Imperial College London

ProfessorMichaelSternberg

Faculty of Natural SciencesDepartment of Life Sciences

Director Centre for Bioinformatics
 
 
 
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Contact

 

+44 (0)20 7594 5212m.sternberg Website

 
 
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Location

 

306Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Janin:2013:10.3410/B5-2,
author = {Janin, J and Sternberg, MJE},
doi = {10.3410/B5-2},
journal = {F1000 Biol Rep},
title = {Protein flexibility, not disorder, is intrinsic to molecular recognition.},
url = {http://dx.doi.org/10.3410/B5-2},
volume = {5},
year = {2013}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - An 'intrinsically disordered protein' (IDP) is assumed to be unfolded in the cell and perform its biological function in that state. We contend that most intrinsically disordered proteins are in fact proteins waiting for a partner (PWPs), parts of a multi-component complex that do not fold correctly in the absence of other components. Flexibility, not disorder, is an intrinsic property of proteins, exemplified by X-ray structures of many enzymes and protein-protein complexes. Disorder is often observed with purified proteins in vitro and sometimes also in crystals, where it is difficult to distinguish from flexibility. In the crowded environment of the cell, disorder is not compatible with the known mechanisms of protein-protein recognition, and, foremost, with its specificity. The self-assembly of multi-component complexes may, nevertheless, involve the specific recognition of nascent polypeptide chains that are incompletely folded, but then disorder is transient, and it must remain under the control of molecular chaperones and of the quality control apparatus that obviates the toxic effects it can have on the cell.
AU - Janin,J
AU - Sternberg,MJE
DO - 10.3410/B5-2
PY - 2013///
SN - 1757-594X
TI - Protein flexibility, not disorder, is intrinsic to molecular recognition.
T2 - F1000 Biol Rep
UR - http://dx.doi.org/10.3410/B5-2
UR - https://www.ncbi.nlm.nih.gov/pubmed/23361309
UR - http://hdl.handle.net/10044/1/56808
VL - 5
ER -