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Force spectroscopy of an elastic peptide: Effect of D(2) O and temperature on persistence length.
MedLine Citation:
PMID:  21275005     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
This study explores the mechanical unfolding of elastic protein analogues as a function of temperature, in both H(2) O and D(2) O, using atomic force microscopy (AFM) force spectroscopy in a specially constructed AFM liquid cell. This represents the first time that the effect of D(2) O on protein flexibility has been investigated at the single molecule level by this technique. Model elastic peptides, R6, were encoded from synthetic genes expressed in Escherichia coli. The peptides possess short N- and C-terminal domains with central repetitive domains containing 13 repeats of the motif PGQGQQ-plus-GYYPTSLQQ. These sequences mimic those in native high molecular weight subunit glutenin proteins which confer elasticity to bread dough. Fitting single molecule stretching events to the worm-like chain model, allows determination of the molecular persistence length under various experimental conditions. The effect of increasing the temperature is to increase the persistence length of the peptide in both H(2) O and D(2) O, consistent with the expected "thermal softening" effect. However, the effect is significantly enhanced in D(2) O, in which the persistence length at 45°C is ∼25% greater than the value measured in H(2) O at the same temperature. Stronger intrapeptide H-bonding due to isotopic substitution of hydrogen for deuterium is the most likely cause of the enhanced backbone rigidity. Microsc. Res. Tech. 74:170-176, 2011. © 2010 Wiley-Liss, Inc.
Authors:
Simon J Haward; Peter R Shewry; Justin Marsh; Mervyn J Miles; Terence J Mc Master
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Microscopy research and technique     Volume:  74     ISSN:  1097-0029     ISO Abbreviation:  Microsc. Res. Tech.     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2011-01-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9203012     Medline TA:  Microsc Res Tech     Country:  United States    
Other Details:
Languages:  eng     Pagination:  170-6     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Wiley-Liss, Inc.
Affiliation:
H. H. Wills Physics Laboratory, University of Bristol, Tyndall Avenue, Bristol BS8 1TL, United Kingdom. s.j.haward@bristol.ac.uk.
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