Molecular Conformational Diversity
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Chemical Biology".
Deadline for manuscript submissions: 28 February 2027 | Viewed by 8
Special Issue Editors
Interests: protein structure; protein folding; protein misfolding; intrinsically disordered proteins; conformational disease; partially folded protein; folding intermediate; protein aggregation
Special Issues, Collections and Topics in MDPI journals
Interests: structural biology; solution NMR: conformational analyses of proteins, peptides; self-assembling peptides: structural analyses; solution NMR: interaction studies [(protein–protein (PPIs)/protein–ligand (=peptides and small molecules) interactions]; NMR techniques in drug discovery; design and evaluation of PPI modulators; structure-based drug design; molecular modelling and docking; Sam domains; EphA2 receptor; cancer
Special Issues, Collections and Topics in MDPI journals
Special Issue Information
Dear Colleagues,
This Special Issue of Molecules will showcase recent advances in our understanding of the importance of molecular conformational diversity. Recent years witnessed the shift from a "static" single-structure paradigm to a "dynamic" ensemble-based understanding of molecules. This paradigm shift highlights that proteins, RNA, and other biomolecules exist as populations of rapidly interconverting conformers (conformational ensembles) rather than a single, fixed, 3D structure. It represents a critical advancement in understanding biological function, since conformational diversity (i.e., the range of 3D orientations a molecule adopts without breaking covalent bonds) is essential for mediating molecular recognition, enzymatic catalysis, and allosteric regulation, as these functions often rely on the ability of a molecule to transition between different functional states.
The shift from a static to a dynamic view impacts several key areas of research, ranging from protein folding and misfolding to protein interactions via induced fit and conformational selection, to analysis of intrinsically disordered proteins, and to development of new approaches for drug discovery and protein engineering. In fact, understanding that proteins exist in a landscape of energy minima helps explain how they transition from functional states to pathological ones (such as amyloid fibrils in Alzheimer’s disease). Furthermore, rather than a simple "lock-and-key" model, where a rigid ligand fits a rigid protein, the "conformational selection" model suggests that all functional conformations pre-exist, and a ligand selects and stabilizes the most favored state. This is often combined with "induced fit", where the protein further adjusts to the ligand, highlighting that binding is a population shift rather than a static event. Often, the ability to flip between different conformations is essential for enzyme catalysis, signal transduction, and molecular recognition and many proteins are known to transition between "closed" (active) and "open" (inactive) conformations, and the balance of this ensemble determines activity. Furthermore, many proteins or regions of proteins are intrinsically disordered (IDRs/IDRs). They do not adopt a stable 3D structure but are still functional, acting as high-speed signaling hubs that can interact with multiple partners and demonstrating that high structural flexibility and malleability allows for diverse regulatory and signaling interactions. Furthermore, understanding the full conformational landscape allows for the identification of rare "excited" states (transient, higher-energy conformations) that are critical for drug targeting and protein engineering.
This Special Issue of Molecules will highlight how these dynamic perspectives are reshaping our approach to molecular recognition and function. We invite original research articles that explore molecular conformational diversity of peptides, proteins, nucleic acids, polysaccharides, and related biopolymers. Submissions from diverse disciplines—including biochemistry, biophysics, bioconjugation, biomaterials, bioorganic chemistry, chemical biology, protein design, supramolecular assembly, and structural biology—are welcome, provided they are relevant to the core chemical focus of this Special Issue.
Prof. Dr. Vladimir N. Uversky
Dr. Marilisa Leone
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 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. Molecules is an international peer-reviewed open access semimonthly 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
- conformational diversity
- conformational ensemble
- conformational flexibility
- conformational sampling
- energy landscape
- protein dynamics
- structural heterogeneity
- intrinsically disordered proteins
- molecular recognition
- ligand binding
- protein–protein interactions
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