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Evidence for cysteine clustering in thermophilic proteomes

TitoloEvidence for cysteine clustering in thermophilic proteomes
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2002
AutoriRosato, V., Pucello N., and Giuliano Giovanni
RivistaTrends in Genetics
Volume18
Paginazione278-281
ISSN01689525
Parole chiaveamino acid analysis, Amino Acid Sequence, Bacteria (microorganisms), bacterial growth, Cysteine, disulfide bond, Evolution, nonhuman, priority journal, protein motif, proteome, review, Site directed mutagenesis, Temperature, thermophilic bacterium, thermostability, tryptophan
Abstract

Through linguistic analysis, we show that the presence of an amino acid at a given position within a proteome positively influences the presence of identical amino acids at nearby positions. We call this phenomenon 'amino acid clustering'. Clustering extends well beyond the closest neighbouring sites and is particularly pronounced for cysteine and tryptophan. Cysteine clusters preferentially form CXXC structures, and they are often involved in metal coordination or disulfide bond formation. Cysteine clustering shows a clear correlation with the growth temperature of the organism. This seems to be a general property of living organisms.

Note

cited By 32

URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-0036606927&doi=10.1016%2fS0168-9525%2802%2902691-4&partnerID=40&md5=c3ecb34fc262d18daaa7b5a6f3d27f91
DOI10.1016/S0168-9525(02)02691-4
Citation KeyRosato2002278