Expanding the proteome: disordered and alternatively folded proteins.
Ontology highlight
ABSTRACT: Proteins provide much of the scaffolding for life, as well as undertaking a variety of essential catalytic reactions. These characteristic functions have led us to presuppose that proteins are in general functional only when well structured and correctly folded. As we begin to explore the repertoire of possible protein sequences inherent in the human and other genomes, two stark facts that belie this supposition become clear: firstly, the number of apparent open reading frames in the human genome is significantly smaller than appears to be necessary to code for all of the diverse proteins in higher organisms, and secondly that a significant proportion of the protein sequences that would be coded by the genome would not be expected to form stable three-dimensional (3D) structures. Clearly t
SUBMITTER: Dyson HJ
PROVIDER: S-EPMC3189428 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
ACCESS DATA