Please use this identifier to cite or link to this item: https://doi.org/10.1002/anie.201308512
Title: An off-pathway folding intermediate of an acyl carrier protein domain coexists with the folded and unfolded states under native conditions
Authors: Lim, J.
Xiao, T.
Fan, J. 
Yang, D. 
Keywords: acyl carrier protein
folding intermediates
protein dynamics
protein folding
protein structure
Issue Date: 24-Feb-2014
Citation: Lim, J., Xiao, T., Fan, J., Yang, D. (2014-02-24). An off-pathway folding intermediate of an acyl carrier protein domain coexists with the folded and unfolded states under native conditions. Angewandte Chemie - International Edition 53 (9) : 2358-2361. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.201308512
Abstract: A protein can exist in multiple states under native conditions and those states with low populations are often critical to biological function and self-assembly. To investigate the role of the minor states of an acyl carrier protein, NMR techniques were applied to determine the number of minor states and characterize their structures and kinetics. The acyl carrier protein from Micromonospora echinospora was found to exist in one major folded state (95.2 %), one unfolded state (4.1 %), and one intermediate state (0.7 %) under native conditions. The three states are in dynamic equilibrium and the intermediate state very likely adopts a native-like structure and is an off-pathway folding product. The intermediate state may mediate the formation of oligomers in vitro and play an important role in the recognition of partner enzymes in vivo. Neither U(p) nor (dow)N: Acyl carrier protein from Micromonospora echinospora adopts three conformations; one folded (N), one unfolded (U), and one intermediate (I). These undergo slow conformational exchange under native conditions. The intermediate state, which is an off-pathway rather than on-pathway product, may mediate the formation of oligomers in vitro and play an important role in the recognition of partner enzymes in vivo. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Source Title: Angewandte Chemie - International Edition
URI: http://scholarbank.nus.edu.sg/handle/10635/100075
ISSN: 14337851
DOI: 10.1002/anie.201308512
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

8
checked on Oct 12, 2018

WEB OF SCIENCETM
Citations

8
checked on Oct 3, 2018

Page view(s)

65
checked on Oct 12, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.