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

S. Parthasarathy, M. R N Murthy

Research output: Contribution to journalArticle

128 Citations (Scopus)

Abstract

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 Cα 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 Ca 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.

Original languageEnglish (US)
Pages (from-to)9-13
Number of pages5
JournalProtein Engineering
Volume13
Issue number1
StatePublished - 2000
Externally publishedYes

Fingerprint

Protein Stability
Thermodynamic stability
Hot Temperature
Proteins
Amino acids
Amino Acids
Amino Acid Substitution
Atoms
Membrane Proteins
Polypeptides
X-Rays
Substitution reactions
Peptides
Crystal structure
X rays
Chemical analysis

Keywords

  • Protein dynamics
  • Protein stability
  • Temperature factors
  • Thermophiles
  • X-ray structures

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

Cite this

Protein thermal stability : Insights from atomic displacement parameters (B values). / Parthasarathy, S.; Murthy, M. R N.

In: Protein Engineering, Vol. 13, No. 1, 2000, p. 9-13.

Research output: Contribution to journalArticle

Parthasarathy, S & Murthy, MRN 2000, 'Protein thermal stability: Insights from atomic displacement parameters (B values)', Protein Engineering, vol. 13, no. 1, pp. 9-13.
Parthasarathy, S. ; Murthy, M. R N. / Protein thermal stability : Insights from atomic displacement parameters (B values). In: Protein Engineering. 2000 ; Vol. 13, No. 1. pp. 9-13.
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