The Protein Trinity: Structure/Function Relationships That Include Intrinsic Disorder
Author(s) -
A. Keith Dunker,
Celeste J. Brown,
J. David Lawson,
Lilia M. Iakoucheva-Sebat,
Slobodan Vučetić,
Zoran Obradović
Publication year - 2002
Publication title -
the scientific world journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.453
H-Index - 93
eISSN - 2356-6140
pISSN - 1537-744X
DOI - 10.1100/tsw.2002.25
Subject(s) - function (biology) , intrinsically disordered proteins , protein structure , computational biology , protein function , protein function prediction , peptide sequence , protein structure prediction , chemistry , biology , biophysics , biochemistry , microbiology and biotechnology , gene
. The current, dominant view relating protein structure to function can be expressed as amino acid sequence → 3-D structure → function. Currently, more than 200 counter examples in which function depends on nonfolded or incompletely folded regions of protein have been described. Furthermore, reviews on intrinsically disordered proteins are beginning to appear[1,2,3]. In one of these reviews, it is suggested that the existence of proteins with intrinsic protein disorder calls for a re-assessment of the protein structure-function paradigm[3].
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