Document Detail


Exploring the folding energy landscape with pressure.
MedLine Citation:
PMID:  23246376     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The unique role of pressure in protein folding studies is emphasized. The variable-pressure NMR experiments carried out under equilibrium conditions gives unique opportunities to explore the energy landscape for protein folding. Intermediate conformers that may appear transiently in the kinetic folding experiments may be stably trapped under pressure, allowing examination of their conformations in site-specific detail with modern NMR spectroscopy. The intimate relationship between the kinetic folding experiment and the equilibrium pressure experiment is described with examples from ubiquitin and hen lysozyme.
Authors:
Kazuyuki Akasaka; Ryo Kitahara; Yuji O Kamatari
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-12-11
Journal Detail:
Title:  Archives of biochemistry and biophysics     Volume:  -     ISSN:  1096-0384     ISO Abbreviation:  Arch. Biochem. Biophys.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372430     Medline TA:  Arch Biochem Biophys     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012 Elsevier Inc. All rights reserved.
Affiliation:
High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan. Electronic address: akasaka@waka.kindai.ac.jp.
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