Special Issue "Advanced Research on Structure–Function Relationships of Membrane Proteins"
Deadline for manuscript submissions: 31 July 2021.
Interests: structure–function relationships of ion pump membrane proteins; photoreaction pathways of retinal-binding membrane proteins; membrane-bound structure of antimicrobial peptides; amyloid fibril formation mechanism; development of solid-state NMR spectroscopy
Interests: biological solid-state NMR; microbial rhodopsins; antimicrobial peptides; D-amino acid-containing peptides; membrane
Membrane proteins embedded in biological membranes account for 30% of the proteins encoded in the human genome and play an essential role in maintaining the homeostasis of cells by functioning as transporters and in signal transaction and energy conversion, amongst other functions, and knowledge of the atomic resolution structure of membrane proteins is extremely important to understanding their functions. However, it is difficult to determine the structure of membrane proteins at the atomic resolution, as compared with soluble proteins, because of the difficulty of their crystallization.
Recent developments in the methodology of structure determination are providing high-resolution structures of membrane proteins, and a number of high-resolution structures of membrane proteins have been reported (~4% of PDB). Solid-state NMR spectroscopy does not require crystallization and is not restricted by the upper limits to molecular weight. Solution state NMR spectroscopy is recently used to determine structure of membrane proteins using nanodisc as a membrane mimic system. For X-ray crystallography, it is becoming possible to determine structures of membrane proteins by using membrane or membrane mimic systems to form the crystals. The recently developed time-resolved method allows determining the structure of short-lived intermediates of membrane proteins. Attention is now being focused on cryo-electron microscopy as a powerful method to determine the structure of membrane proteins using two-dimensional crystals. The determination of membrane protein structure based on single-molecule observation has also recently become possible.
This Special Issue will focus on advanced studies on structure–function relationships using advanced methods to determine the high-resolution structures of membrane proteins, including developments in methodology. Within the scope of this Special Issue are not only determinations of complete structure but also of local structure changes and the dynamic properties of membrane proteins.
Prof. Dr. Akira Naito
Prof. Dr. Izuru Kawamura
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 papers will be 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. Membranes 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 1800 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.
- membrane protein structure
- membrane protein transporters
- signal transduction
- energy conversion
- solid-state NMR
- solution-state NMR
- X-ray crystallography
- cryo-electron microscopy