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Titolo:
A COMPUTER VISION-BASED TECHNIQUE FOR 3-D SEQUENCE-INDEPENDENT STRUCTURAL COMPARISON OF PROTEINS
Autore:
BACHAR O; FISCHER D; NUSSINOV R; WOLFSON H;
Indirizzi:
TEL AVIV UNIV,FAC MED,SACKLER INST MOLEC MED IL-69978 TEL AVIV ISRAEL TEL AVIV UNIV,FAC MED,SACKLER INST MOLEC MED IL-69978 TEL AVIV ISRAEL TEL AVIV UNIV,SCH MATH SCI,DEPT COMP SCI IL-69978 TEL AVIV ISRAEL NCI,FCRF,PRI DYNACORP,MATH BIOL LAB FREDERICK MD 21702 NYU,COURANT INST MATH SCI,ROBOT RES LAB NEW YORK NY 10012
Titolo Testata:
Protein engineering
fascicolo: 3, volume: 6, anno: 1993,
pagine: 279 - 288
SICI:
0269-2139(1993)6:3<279:ACVTF3>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SEQUENCE; STRUCTURE ALIGNMENT; BACTERIAL FERREDOXIN; GENERAL METHOD; RECOGNITION; EVOLUTION; TAXONOMY;
Keywords:
COMPUTER VISION; 3-D PROTEIN MOTIFS; GEOMETRIC HASHING; PROTEIN FOLDING; PROTEIN STRUCTURAL COMPARISON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
O. Bachar et al., "A COMPUTER VISION-BASED TECHNIQUE FOR 3-D SEQUENCE-INDEPENDENT STRUCTURAL COMPARISON OF PROTEINS", Protein engineering, 6(3), 1993, pp. 279-288

Abstract

A detailed description of an efficient approach to comparison of protein structures is presented. Given the 3-D coordinate data of the structures to be compared, the system automatically identifies every region of structural similarity between the structures without prior knowledge of an initial alignment. The method uses the geometric hashing technique which was originally developed for model-based object recognition problems in the area of computer vision. It exploits a rotationallyand translationally invariant representation of rigid objects, resulting in a highly efficient, fully automated tool. The method is independent of the amino acid sequence and, thus, insensitive to insertions, deletions and displacements of equivalent substructures between the molecules being compared. The method described here is general, identifies 'real' 3-D substructures and is not constrained by the order imposed by the primary chain of the amino acids. Typical structure comparison problems are examined and the results of the new method are comparedwith the published results from previous methods. These results, obtained without using the sequence order of the chains, confirm publishedstructural analogies that use sequence-dependent techniques. Our results also extend previous analogies by detecting geometrically equivalent out-of-sequential-order structural elements which cannot be obtained by current techniques.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 03:28:01