Autor según el artículo: Viñuales, Y. Negrete, J. Palau, J.

Departamento: Bioquímica i Biotecnologia

Autor/es de la URV: VIÑUALES ELIAS, YOLANDA Negrete, J. Palau, J.

Palabras clave: helical patterns hydrophilic residues hydrophobic residues

Resumen: We made several statistical analyses in a large sample of nearly 4,000 helices (from 546 redundancy-controlled PDB protein subunits), which give new insights into the helical properties of globular proteins. In a first experiment, the amino acid composition of the whole sample was compared with the composition of two helical sample subgroups (the “mainly-α” and the “(α/β)8 barrel” domain classes); we reached the conclusion that composition-based helical propensities for secondary structure prediction do not depend on the structural class. Running a five-residue window through the whole sample, the positional composition revealed that positive and negative residues are located throughout the helices and tend to neutralize the macrodipole effect. On this basis, we analyzed charged triplets using a running five-residue window. The conclusion was that only mixed charged residues [positive (+) and negative (-)] located at positions 1-2-5 and 1-4-5 are clearly favored. In these locations the most abundant are (–.+) and (-.++), and this shows the existence of side chain microdipoles, which neutralize the large macrodipole of the helix.

Áreas temáticas: Antropologia Antropología Anthropology

Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/

ISSN: 0961-8368

Identificador del autor: n/a n/a n/a

Fecha de alta del registro: 2015-02-19

Página final: 1379

Volumen de revista: 7

Versión del articulo depositado: info:eu-repo/semantics/publishedVersion

Enlace a la fuente original: http://onlinelibrary.wiley.com/doi/10.1002/pro.5560070613/abstract

Entidad: Universitat Rovira i Virgili

Año de publicación de la revista: 1998

Página inicial: 1368

Tipo de publicación: Article Artículo Article