit the utility of informatics in protein biophysics.Evolutionary analysis of heterochromatin protein compatibility by interspecies complementation in Saccharomyces.Homology modelling and spectroscopy, a never-ending love story.Exploring the potential of a structural alphabet-based tool for mining multiple target conformations and target flexibility insight.Topological network alignment uncovers biological function and phylogeny.Automated antibody structure prediction using Accelrys tools: results and best practices.A genome-wide structure-based survey of nucleotide binding proteins in M. tuberculosis.The 11th misconception?Optimal network alignment with graphlet degree vectors.GRAFENE: Graphlet-based alignment-free network approach integrates 3D structural and sequence (residue order) data to improve protein structural comparison.Predicting loop conformational ensembles.Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes.Homology modeling in a dynamical world.Atrial natriuretic peptide vs. N-terminal-pro-atrial natriuretic peptide for the detection of left atrial dilatation in horses.The Relation between α-Helical Conformation and Amyloidogenicity.Machine Learning Methods for X-Ray Scattering Data Analysis from Biomacromolecular Solutions
P2860
Q27000781-30B85773-334F-4819-B894-3F34825EC137Q30361821-DF95ECFF-BEA5-48FA-ADE7-9CF417C8196BQ30362846-A61F138B-D96B-4D24-B9E7-5B51EAA8A815Q30369339-6DEE8486-CA54-4D76-B223-148B5A1CBEB0Q30378405-5176A96F-CA0E-4869-B87B-96A614DCA329Q30385398-F3646058-C956-41F2-84ED-1EA018238325Q30389338-7B285FF2-DFE2-43B2-8F72-5C05D43DF6E3Q30404013-724EF399-1AA8-4747-814C-5DF3C68BDEBFQ30406075-4430115E-2B2B-47B0-9298-954F71010B34Q30417121-2F50D338-FF3D-42EC-9263-F7FE53757A9AQ30417143-243E7BFF-E060-44E6-8984-5CCEAD3EF459Q30432596-05846E3C-29C0-48A8-95BC-8FCD4293A7B9Q30830738-94A55698-D28C-46BA-A17A-ED17A2F7AA80Q33750114-156CF4EE-E64A-4C76-8B0F-A7AACCFD2B1AQ33810210-2EA3F54A-F01A-4C8D-8792-D47148A7A4F0Q34052884-F7E57024-0AA5-4627-963F-0C623AB95ACAQ34265152-CF9B98E6-193D-4CA5-A44A-D37BBF3E7295Q34683409-BFC9CEB1-98A4-49FF-A68C-0F162FA1D0E8Q34729536-13C1EEA1-CC71-44BE-9BFA-552906654BCFQ35485439-DD20339E-97BA-4AB2-AB82-A60BEC3B1DE7Q36117991-6C735D81-9B53-4DB8-9D3D-F3F56080AFCDQ36172642-9D17B578-615A-4B3E-B5FF-73D4AA3FAFC8Q36466270-85559406-2B10-4E73-B51E-1BCE03BF11B2Q37589490-C9259CB7-BC60-4E59-BA5C-33F67EC87708Q38619920-DC3E898C-094A-4675-97AF-CE024DB48FAEQ41592105-374F25EA-EA9F-4AEF-A742-39D783EF3139Q42005537-7C256FAC-907E-472E-9119-9656400F9551Q42083154-B65B80D4-8504-4744-8E9B-B7BE6D0F87F3Q42147682-19EDC2AA-D207-4C9A-9DDA-F0337B89C9A1Q42735175-F4A848CB-5941-4CA2-86C0-213F8674B4BAQ47161898-D1C3761A-325C-4F4E-BC23-0E2B1DFA8B18Q47307363-6504FE32-1A52-439B-B11E-88F1914C1CDCQ47727645-0AD8FBF2-097A-4D7F-834D-4EEBFFFBA3EAQ47942457-81F34246-99FC-4B09-B50F-294F20F843A4Q49043967-C8A68CDE-3E57-4B91-B351-D1157D768E1CQ53695647-6342C0CE-E691-445C-95BC-6F733120A48FQ57978812-6AF1B7E9-FD90-427E-A1EC-5F99286806F0
P2860
Sequence-similar, structure-dissimilar protein pairs in the PDB.
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
name
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@ast
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@en
type
label
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@ast
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@en
prefLabel
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@ast
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@en
P2860
P356
P1433
P1476
Sequence-similar, structure-dissimilar protein pairs in the PDB.
@en
P2093
Mickey Kosloff
P2860
P304
P356
10.1002/PROT.21770
P407
P577
2008-05-01T00:00:00Z