Recent Molecular Research on Protein Structure and Function

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 15 December 2026 | Viewed by 980

Special Issue Editor


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Guest Editor
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22903, USA
Interests: protein chemistry; biochemistry; structural biology; protein-protein interactions; structrual and functional elucidation of proteins and protiein complexes

Special Issue Information

Dear Colleagues,

We are pleased to invite you to submit your original research and review articles for a Special Issue of Biomolecules titled ‘Recent Molecular Research on Protein Structure and Function’. Proteins are central to virtually all cellular processes, and understanding their structure and function is crucial for advancing our knowledge in molecular biology, biotechnology, and medicine.

This Special Issue aims to bring together the latest research on the molecular mechanisms underlying protein structure, function, and interactions. We encourage submissions that explore the dynamic relationship between protein architecture and its functional roles in diverse biological contexts. This includes both experimental and computational studies that investigate how protein structures contribute to their biological activities, as well as the development of new technologies for probing these relationships.

In this Special Issue, original research articles and reviews are welcome. Research areas may include (but are not limited to) the following:

  • Protein folding and misfolding mechanisms;
  • Protein–protein and protein–ligand interactions ;
  • Computational predictions of protein structure and function;
  • Structure–function relationships in enzymes and other functional proteins;
  • Structural insights into disease-related proteins (e.g., neurodegenerative diseases, cancer);
  • Advances in techniques for structural analysis (X-ray crystallography, NMR, cryo-EM, etc.);
  • Impact of post-translational modifications on protein function and stability.

We look forward to receiving your contributions and to the opportunity to showcase cutting-edge research in the field of protein structure and function.

Dr. Sonani Ravi Raghav
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 250 words) can be sent to the Editorial Office for assessment.

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. Biomolecules 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 structure
  • protein function
  • molecular mechanisms
  • protein folding
  • structural biology

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Published Papers (1 paper)

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Research

19 pages, 1525 KB  
Article
Screening and Validation of Functional Residues of the Antimicrobial Peptide PpRcys1
by Ming Tao, Zixun Fei, Aobo Sun, Guangming Yu, Huaiyuan Ye, Huishao Shi, Wei Zhang and Junjian Wang
Biomolecules 2025, 15(11), 1617; https://doi.org/10.3390/biom15111617 - 18 Nov 2025
Viewed by 322
Abstract
The excessive use of conventional antibiotics in aquaculture has created significant challenges, making it essential to explore and develop effective alternatives. Antimicrobial peptides (AMPs) have gained attention as potential therapeutic agents owing to their wide-ranging antibacterial effects and their ability to address pathogens [...] Read more.
The excessive use of conventional antibiotics in aquaculture has created significant challenges, making it essential to explore and develop effective alternatives. Antimicrobial peptides (AMPs) have gained attention as potential therapeutic agents owing to their wide-ranging antibacterial effects and their ability to address pathogens resistant to conventional drugs. PpRcys1 is an antimicrobial peptide that mainly targets bacterial cell membranes, exhibiting a minimum inhibitory concentration of 8–32 μM. Its antibacterial activity should be further optimized. Before such optimization, however, it is crucial to identify the key amino acid residues that determine its functional activity. In this study, molecular dynamics simulations indicated that arginine 40 (ARG40), lysine 55 (LYS55), lysine 90 (LYS90), and lysine 93 (LYS93) play critical roles in the interaction between PpRcys1 and bacterial membranes. To investigate this further, these residues were mutated to serine, producing the mutant peptide PpRcys1_RMRK. Compared with PpRcys1, the mutant peptide PpRcys1_RMRK showed a significant reduction in antibacterial activity. Results from molecular dynamics simulations, Western blot, and ELISA demonstrated a marked decrease in its ability to bind to bacterial cell membranes. Membrane permeation assays, cell membrane depolarization experiments, and scanning electron microscopy revealed that PpRcys1 could not compromise the integrity of the bacterial membrane after losing ARG40, LYS55, LYS90 and LYS93. These findings highlight the critical roles of ARG40, LYS55, LYS90, and LYS93 in sustaining the antibacterial activity of PpRcys1. This study provides important initial insights into the structure–activity relationship of PpRcys1 and establishes a theoretical foundation for its future optimization. Full article
(This article belongs to the Special Issue Recent Molecular Research on Protein Structure and Function)
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