Mechanisms of Protein Thermostability

A special issue of Biology (ISSN 2079-7737).

Deadline for manuscript submissions: 30 November 2024 | Viewed by 1523

Special Issue Editor

Department of Biology, University of Waterloo, Waterloo, ON, Canada
Interests: enzymes; microbiology; biochemistry; enzymology; protein purification; protein analysis; hyperthermophiles
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Proteins are essential and play structural and catalytical roles in all life forms. Their stabilities are required for performing various physiological functions under different growth conditions. Many proteins are stable in a wider range of temperatures, particularly at high temperatures (>100°C). Progress has been made to understand the nature of their thermostability. It is known that multiple factors may be involved in protein thermostability, such as amino acid composition, salt bridge, core packing, hydrophobicity, etc. Elucidation of mechanisms of protein thermostability will not only contribute to understanding life processes at different temperatures, but also the applications of enzyme catalysis in biotechnology. More studies, including bioengineering, will advance our knowledge in this area.

Dr. Kesen Ma
Guest Editor

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Keywords

  • protein thermostability
  • enzyme stability
  • biocatalysis
  • mechanism of protein thermostability
  • protein structure and function
  • bioengineering for protein thermostability

Published Papers (1 paper)

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Research

16 pages, 3081 KiB  
Article
Thermal Characterization and Interaction of the Subunits from the Multimeric Bacteriophage Endolysin PlyC
by J. Todd Hoopes, Ryan D. Heselpoth, Frederick P. Schwarz and Daniel C. Nelson
Biology 2023, 12(10), 1277; https://doi.org/10.3390/biology12101277 - 25 Sep 2023
Viewed by 1079
Abstract
Bacteriophage endolysins degrade the bacterial peptidoglycan and are considered enzymatic alternatives to small-molecule antibiotics. In particular, the multimeric streptococcal endolysin PlyC has appealing antibacterial properties. However, a comprehensive thermal analysis of PlyC is lacking, which is necessary for evaluating its long-term stability and [...] Read more.
Bacteriophage endolysins degrade the bacterial peptidoglycan and are considered enzymatic alternatives to small-molecule antibiotics. In particular, the multimeric streptococcal endolysin PlyC has appealing antibacterial properties. However, a comprehensive thermal analysis of PlyC is lacking, which is necessary for evaluating its long-term stability and downstream therapeutic potential. Biochemical and kinetic-based methods were used in combination with differential scanning calorimetry to investigate the structural, kinetic, and thermodynamic stability of PlyC and its various subunits and domains. The PlyC holoenzyme structure is irreversibly compromised due to partial unfolding and aggregation at 46 °C. Unfolding of the catalytic subunit, PlyCA, instigates this event, resulting in the kinetic inactivation of the endolysin. In contrast to PlyCA, the PlyCB octamer (the cell wall-binding domain) is thermostable, denaturing at ~75 °C. The isolation of PlyCA or PlyCB alone altered their thermal properties. Contrary to the holoenzyme, PlyCA alone unfolds uncooperatively and is thermodynamically destabilized, whereas the PlyCB octamer reversibly dissociates into monomers and forms an intermediate state at 74 °C in phosphate-buffered saline with each subunit subsequently denaturing at 92 °C. Adding folded PlyCA to an intermediate state PlyCB, followed by cooling, allowed for in vitro reconstitution of the active holoenzyme. Full article
(This article belongs to the Special Issue Mechanisms of Protein Thermostability)
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