Logo image
Back
Lessons in stability from thermophilic proteins
Journal article   Open access   Peer reviewed

Lessons in stability from thermophilic proteins

Abbas Razvi and J. Martin Scholtz
Protein science, Vol.15(7), pp.1569-1578
07/01/2006
DOI: 10.1110/ps.062130306
PMCID: PMC2242557
PMID: 16815912
url
https://europepmc.org/articles/pmc2242557View
Published (Version of record) Open Access

Abstract

Studies that compare proteins from thermophilic and mesophilic organisms can provide insights into ability of thermophiles to function at their high habitat temperatures and may provide clues that enable us to better define the forces that stabilize all proteins. Most of the comparative studies have focused on thermal stability and show, as expected, that thermophilic proteins have higher T m values than their mesophilic counterparts. Although these comparisons are useful, more detailed thermodynamic analyses are required to reach a more complete understanding of the mechanisms thermophilic protein employ to remain folded over a wider range of temperatures. This complete thermodynamic description allows one to generate a stability curve for a protein that defines how the conformational stability (Δ G ) varies with temperature. Here we compare stability curves for many pairs of homologous proteins from thermophilic and mesophilc organisms. Of the basic methods that can be employed to achieve enhanced thermostability, we find that most thermophilic proteins use the simple method that raises the Δ G at all temperatures as the principal way to increase their T m . We discuss and compare this thermodynamic method with the possible alternatives. In addition we propose ways that structural alterations and changes to the amino acid sequences might give rise to varied methods used to obtain thermostability.
 protein folding protein stability curves Review thermodynamics thermophiles thermostability

Details

Metrics

51 Record Views
265 Times Cited - Web of Science
Logo image