A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary - Test2 - elhamkhani - TriplyDB

A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

http://www.wikidata.org/entity/Q24647013

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A consensus view of protein dynamics Improving the precision of the structure-function relationship by considering phylogenetic context FIEFDom: a transparent domain boundary recognition system using a fuzzy mean operator Exploring early stages of the chemical unfolding of proteins at the proteome scale Novel protein folds and their nonsequential structural analogs Structure-based barcoding of proteins.A framework for protein structure classification and identification of novel protein structures.Dynameomics: data-driven methods and models for utilizing large-scale protein structure repositories for improving fragment-based loop prediction.Identifying foldable regions in protein sequence from the hydrophobic signal.How a spatial arrangement of secondary structure elements is dispersed in the universe of protein folds.Cross-over between discrete and continuous protein structure space: insights into automatic classification and networks of protein structures.Systematic comparison of SCOP and CATH: a new gold standard for protein structure analysis.Improving protein fold recognition with hybrid profiles combining sequence and structure evolution.Discrete-continuous duality of protein structure space.Modular architecture of nucleotide-binding pockets.Generation of a consensus protein domain dictionary.Exploring the limits of fold discrimination by structural alignment: a large scale benchmark using decoys of known fold.A chemical group graph representation for efficient high-throughput analysis of atomistic protein simulations.The effect of edge definition of complex networks on protein structure identification.Implementation of 3D spatial indexing and compression in a large-scale molecular dynamics simulation database for rapid atomic contact detection Compression-based classification of biological sequences and structures via the Universal Similarity Metric: experimental assessment.New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins.ROC and confusion analysis of structure comparison methods identify the main causes of divergence from manual protein classification.3D complex: a structural classification of protein complexes The Dynameomics rotamer library: amino acid side chain conformations and dynamics from comprehensive molecular dynamics simulations in water.A comprehensive multidimensional-embedded, one-dimensional reaction coordinate for protein unfolding/folding.Dynameomics: a comprehensive database of protein dynamics.Protein folds and protein folding.Wavelet Analysis of Protein Motion Conformational entropy of alanine versus glycine in protein denatured states Rapid and enhanced remote homology detection by cascading hidden Markov model searches in sequence space.Touring protein space with Matt.A one-dimensional reaction coordinate for identification of transition states from explicit solvent P(fold)-like calculations.Development of a motif-based topology-independent structure comparison method to identify evolutionarily related folds.Exploring the suitability of coarse-grained techniques for the representation of protein dynamics.Architectures and functional coverage of protein-protein interfaces.Structural consequences of mutations to the α-tocopherol transfer protein associated with the neurodegenerative disease ataxia with vitamin E deficiency An in silico algorithm for identifying stabilizing pockets in proteins: test case, the Y220C mutant of the p53 tumor suppressor protein.Defining the structural origin of the substrate sequence independence of O-GlcNAcase using a combination of molecular docking and dynamics simulation.

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

http://www.wikidata.org/entity/Q24647013

description

2003 nî lūn-bûn

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2003 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2003 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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Protein Science

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A consensus view of fold space: combining SCOP, CATH, and the Dali Domain Dictionary

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David A C Beck

http://www.w3.org/2001/XMLSchema#string

Roger S Armen

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Ryan Day

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P2860

The Protein Data Bank

A fully automatic evolutionary classification of protein folds: Dali Domain Dictionary version 3

Domain assignment for protein structures using a consensus approach: characterization and analysis

SCOP: a structural classification of proteins database for the investigation of sequences and structures

CATH--a hierarchic classification of protein domain structures

The ASTRAL compendium for protein structure and sequence analysis

A systematic comparison of protein structure classifications: SCOP, CATH and FSSP

Parser for protein folding units

Protein structure alignment

Toward more meaningful hierarchical classification of protein three-dimensional structures.

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2150-60

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scholarly article

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10.1110/PS.0306803

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