Structural Biology: Mechanisms, Technologies, and Insights

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Biochemistry, Biophysics and Computational Biology".

Deadline for manuscript submissions: 30 November 2026 | Viewed by 1061

Special Issue Editors


E-Mail Website
Guest Editor
Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA, USA
Interests: structural biology; conformational dynamics; cryo-EM; immune receptor signaling; antibody engineering

E-Mail Website
Guest Editor Assistant
Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA, USA
Interests: HDX-MS; thermodynamics; membrane proteins; ion channels

E-Mail Website
Guest Editor Assistant
Department of Pathology, University of California San Francisco, San Francisco, CA, USA
Interests: Integrin; NMR; protein conformational dynamic

Special Issue Information

Dear Colleagues,

Understanding the relationship between protein structure and biological function remains central to modern life sciences. Recent advances in structural biology, particularly cryo-electron microscopy (cryo-EM), NMR spectroscopy, HDX-MS (Hydrogen/Deuterium Exchange Mass Spectrometry), and integrative methods, have offered unprecedented and detailed insights into protein dynamics and allosteric mechanisms. These tools reveal not only static snapshots but also conformational landscapes that underpin molecular recognition, signaling, and catalysis. In parallel, the integration of structural data with functional assays and computational modeling has greatly expanded the impact of the field.

This Special Issue aims to showcase cutting-edge research in structural biology and mechanistic discoveries and insights. We welcome original research articles, perspectives, and reviews that address fundamental principles or translational advances. Topics of interest include, but are not limited to, conformational dynamics, structure-guided drugs, antibody design, macromolecular assemblies, and new frontiers in cryo-EM, NMR, and HDX methodology.

By presenting recent trends and integrative approaches, this Special Issue will provide a timely resource for researchers across biochemistry, molecular biology, biophysics, and biomedical sciences.

Dr. Mingliang Jin
Guest Editor

Dr. Xiaoxuan Lin
Dr. Hoa Nguyen
Guest Editor Assistants

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. 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.

Keywords

  • protein structure
  • allosteric regulation
  • protein dynamics
  • structure-guided therapeutics
  • structural methodology

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.

Published Papers (1 paper)

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

Research

11 pages, 1613 KB  
Article
Structural Analysis of Human LonP1 Protease Bound with the Native Substrate
by Ming Li, Hongwei Liu, Shengchun Zhang, Qijun Gao, Shanshan Li, Junfeng Wang and Kaiming Zhang
Life 2026, 16(3), 478; https://doi.org/10.3390/life16030478 - 16 Mar 2026
Viewed by 640
Abstract
The human mitochondrial Lon protease (LonP1) is a central regulator of mitochondrial DNA copy number and metabolic reprogramming. However, the structural basis for how LonP1 recognizes native physiological substrates remains elusive. Here, we present the high-resolution cryo-EM structure of the human LonP1 hexamer [...] Read more.
The human mitochondrial Lon protease (LonP1) is a central regulator of mitochondrial DNA copy number and metabolic reprogramming. However, the structural basis for how LonP1 recognizes native physiological substrates remains elusive. Here, we present the high-resolution cryo-EM structure of the human LonP1 hexamer actively engaging its native substrate, TFAM. The reconstruction reveals a distinct bipartite search-and-shred mechanism. Unlike its bacterial homologs, the human N-terminal domain (NTD) adopts a compact architecture acting as a selective vestibule to recruit and initially unfold the substrate tertiary structure. Subsequently, the polypeptide is threaded through the central channel via a hand-over-hand mechanism driven by a spiral array of aromatic pore-loops. This structural framework provides a mechanistic rationale for the spatial segregation of LonP1 and offers a template for targeting mitochondrial proteostasis in human diseases. Full article
(This article belongs to the Special Issue Structural Biology: Mechanisms, Technologies, and Insights)
Show Figures

Figure 1

Back to TopTop