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Titolo:
THE ALPHA-HELIX AS SEEN FROM THE PROTEIN TERTIARY STRUCTURE - A 3-D STRUCTURAL CLASSIFICATION
Autore:
BLUNDELL TL; ZHU ZY;
Indirizzi:
UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,IMPERIAL CANC RES FUND,STRUCT MOLEC BIOL UNIT,MALET ST LONDON WC1E 7HX ENGLAND
Titolo Testata:
Biophysical chemistry
fascicolo: 1-2, volume: 55, anno: 1995,
pagine: 167 - 184
SICI:
0301-4622(1995)55:1-2<167:TAASFT>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID SUBSTITUTION TABLES; OCCURRING AMINO-ACIDS; SECONDARY-STRUCTURE; GLOBULAR-PROTEINS; DATA-BANK; PREDICTION; STABILITY; TEMPLATES; SEQUENCE; GLYCINE;
Keywords:
PROTEIN CLASSIFICATION; AMPHIPATHIC ALPHA-HELIX; AMINO ACID PATTERN; SECONDARY STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
T.L. Blundell e Z.Y. Zhu, "THE ALPHA-HELIX AS SEEN FROM THE PROTEIN TERTIARY STRUCTURE - A 3-D STRUCTURAL CLASSIFICATION", Biophysical chemistry, 55(1-2), 1995, pp. 167-184

Abstract

Helices are selected from globular protein structures defined at highresolution by X-ray analysis. We cluster cr-helices in two ways: according to their position in the tertiary structure by considering patterns of solvent inaccessible residues and according to the are of the solvent inaccessible face. For each class of helices we have defined propensities for amino acids at each position; these can be used to calculate templates for recognition of a member of that class. The analysis provides a basis for the prediction of alpha-helices and estimation of their approximate position in a protein tertiary structure. It alsoprovides an approach to estimating the probability of finding amino acid sequences as helices in solution and in a folded protein, thus indicating those helices that might be involved in nucleation of protein folding.

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Documento generato il 01/12/20 alle ore 07:08:00