Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/47843
Title: Meta-structure correlation in protein space unveils different selection rules for folded and intrinsically disordered proteins
Author: Naranjo, Yandi
Pons Vallès, Miquel
Konrat, Robert
Keywords: Biomolècules
Ressonància magnètica nuclear
Seqüència d'aminoàcids
Àcids nucleics
Bioinformàtica
Biomolecules
Nuclear magnetic resonance
Amino acid sequence
Nucleic acids
Bioinformatics
Issue Date: 2012
Publisher: Royal Society of Chemistry
Abstract: The number of existing protein sequences spans a very small fraction of sequence space. Natural proteins have overcome a strong negative selective pressure to avoid the formation of insoluble aggregates. Stably folded globular proteins and intrinsically disordered proteins (IDP) use alternative solutions to the aggregation problem. While in globular proteins folding minimizes the access to aggregation prone regions IDPs on average display large exposed contact areas. Here, we introduce the concept of average meta-structure correlation map to analyze sequence space. Using this novel conceptual view we show that representative ensembles of folded and ID proteins show distinct characteristics and responds differently to sequence randomization. By studying the way evolutionary constraints act on IDPs to disable a negative function (aggregation) we might gain insight into the mechanisms by which function - enabling information is encoded in IDPs.
Note: Versió postprint del document publicat a: http://dx.doi.org/10.1039/c1mb05367a
It is part of: Molecular Biosystems, 2012, vol. 8, num. 1, p. 411-416
Related resource: http://dx.doi.org/10.1039/c1mb05367a
URI: http://hdl.handle.net/2445/47843
ISSN: 1742-206X
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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