Journal ArticleDOI
The interaction of Naphthol Yellow S (NYS) with pepsin: Insights from spectroscopic to molecular dynamics studies.
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TLDR
The experimental results from fluorescence spectroscopy showed that the changes in pepsin's tertiary structure were caused by NYS binding, and NYS could be considered as an inhibitor with adverse effects on pepingin structure and function.About:
This article is published in International Journal of Biological Macromolecules.The article was published on 2020-12-15. It has received 46 citations till now. The article focuses on the topics: Naphthol yellow S & Circular dichroism.read more
Citations
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Evaluation of interactions between food colorant, tartrazine, and Apo-transferrin using spectroscopic analysis and docking simulation
TL;DR: The tartrazine occurrence was investigated in Iranian cooked rice and confectioneries by HPLC-DAD using different spectroscopic and simulation methods as discussed by the authors, which revealed spontaneous interactions between tartrazines and Apo-transferrin, hydrogen bond and van der Waals forces most certainly played seminal roles.
Journal ArticleDOI
The interaction of the green tea polyphenol (catechin) with pepsin: Insights from spectroscopic to molecular dynamics studies
TL;DR: Pepsin is an aspartic proteinase that plays an essential role in controlling many biological processes, therapy, and pharmaceutical research, and catechin hydrate could be considered as an inhibitor with adverse effects on pepsin structure and function.
Journal ArticleDOI
Effect of Naphthol yellow S as a food dye on the lysozyme structure and its mechanisms of action
TL;DR: Molecular dynamics simulation was carried out to assess the stability of the lyso enzyme- NYS complex with RMSD, showing that hydrogen-bonding and van der Waals contributions played an essential role in binding NYS to lysozyme.
Journal ArticleDOI
Characterizing the binding affinity and molecular interplay between quinoline yellow and pepsin
TL;DR: The data indicated Qy had a high binding constant and thereby affect the structure and function of pepsin, and hydrogen bonds and Van der Waals interactions were the dominant forces in the formation of the pepsIn-Qy complex.
References
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Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI
Development and testing of a general amber force field.
TL;DR: A general Amber force field for organic molecules is described, designed to be compatible with existing Amber force fields for proteins and nucleic acids, and has parameters for most organic and pharmaceutical molecules that are composed of H, C, N, O, S, P, and halogens.
Journal ArticleDOI
Thermodynamics of protein association reactions: forces contributing to stability
Philip D. Ross,S. Subramanian +1 more
TL;DR: On the basis of the thermochemical behavior of small molecule interactions, it is concluded that the strengthening of hydrogen bonds in the past decade, a complete thermodynamic description of the self-association of many proteins and their interactions is concluded.
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Quantitation of protein.
TL;DR: This chapter discusses various methods of estimating protein concentration as defined by the difference in energy between the orbital of the unexcited electron and a higher energy orbital.
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Quantifying the chemical beauty of drugs
TL;DR: The utility of QED is extended by applying it to the problem of molecular target druggability assessment by prioritizing a large set of published bioactive compounds and may also capture the abstract notion of aesthetics in medicinal chemistry.
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Thermodynamics of protein association reactions: forces contributing to stability
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