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Low-complexity sequences and single amino acid repeats: not just "junk" peptide sequences.

Abstract:

For decades proteins were thought to interact in a "lock and key" system, which led to the definition of a paradigm linking stable three-dimensional structure to biological function. As a consequence, any non-structured peptide was considered to be nonfunctional and to evolve neutrally. Surprisingly, the most commonly shared peptides between eukaryotic proteomes are low-complexity sequences that in most conditions do not present a stable three-dimensional structure. However, because these seq...

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Publisher copy:
10.1139/g10-063

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Physiology Anatomy and Genetics
Golding, GB More by this author
Journal:
Genome / National Research Council Canada = Genome / Conseil national de recherches Canada
Volume:
53
Issue:
10
Pages:
753-762
Publication date:
2010-10-05
DOI:
EISSN:
1480-3321
ISSN:
0831-2796
URN:
uuid:fbabe8e7-7a3b-4eec-8d34-884cc845896f
Source identifiers:
237085
Local pid:
pubs:237085

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