Exploring the folding energy landscape with pressure

Kazuyuki Akasaka; Ryo Kitahara; Yuji O Kamatari

doi:10.1016/j.abb.2012.11.016

Exploring the folding energy landscape with pressure

Arch Biochem Biophys. 2013 Mar;531(1-2):110-5. doi: 10.1016/j.abb.2012.11.016. Epub 2012 Dec 12.

Authors

Kazuyuki Akasaka¹, Ryo Kitahara, Yuji O Kamatari

Affiliation

¹ High Pressure Protein Research Center, Institute of Advanced Technology, Kinki University, 930 Nishimitani, Kinokawa 649-6493, Japan. akasaka@waka.kindai.ac.jp

PMID: 23246376
DOI: 10.1016/j.abb.2012.11.016

Abstract

The unique role of pressure in protein folding studies is emphasized. Variable-pressure NMR experiments carried out under equilibrium conditions give 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.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Kinetics
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular / methods
Pressure
Protein Folding*
Proteins / chemistry*

Substances

Proteins