Active-site studies of enzymes by secondary structure prediction and by molecular modeling

Cid, H.; Bunster, M

Keywords: sequence, dynamics, model, acid, inhibition, enzyme, activation, tertiary, animals, protein, structure, beta, ray, site, bisphosphatase, x-rays, molecular, data, active, article, secondary, hydrophobicity, venom, fructose, folding, crystallography, snake, phospholipase, amino, X, Models,, lactamase, 2,6, bisphosphate, a2, Structure,

Abstract

Since the determination of the tertiary structure by X-ray crystallography has been achieved only for a limited number of proteins, alternative approaches are being sought. In this article, the use of secondary structure prediction and of molecular modeling is discussed. Several examples are analyzed in detail.

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Título de la Revista: BIOLOGICAL RESEARCH
Volumen: 29
Número: 1
Editorial: Springer Nature
Fecha de publicación: 1996
Página de inicio: 77
Página final: 100
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-0029930008&partnerID=q2rCbXpz