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 KUHLMAN, B.
Right arrow Articles by RALEIGH, D. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by KUHLMAN, B.
Right arrow Articles by RALEIGH, D. P.
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 7, Issue 11 2405-2412, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H(2)O and D(2)O. Determination of the thermodynamic parameters, {Delta}H{deg}, {Delta}S{deg}, and {Delta}C{deg}(p), and evaluation of solvent isotope effects

B. KUHLMAN and D. P. RALEIGH
Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400

The stability of the N-terminal domain of the ribosomal protein L9, NTL9, from Baccilus stearothermophilus has been monitored by circular dichroism at various temperatures and chemical denaturant concentrations in H(2)O and D(2)O. The basic thermodynamic parameters for the unfolding reaction, {Delta}H{deg}, {Delta}S{deg}, and {Delta}C{deg}(p), were determined by global analysis of temperature and denaturant effects on stability. The data were well fit by a model that assumes stability varies linearly with denaturant concentration and that uses the Gibbs-Helmholtz equation to model changes in stability with temperature. The results obtained from the global analysis are consistent with information obtained from individual thermal and chemical denaturations. NTL9 has a maximum stability of 3.78 +/- 0.25 kcal mol(-1) at 14{deg}C. {Delta}H{deg}(25{deg}C) for protein unfolding equals 9.9 +/- 0.7 kcal mol(-1) and T{Delta}S{deg}(25{deg}C) equals 6.2 +/- 0.6 kcal mol(-1). {Delta}C{deg}(p) equals 0.53 +/- 0.06 kcal mol(-1) deg(-1). There is a small increase in stability when D(2)O is substituted for H(2)O. Based on the results from global analysis, NTL9 is 1.06 +/- 0.60 kcal mol(-1) more stable in D(2)O at 25{deg}C and T(m) is increased by 5.8 +/- 3.6{deg}C in D(2)O. Based on the results from individual denaturation experiments, NTL9 is 0.68 +/- 0.68 kcal mol(-1) more stable in D(2)O at 25{deg}C and T(m) is increased by 3.5 +/- 2.1{deg}C in D(2)O. Within experimental error there are no changes in {Delta}H{deg} (25{deg}C) when D(2)O is substituted for H(2)O.
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
 Proc. Natl. Acad. Sci. USAHome page
N. L. Ogihara, G. Ghirlanda, J. W. Bryson, M. Gingery, W. F. DeGrado, and D. Eisenberg
Design of three-dimensional domain-swapped dimers and fibrous oligomers
PNAS, February 13, 2001; 98(4): 1404 - 1409.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by The Protein Society.