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Crystals
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Biomolecular Crystals Characterization by Powder Diffraction
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Biomolecular Crystals Characterization by Powder Diffraction

A special issue of Crystals (ISSN 2073-4352). This special issue belongs to the section "Biomolecular Crystals".

Deadline for manuscript submissions: closed (15 July 2021) | Viewed by 4275

Special Issue Editors

Dr. Ryan Taoran Wang

E-Mail Website
Guest Editor
Material Science and Engineering with Energy Material, McMaster University, Hamilton, Hamilton, ON L8S4L8, Canada
Interests: organic–inorganic functional crystals; bioelectronic devices
Dr. Yi Feng

E-Mail Website
Guest Editor
Material Science and Engineering with energy material, McMaster University, Hamilton, Hamilton, ON L8S4L8, Canada
Interests: solidification; casting; hot tearing; multi-physics simulation
Dr. Ya-Dong Yu

E-Mail Website
Guest Editor
Material Science and Engineering with energy material, McMaster University, Hamilton, Hamilton, ON L8S4L8, Canada
Interests: coordination complexes; organometallic crystals
Prof. Dr. Eliana B. Souto

E-Mail Website
Guest Editor
Professor of Pharmaceutical Technology, Faculty of Pharmacy, University of Porto, 4099-002 Porto, Portugal
Interests: drug delivery; drug targeting; active pharmaceutical ingredients; volatile compounds; encapsulation
Special Issues, Collections and Topics in MDPI journals
Dr. Yan V. Zubavichus

E-Mail Website
Guest Editor
Siberian Branch of the Russian Academy of Sciences, Boreskov Institute of Catalysis, 630090 Novosibirsk, Russia
Interests: synchrotron radiation; instrumentation development; in situ crystallography; defects and disorder

Special Issue Information

Dear Colleagues,

Organic materials have been widely applied in many research fields, including biosensing/bioimaging devices, organic catalysts, and functional materials. However, the application of organics depends largely on the crystalline properties of such materials, which are much more complex than in other crystalline materials. For example, the characterization of the crystal structure of the SARS-CoV-2 virus spike has been greatly hindered not only as a result of its unknown crystalline properties, but also because of the damage the instrument may cause. Therefore, the advancement of the characterization of organic and biomolecular crystals by powder XRD, cryo-electron microscope, etc., is worthy of further investigation.

This Special Issue focuses on the recent development of the characterization of organic and biomolecular crystals. We would like to invite you to submit your original research articles and reviews to this Special Issue

Dr. Ryan Taoran Wang
Dr. Yi Feng
Dr. Ya-Dong Yu
Prof. Dr. Eliana B. Souto
Dr. Yan V. Zubavichus
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 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. Crystals 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

  • Biomaterials
  • Bioengineering
  • Metallic crystals
  • Organic crystals
  • Crystal structure simulation.

Published Papers (2 papers)

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Research

13 pages, 6948 KiB  
Article
Crystalline S-Layer Protein Monolayers Induce Water Turbulences on the Nanometer Scale
by Rupert Tscheliessnig, Andreas Breitwieser, Uwe B. Sleytr and Dietmar Pum
Crystals 2021, 11(9), 1147; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst11091147 - 20 Sep 2021
Viewed by 1638
Abstract
Bacterial surface layers (S-layers) have been observed as the outermost cell envelope component in a wide range of bacteria and most archaea. They are one of the most common prokaryotic cell surface structures and cover the cells completely. It is assumed that S-layers [...] Read more.
Bacterial surface layers (S-layers) have been observed as the outermost cell envelope component in a wide range of bacteria and most archaea. They are one of the most common prokaryotic cell surface structures and cover the cells completely. It is assumed that S-layers provide selection advantages to prokaryotic cells in their natural habitats since they act as protective envelopes, as structures involved in cell adhesion and surface recognition, as molecular or ion traps, and as molecular sieves in the ultrafiltration range. In order to contribute to the question of the function of S-layers for the cell, we merged high-resolution cryo-EM and small-angle X-ray scattering datasets to build a coarse-grained functional model of the S-layer protein SbpA from Lysinibacillus sphaericus ATCC 4525. We applied the Navier–Stokes and the Poisson equations for a 2D section through the pore region in the self-assembled SbpA lattice. We calculated the flow field of water, the vorticity, the electrostatic potential, and the electric field of the coarse-grained model. From calculated local changes in the flow profile, evidence is provided that both the characteristic rigidity of the S-layer and the charge distribution determine its rheological properties. The strength of turbulence and pressure near the S-layer surface in the range of 10 to 50 nm thus support our hypothesis that the S-layer, due to its highly ordered repetitive crystalline structure, not only increases the exchange rate of metabolites but is also responsible for the remarkable antifouling properties of the cell surface. In this context, studies on the structure, assembly and function of S-layer proteins are promising for various applications in nanobiotechnology, biomimetics, biomedicine, and molecular nanotechnology. Full article
(This article belongs to the Special Issue Biomolecular Crystals Characterization by Powder Diffraction)
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10 pages, 1863 KiB  
Article
Binding Strength and Hydrogen Bond Numbers between COVID-19 RBD and HVR of Antibody
by Ryan Taoran Wang, Alex Fan Xu, Qi Zhou, Tinglu Song, Kelvin J. Xu and Gu Xu
Crystals 2021, 11(8), 997; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst11080997 - 21 Aug 2021
Cited by 4 | Viewed by 2022
Abstract
The global battle against the COVID-19 pandemic relies strongly on the human defense of antibody, which is assumed to bind the antigen’s receptor binding domain (RBD) with its hypervariable region (HVR). Due to the similarity to other viruses such as SARS, however, our [...] Read more.
The global battle against the COVID-19 pandemic relies strongly on the human defense of antibody, which is assumed to bind the antigen’s receptor binding domain (RBD) with its hypervariable region (HVR). Due to the similarity to other viruses such as SARS, however, our understanding of the antibody-virus interaction has been largely limited to the genomic sequencing, which poses serious challenges to containment and rapid serum testing. Based on the physical/chemical nature of the interaction, infrared spectroscopy was employed to reveal the binding disparity, the real cause of the antibody-virus specificity at the molecular level, which is inconceivable to be investigated otherwise. Temperature dependence was discovered in the absorption value from the 1550 cm−1 absorption band, attributed to the hydrogen bonds by carboxyl/amino groups, binding the SARS-CoV-2 spike protein and closely resembled SARS-CoV-2 or SARS-CoV-1 antibodies. The infrared absorption intensity, associated with the number of hydrogen bonds, was found to increase sharply between 27 °C and 31 °C, with the relative absorbance matching the hydrogen bonding numbers of the two antibody types (19 vs. 12) at 37 °C. Meanwhile, the ratio of bonds at 27 °C, calculated by thermodynamic exponentials, produces at least 5% inaccuracy. Beyond genomic sequencing, the temperature dependence, as well as the bond number match at 37 °C between relative absorbance and the hydrogen bonding numbers of the two antibody types, is not only of clinical significance in particular but also as a sample for the physical/chemical understanding of vaccine–antibody interactions in general. Full article
(This article belongs to the Special Issue Biomolecular Crystals Characterization by Powder Diffraction)
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