Meta-structure correlation in protein space unveils different selection rules for folded and intrinsically disordered proteins

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 solu...

ver descrição completa

Detalhes bibliográficos
Autores: Naranjo, Yandi, Pons Vallès, Miquel, Konrat, Robert
Formato: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2012
País:España
Recursos:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/47843
Acesso em linha:https://hdl.handle.net/2445/47843
Access Level:acceso abierto
Palavra-chave:Biomolècules
Ressonància magnètica nuclear
Seqüència d'aminoàcids
Àcids nucleics
Bioinformàtica
Biomolecules
Nuclear magnetic resonance
Amino acid sequence
Nucleic acids
Bioinformatics
Descrição
Resumo: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.