Special Issue "Recent Advances in Chiroptical Spectroscopy"
Deadline for manuscript submissions: 31 May 2018
Prof. Dr. Reiko Kuroda
Research Institute for Science and Technology, Tokyo University of Science, 2641 Yamazaki,Noda-shi, Chiba 278-8510 Japan
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Interests: chiroptical spectroscopy especially in the condensed phase; chiral recognition, discrimination and enhancement in the solid state; chirality determination mechanism of snail Lymnaea stagnalis by a single gene during the embryogenesis
Chirality is expressed throughout nature, whether microscopic or macroscopic, and animate or inanimate. Examples include molecules, crystals and complex living organisms. From the molecular standpoint, life is totally homochiral; that is, all living organisms on Earth use molecules of a unique invariant handedness: only D- (deoxy) ribose in nucleic acids and only L-amino acids in proteins. Thus, chirality is a key issue in understanding the origin of life on Earth, as well as in agricultural, pharmaceutical and food industries as their biological effects often depend on the chirality of compounds.
The present Special Issue, “Recent Advances in Chiroptical Spectroscopy”, aims to provide comprehensive coverage of the most important and up-to-date methods dealing with polarized light, including their basic principles, instrumentation, and theoretical simulation for application to organic molecules, inorganic molecules, and biomolecules.
Prof. Dr. Reiko Kuroda
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. Molecules 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.
- Instrumentation (condensed phases, fast measurements etc.)
- Theoretical approaches
- Biomolecules (proteins/peptides/lipids/nucleic acids/sugars etc.)
- Organic compounds/liquid crystals/supramolecules
- Inorganic compounds (transition metal complexes, lanthanides etc.)
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Author: Rohanah Hussain (Harwell Science Innovation Campus, UK)
Abstract: High photon flux in the vacuum and far UV region is known to denature/degrade biopolymers. Measures are in place at Diamond Light Source Synchrotron Radiation Circular Dichroism (SRCD) B23 beamline to control and make this effect negligible. However, UV denaturation/degradation can also be exploited as a novel method for assessing biopolymer stability as well as ligand binding interactions. Usually host-ligand binding interactions can be assessed monitoring CD changes of the host upon ligand addition. The novel method of identifying ligand binding monitoring the change of relative UV denaturation using SRCD is especially important when there are very little or insignificant secondary structure changes of the host protein upon ligand binding. The temperature study, another method used to determine molecular interactions can often be inconclusive when the thermal effect, associated with the displacement of the bound solvent molecules by the ligand is also small making the determination of the binding interaction inconclusive. Here we present a review on the novel protein stability and ligand binding assay methods using the high photon flux of SRCD B23 beamline and to discriminate the relative stability of different types of protein folding in different formulations and also in the presence of ligands.