Deciphering the structural code for proteins: Helical propensities in domain classes and statistical multiresidue information in α-helices

Viñuales, Y. Negrete, J. Palau, J.

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Deciphering the structural code for proteins: Helical propensities in domain classes and statistical multiresidue information in α-helices - PC:77

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https://hdl.handle.net/20.500.11797/PC77

Autor/es de la URV:	VIÑUALES ELIAS, YOLANDA Negrete, J. Palau, J.
Autor según el artículo:	Viñuales, Y. Negrete, J. Palau, J.
Identificador del autor:	n/a n/a n/a
Año de publicación de la revista:	1998
Tipo de publicación:	Artículo
ISSN:	0961-8368
Enlace a la fuente original:	http://onlinelibrary.wiley.com/doi/10.1002/pro.5560070613/abstract
Versión del articulo depositado:	info:eu-repo/semantics/publishedVersion
Acceso a la licencia de uso:	https://creativecommons.org/licenses/by/3.0/es/
Departamento:	Bioquímica i Biotecnologia
URL Documento de licencia:	https://repositori.urv.cat/ca/proteccio-de-dades/
Áreas temáticas:	Antropología
Entidad:	Universitat Rovira i Virgili
Fecha de alta del registro:	2015-02-19
Página inicial:	1368
Página final:	1379
Volumen de revista:	7

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Descripción:	Prova. Registre ja existent a GREC (TPAR 020035) 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.
Cobertura:	Anglès
Tipo:	article Article Artículo Article info:eu-repo/semantics/publishedVersion
Coautor:	Bioquímica i Biotecnologia Universitat Rovira i Virgili
Títol:	Deciphering the structural code for proteins: Helical propensities in domain classes and statistical multiresidue information in α-helices
Materia:	aigua helical patterns hydrophilic residues hydrophobic residues Antropologia Antropología Anthropology 0961-8368
Fecha:	1998
Formato:	3184 kb
Autor:	Viñuales, Y. Negrete, J. Palau, J.
Derechos:	info:eu-repo/semantics/openAccess

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