Structural Biochemistry and Evolution of Proteins

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Proteins and Proteomics".

Deadline for manuscript submissions: closed (28 February 2023) | Viewed by 2327

Special Issue Editors


E-Mail Website
Guest Editor
Department of General Chemistry, Belarusian State Medical University, Dzerzhinskogo 83, 220045 Minsk, Belarus
Interests: DNA; genomics; sequencing; proteins; biochemistry; RNA; DNA sequencing; PCR; gel electrophoresis; bioinformatics

E-Mail Website
Guest Editor
Department of Chemical Sciences, Universita di Napoli, 80131 Naples, Italy
Interests: cold denaturation of proteins; marginally stable proteins; structural Biology; taste receptors; sweet proteins; crowding and confinement

Special Issue Information

Dear Colleagues,

The Special Issue, “Structural Biochemistry and Evolution of Proteins”, is intended to provide a forum for the publication of articles on the structural biochemistry of proteins in which the data are interpreted from an evolutionary perspective. Both “dry” and “wet” biochemical studies are welcome, while preference would be given to manuscripts that combine both approaches. New data, dependences, hypotheses, concepts and theories on the structure, function and origin of proteins obtained with the help of computational biology are expected to be published in this Special Issue. Fields in which the structural biochemistry of proteins is applied include drug design studies, immunology, microbiology, virology, phylogenetics, proteomics, enzymology, and metallomics. Manuscripts in the abovementioned fields of science are acceptable if they include methodologies for exploring the structural and/or evolutionary biochemistry of proteins. In the same manner, articles describing new methods for the secondary, tertiary, and quaternary structure prediction of proteins are suitable as long as they use evolutionary thinking, as are studies on the role of intrinsically disordered regions of proteins in evolution. Reviews on the molecular evolution of certain proteins, their families, superfamilies, are structural classes are expected to become highlights of this Special Issue—especially if they refer to the theory of neutral evolution.

Dr. Vladislav Khrustalev
Prof. Dr. Pierandrea Temussi
Guest Editors

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. Life 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 2600 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.

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

8 pages, 2053 KiB  
Communication
Assessment of Thermal Stability of Mutant p53 Proteins via Differential Scanning Fluorimetry
by Raniya Khadiullina, Regina Mirgayazova, Damir Davletshin, Elvina Khusainova, Vitaly Chasov and Emil Bulatov
Life 2023, 13(1), 31; https://doi.org/10.3390/life13010031 - 22 Dec 2022
Cited by 7 | Viewed by 1901
Abstract
The p53 protein is a transcription factor that preserves the integrity of the genome. The TP53 gene has inactivating mutations in about 50% of all human cancers. Some missense mutations lead to decreased thermal stability in the p53 protein, its unfolding and aggregation [...] Read more.
The p53 protein is a transcription factor that preserves the integrity of the genome. The TP53 gene has inactivating mutations in about 50% of all human cancers. Some missense mutations lead to decreased thermal stability in the p53 protein, its unfolding and aggregation under physiological conditions. A general understanding of the impact of point mutations on the stability and conformation of mutant p53 is essential for the design and development of small molecules that target specific p53 mutations. In this work, we determined the thermostability properties of some of the most common mutant forms of the p53 protein—p53(R273H), p53(R248Q), p53(R248W) and p53(Y220C)—that are often considered as attractive therapeutic targets. The results showed that these missense mutations lead to destabilization of the p53 protein and a decrease in its melting temperature. Full article
(This article belongs to the Special Issue Structural Biochemistry and Evolution of Proteins)
Show Figures

Figure 1

Back to TopTop