Density discriminates between thermophilic and mesophilic proteins

J Biomol Struct Dyn. 2018 Sep;36(12):3265-3273. doi: 10.1080/07391102.2017.1385537. Epub 2017 Oct 13.

Abstract

Despite an intense interest and a remarkable number of studies on the subject, the relationships between thermostability and (primary, secondary and tertiary) structure of proteins are still not fully understood. Here, comparing the protein density - defined by the ratio between the residue number and protein excluded volume - for a set of thermophilic/mesophilic pairs, we provide evidence that this property is connected to the optimal growth temperature. In particular, our results indicate that thermophilic proteins have - in general - a lower density with respect to the mesophilic counterparts, being such a correlation more pronounced for optimal growth temperature differences greater than 40°C. The effect of the protein thermostability changes on the molecular shape is also presented.

Keywords: mesophilic and thermophilic proteins; protein density; protein structure; thermostability.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Bacteria / chemistry*
  • Bacteria / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Hot Temperature
  • Protein Stability*
  • Temperature

Substances

  • Amino Acids
  • Bacterial Proteins