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Biology
Special Issues
Mechanisms of Protein Thermostability
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Mechanisms of Protein Thermostability

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

Deadline for manuscript submissions: 30 November 2024 | Viewed by 1340

Special Issue Editor

Dr. Kesen Ma

E-Mail Website
Guest 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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biology is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

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 941
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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