Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
THE LINKED PHI-PSI CHAIN PLOT FOR VISUAL COMPARISON OF THE BACKBONE CONFORMATION OF PEPTIDES AND PROTEINS
Autore:
MCCLAIN RD; ERICKSON BW;
Indirizzi:
UNIV N CAROLINA,DEPT CHEM,CB 3290 CHAPEL HILL NC 27599 UNIV N CAROLINA,DEPT CHEM CHAPEL HILL NC 27599
Titolo Testata:
International journal of peptide & protein research
fascicolo: 3, volume: 45, anno: 1995,
pagine: 272 - 281
SICI:
0367-8377(1995)45:3<272:TLPCPF>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
SECONDARY STRUCTURE; GLOBULAR-PROTEINS; RESOLUTION; RECOGNITION; DESIGN;
Keywords:
BACKBONE GEOMETRY; BETA-TURNS; BETA-SHEETS; CHAIN PLOTS; DIHEDRAL ANGLES; HELICES; LINKED PHI-PSI CHAIN PLOT; LINKING PATTERNS; PEPTIDE CONFORMATIONS; PROTEIN CONFORMATIONS; SECONDARY STRUCTURE; 3-DIMENSIONAL STRUCTURAL COMPARISON; 2-DIMENSIONAL GRAPHS; VISUAL COMPARISON;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
R.D. Mcclain e B.W. Erickson, "THE LINKED PHI-PSI CHAIN PLOT FOR VISUAL COMPARISON OF THE BACKBONE CONFORMATION OF PEPTIDES AND PROTEINS", International journal of peptide & protein research, 45(3), 1995, pp. 272-281

Abstract

A new graphic method is described for presenting in two dimensions the phi and psi dihedral angles that describe the backbone conformation of a peptide or protein chain. For each residue in sequence, phi and psi are plotted as dots on the y-axis above the next two points on the x-axis representing the residue number. Each dot is linked to the nextdot by a slanting line segment (link) and each cis-peptide bond (omega similar to 0 degrees) between residues X and Y is indicated by marking dots psi(X) and phi(Y) with a diamond. This linked phi psi chain plot is more useful than an unlinked phi psi chain plot for visually recognizing helices, sheets and turns and for graphically comparing several protein structures. Overlaying the linked phi psi chain plots for 15 beta-hairpins classified as type-I' beta-turns revealed that three were significantly different from the rest. The dihedral angles (mean +/- standard deviation) of the loop residues (L1, L2) for a cluster of 12 beta-hairpins with an inverse-common, type-I' beta-turn (phi(L1) = 52 +/- 7 degrees, psi(L1) = 40 +/- 8 degrees, phi(L2) = 80 +/- 9 degrees, psi(L2) = - 1 +/- 13 degrees) are similar to the standard dihedralangles for the type-1' turn (60, 30, 90 and 0 degrees, respectively). (C) Munksgaard 1995.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 04:23:20