Repositori institucional URV
Español Català English
TITLE:
Deciphering the structural code for proteins: Helical propensities in domain classes and statistical multiresidue information in α-helices - PC:77

URV's Author/s:VIÑUALES ELIAS, YOLANDA
Negrete, J.
Palau, J.
Author, as appears in the article.:Viñuales, Y.
Negrete, J.
Palau, J.
Author identifier:n/a
n/a
n/a
Journal publication year:1998
Publication Type:Article
ISSN:0961-8368
Abstract: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.
Link to the original source:http://onlinelibrary.wiley.com/doi/10.1002/pro.5560070613/abstract
Papper version:info:eu-repo/semantics/publishedVersion
licence for use:https://creativecommons.org/licenses/by/3.0/es/
Department:Bioquímica i Biotecnologia
Licence document URL:https://repositori.urv.cat/ca/proteccio-de-dades/
Thematic Areas:Anthropology
Keywords:helical patterns
hydrophilic residues
hydrophobic residues
Entity:Universitat Rovira i Virgili
Record's date:2015-02-19
First page:1368
Last page:1379
Journal volume:7
Search your record at:

Available files
FileDescriptionFormat
DocumentPrincipalDocumentPrincipalapplication/pdf

Information

© 2011 Universitat Rovira i Virgili