z-logo
open-access-imgOpen Access
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].

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom