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8.3
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Biomolecules
Special Issues
Dynamic Biomolecular Complexes
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Dynamic Biomolecular Complexes

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Chemical Biology".

Deadline for manuscript submissions: closed (30 September 2021) | Viewed by 2614

Special Issue Editor

Prof. Dr. Steven R. Van Doren

E-Mail Website
Guest Editor
Department of Biochemistry, University of Missouri-Columbia, Columbia, SC 29501, USA
Interests: structural biology; NMR investigations of protein structure; dynamics and protein-protein interactions; particularly proteins important in inflammatory diseases
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Dynamic biomolecular associations shape biological communication and action. Fluctuating associations pair proteins, well-structured or intrinsically disordered, with other proteins, nucleic acids, carbohydrates, membranes, and ligands. The nature of dynamic assemblies have been elucidated in solution, e.g. by NMR, FRET, crosslinking mass spectrometry, cryo-EM, SAXS, computational, and integrative approaches.

This Special Issue will report achievements, experimental strategies, and dynamic structural insights into molecular recognition and function.

Dr. Steven Van Doren
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. Biomolecules 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 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

  • biomolecular recognition
  • biomolecular dynamics
  • protein-protein interactions
  • protein-nucleic acid interactions
  • protein-bilayer interactions
  • biomolecular assemblies
  • intrinsic disorder
  • Nuclear magnetic resonance (NMR)
  • small-angle X-ray or neutron scattering (SAXS/SANS)
  • crosslinking mass spectrometry
  • integrative methods

Published Papers (1 paper)

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Research

12 pages, 2285 KiB  
Article
Kinetic Constraints in the Specific Interaction between Phosphorylated Ubiquitin and Proteasomal Shuttle Factors
by Ling-Yun Qin, Zhou Gong, Kan Liu, Xu Dong and Chun Tang
Biomolecules 2021, 11(7), 1008; https://doi.org/10.3390/biom11071008 - 10 Jul 2021
Cited by 2 | Viewed by 2044
Abstract
Ubiquitin (Ub) specifically interacts with the Ub-associating domain (UBA) in a proteasomal shuttle factor, while the latter is involved in either proteasomal targeting or self-assembly coacervation. PINK1 phosphorylates Ub at S65 and makes Ub alternate between C-terminally relaxed (pUbRL [...] Read more.
Ubiquitin (Ub) specifically interacts with the Ub-associating domain (UBA) in a proteasomal shuttle factor, while the latter is involved in either proteasomal targeting or self-assembly coacervation. PINK1 phosphorylates Ub at S65 and makes Ub alternate between C-terminally relaxed (pUbRL) and retracted conformations (pUbRT). Using NMR spectroscopy, we show that pUbRL but not pUbRT preferentially interacts with the UBA from two proteasomal shuttle factors Ubqln2 and Rad23A. Yet discriminatorily, Ubqln2-UBA binds to pUb more tightly than Rad23A does and selectively enriches pUbRL upon complex formation. Further, we determine the solution structure of the complex between Ubqln2-UBA and pUbRL and uncover the thermodynamic basis for the stronger interaction. NMR kinetics analysis at different timescales further suggests an indued-fit binding mechanism for pUb-UBA interaction. Notably, at a relatively low saturation level, the dissociation rate of the UBA-pUbRL complex is comparable with the exchange rate between pUbRL and pUbRT. Thus, a kinetic constraint would dictate the interaction between Ub and UBA, thus fine-tuning the functional state of the proteasomal shuttle factors. Full article
(This article belongs to the Special Issue Dynamic Biomolecular Complexes)
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