Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (18)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Parthasarathy, S.
Right arrow Articles by Murthy, M.R.N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Parthasarathy, S.
Right arrow Articles by Murthy, M.R.N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 13, No. 1, 9-13, January 2000
© 2000 Oxford University Press

Protein thermal stability: insights from atomic displacement parameters (B values)

S. Parthasarathy and M.R.N. Murthy1

Molecular Biophysics Unit, Indian Institute of Science,Bangalore 560 012, India

The factors contributing to the thermal stability of proteins from thermophilic origins are matters of intense debate and investigation. Thermophilic proteins are thought to possess better packed interiors than their mesophilic counterparts, leading to lesser overall flexibility and a corresponding reduction in surface-to-volume ratio. These observations prompted an analysis of B values reported in high-resolution X-ray crystal structures of mesophilic and thermophilic proteins. In this analysis, the following aspects were addressed: (1) frequency distribution of normalized B values (B' factors) over all the proteins and for individual amino acids; (2) amino acid compositions in high B value regions of polypeptide chains; (3) variation in the B values from core to the surface of proteins in terms of their radius of gyration; and (4) degree of dispersion of normalized B values in spheres around the C{alpha} atoms. The analysis revealed that (1) Ser and Thr have lesser flexibility in thermophiles than in mesophiles, (2) the proportion of Glu and Lys in high B value regions of thermophiles is higher and that of Ser and Thr is lower and (3) the dispersion of B values within spheres at C{alpha} atoms is similar in mesophiles and thermophiles. These observations reflect plausible differences in the dynamics of thermophilic and mesophilic proteins and suggest amino acid substitutions that are likely to change thermal stability.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
R. Linding, R. B. Russell, V. Neduva, and T. J. Gibson
GlobPlot: exploring protein sequences for globularity and disorder
Nucleic Acids Res., July 1, 2003; 31(13): 3701 - 3708.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
Z. Yuan, J. Zhao, and Z.-X. Wang
Flexibility analysis of enzyme active sites by crystallographic temperature factors
Protein Eng. Des. Sel., February 1, 2003; 16(2): 109 - 114.
[Abstract] [Full Text] [PDF]

Home page
 Protein Eng Des SelHome page
N. Kannan and S. Vishveshwara
Aromatic clusters: a determinant of thermal stability of thermophilic proteins
Protein Eng. Des. Sel., November 1, 2000; 13(11): 753 - 761.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.