Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Konno, T.
Right arrow Articles by Nagayama, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Konno, T.
Right arrow Articles by Nagayama, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 9, Issue 3 564-569, Copyright © 2000 by The Protein Society

JOURNAL ARTICLE

Fluorinated alcohol, the third group of cosolvents that stabilize the molten-globule state relative to a highly denatured state of cytochrome c

T Konno, J Iwashita and K Nagayama
Center for Brain Experiment, National Institute for Physiological Sciences, Myodaiji, Okazaki, Japan. konno@nips.ac.jp

The effects of 1,1,1,3,3,3-hexafluoro-isopropanol (HFIP) on the conformation of cytochrome c (cyt c) at pH 1.9 were studied using a combination of spectroscopic and physical methods. Analysis varying the HFIP concentration showed that a compact denatured conformation (M(HF)) accumulates in a low concentration range of HFIP in the middle of structural transition from the highly unstructured acid-denatured state to the highly helical alcohol-denatured state of cyt c. This contrasts clearly with the effect of isopropanol (IP), in which no compact conformation accompanied with the transition. Analysis varying concentrations of HFIP and NaCl concurrently showed that the M(HF) state of cyt c is essentially identical to the salt-induced molten- globule (M(G)) state, and the M(G) state in the presence of salt was also stabilized by a low concentration of HFIP. Furthermore, 2,2,2- trifluoroethanol stabilized M(HF) similarly to HFIP, supporting the proposition that the specific effect observed for HFIP is caused by fluorination of alcohol. The mechanism stabilizing compact conformation by HFIP remains unclear, but is probably distinct from that of salts and polyols, which are also known to stabilize the M(G)-like state.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J BiochemHome page
M. Hameed, B. Ahmad, K. M. Fazili, K. Andrabi, and R. H. Khan
Different Molten Globule-like Folding Intermediates of Hen Egg White Lysozyme Induced by High pH and Tertiary Butanol
J. Biochem., April 1, 2007; 141(4): 573 - 583.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
Y. Kumar, S. Muzammil, and S. Tayyab
Influence of Fluoro, Chloro and Alkyl Alcohols on the Folding Pathway of Human Serum Albumin
J. Biochem., October 1, 2005; 138(4): 335 - 341.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
S. Kanjilal, N. Taulier, J.-Y. Le Huerou, M. Gindre, W. Urbach, and M. Waks
Ultrasonic Studies of Alcohol-Induced Transconformation in {beta}-Lactoglobulin: The Intermediate State
Biophys. J., December 1, 2003; 85(6): 3928 - 3934.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
A. A. Moosavi-Movahedi, J. Chamani, Y. Goto, and G. H. Hakimelahi
Formation of the Molten Globule-Like State of Cytochrome c Induced by n-Alkyl Sulfates at Low Concentrations
J. Biochem., January 1, 2003; 133(1): 93 - 102.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 by The Protein Society.