ijms-logo

Journal Browser

Journal Browser

Biomolecular Structure, Function and Interactions: 2nd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 31 December 2025 | Viewed by 310

Special Issue Editor

Special Issue Information

Dear Colleagues, 

Biophysical chemistry is a truly interdisciplinary endeavour combining the principles of physics, biology, and chemistry to explore the processes in biological systems and their underlying physical and chemical properties. The focus is on understanding how biological molecules, such as proteins, nucleic acids, and lipids, interact with each other and with their environment at a molecular level. Thus, biomolecular interactions are a fundamental part of biophysical chemistry. We aim to publish important and exciting studies on protein–protein, protein–DNA, protein–ligand, and receptor–ligand interactions in this Special Issue. Furthermore, manuscripts on biomolecular structure and function, protein folding, and stability are welcome. Publications on innovations in biophysical techniques facilitating further progress in this prominent field of research would, likewise, be appreciated.

This Special Issue is supervised by Dr. Ivo Crnolatac and assisted by our Topical Advisory Panel Member Dr. Rajendra Rohokale  (University of Florida).

Dr. Ivo Crnolatac
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • biophysical chemistry
  • protein–protein interactions
  • protein–DNA interactions
  • protein–ligand interactions
  • receptor–ligand interactions
  • biomolecular structure and function
  • protein folding and stability

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • Reprint: MDPI Books provides the opportunity to republish successful Special Issues in book format, both online and in print.

Further information on MDPI's Special Issue policies can be found here.

Related Special Issue

Published Papers (1 paper)

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

Research

14 pages, 3713 KiB  
Article
Titin’s Intrinsically Disordered PEVK Domain Modulates Actin Polymerization
by Áron Gellért Altorjay, Hedvig Tordai, Ádám Zolcsák, Nikoletta Kósa, Tamás Hegedűs and Miklós Kellermayer
Int. J. Mol. Sci. 2025, 26(14), 7004; https://doi.org/10.3390/ijms26147004 - 21 Jul 2025
Viewed by 212
Abstract
The multi-domain muscle protein titin provides elasticity and mechanosensing functions to the sarcomere. Titin’s PEVK domain is intrinsically disordered due to the presence of a large number of prolines and highly charged residues. Although PEVK does not have canonical actin-binding motifs, it has [...] Read more.
The multi-domain muscle protein titin provides elasticity and mechanosensing functions to the sarcomere. Titin’s PEVK domain is intrinsically disordered due to the presence of a large number of prolines and highly charged residues. Although PEVK does not have canonical actin-binding motifs, it has been shown to bind F-actin. Here, we explored whether the PEVK domain may also affect actin assembly. We cloned the middle, 733-residue-long segment (called PEVKII) of the full-length PEVK domain, expressed in E. coli and purified by using His- and Avi-tags engineered to the N- and C-termini, respectively. Actin assembly was monitored by the pyrene assay in the presence of varying PEVKII concentrations. The structural features of PEVKII-associated F-actin were studied with atomic force microscopy. The added PEVKII enhanced the initial and log-phase rates of actin assembly and the peak F-actin quantity in a concentration-dependent way. However, the critical concentration of actin polymerization was unaltered. Thus, PEVK accelerates actin polymerization by facilitating its nucleation. This effect was highlighted in the AFM images of F-actin–PEVKII adsorbed to the supported lipid bilayer. The sample was dominated by radially symmetric complexes of short actin filaments. PEVK’s actin polymerization-modulating effect may, in principle, have a function in regulating sarcomeric actin length and turnover. Altogether, titin’s PEVK domain is not only a non-canonical actin-binding protein that regulates sarcomeric shortening, but one that may modulate actin polymerization as well. Full article
(This article belongs to the Special Issue Biomolecular Structure, Function and Interactions: 2nd Edition)
Show Figures

Figure 1

Back to TopTop