Biophysical Characterization and Molecular Engineering of Multidomain Proteins 3.0

Dear Colleagues,

This Special Issue is the continuation of our previous Special Issues "Biophysical Characterization and Molecular Engineering of Multidomain Proteins" and “Biophysical Characterization and Molecular Engineering of Multidomain Proteins 2.0”

Most proteins working in living systems consist of evolutionarily acquired multiple domains, which cooperate with one another and exhibit synergistic actions, thereby exerting sophisticated functions typified by allosteric regulations. Structural proteomics, in conjunction with bioinformatics, have achieved the systematic classification and prediction of tertiary structures of individual domains as globular structural units. However, it remains challenging to delineate or predict the overall conformations of multidomain proteins, primarily because of their dynamic properties. In this class of proteins, the globular domains are connected through flexible linkers and, consequently, are mobile to a greater or lesser extent, which enables variable spatial arrangements of the domains, depending on their cognate ligands or binding partners, as well as solution conditions such as pH. Therefore, to elucidate the mechanisms underlying multidomain protein functions, applications of experimental and theoretical methods are necessary in order to provide dynamic views of domain–domain interactions. This line of approach will offer a structural basis for the design and engineering of multidomain proteins.

As the guest editors of this Special Issue, titled “Biophysical Characterization and Molecular Engineering of Multidomain Proteins 3.0”, in IJMS, we welcome contributions from various research fields, including biophysics, bioinformatics, biomolecular engineering, and molecular phylogenetics. Formats for submissions include original research reports, reviews/mini-reviews, perspectives/opinions, and methodology articles.

Prof. Dr. Koichi Kato
Prof. Dr. Takayuki Uchihashi
Guest Editors

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