Dataset Information

Molecular Dynamics of Jelly Candies by Means of Nuclear Magnetic Resonance Relaxometry.

ABSTRACT: ¹H spin-lattice Nuclear Magnetic Resonance relaxation studies have been performed for different kinds of Haribo jelly and Vidal jelly in a very broad frequency range from about 10 kHz to 10 MHz to obtain insight into the dynamic and structural properties of jelly candies on the molecular level. This extensive data set has been thoroughly analyzed revealing three dynamic processes, referred to as slow, intermediate and fast dynamics occurring on the timescale of 10^-6 s, 10^-7 s and 10^-8 s, respectively. The parameters have been compared for different kinds of jelly for the purpose of revealing their characteristic dynamic and structural properties as well as to enquire into how increasing temperature affects these properties. It has been shown that dynamic processes in different kinds of Haribo jelly are similar (this can be treated as a sign of their quality and authenticity) and that the fraction of confined water molecules is reduced with increasing temperature. Two groups of Vidal jelly have been identified. For the first one, the parameters (dipolar relaxation constants and correlation times) match those for Haribo jelly. For the second group including cherry jelly, considerable differences in the parameters characterizing their dynamic properties have been revealed.

SUBMITTER: Kruk D

PROVIDER: S-EPMC10005792 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature

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Molecular Dynamics of Jelly Candies by Means of Nuclear Magnetic Resonance Relaxometry.

Kruk Danuta D Grunin Leonid L Stankiewicz Aleksandra A Kołodziejski Karol K Ilhan Esmanur E Oztop Mecit Halil MH

Molecules (Basel, Switzerland) 20230227 5

<sup>1</sup>H spin-lattice Nuclear Magnetic Resonance relaxation studies have been performed for different kinds of Haribo jelly and Vidal jelly in a very broad frequency range from about 10 kHz to 10 MHz to obtain insight into the dynamic and structural properties of jelly candies on the molecular level. This extensive data set has been thoroughly analyzed revealing three dynamic processes, referred to as slow, intermediate and fast dynamics occurring on the timescale of 10<sup>-6</sup> s, 10<s ...[more]

PMID: 36903475

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Project description:Protein kinases are ubiquitous enzymes with critical roles in cellular processes and pathology. As a result, researchers have studied their activity and regulatory mechanisms extensively. Thousands of X-ray structures give snapshots of the architectures of protein kinases in various states of activation and ligand binding. However, the extent of and manner by which protein motions and conformational dynamics underlie the function and regulation of these important enzymes is not well understood. Nuclear magnetic resonance (NMR) methods provide complementary information about protein conformation and dynamics in solution. However, until recently, the large size of these enzymes prevented researchers from using these methods with kinases. Developments in transverse relaxation-optimized spectroscopy (TROSY)-based techniques and more efficient isotope labeling strategies are now allowing researchers to carry out NMR studies on full-length protein kinases. In this Account, we describe recent insights into the role of dynamics in protein kinase regulation and catalysis that have been gained from NMR measurements of chemical shift changes and line broadening, residual dipolar couplings, and relaxation. These findings show strong associations between protein motion and events that control kinase activity. Dynamic and conformational changes occurring at ligand binding sites and other regulatory domains of these proteins propagate to conserved kinase core regions that mediate catalytic function. NMR measurements of slow time scale (microsecond to millisecond) motions also reveal that kinases carry out global exchange processes that synchronize multiple residues and allosteric interconversion between conformational states. Activating covalent modifications or ligand binding to form the Michaelis complex can induce these global processes. Inhibitors can also exploit the exchange properties of kinases by using conformational selection to form dynamically quenched states. These investigations have revealed that kinases are highly dynamic enzymes, whose regulation by interdomain interactions, ligand binding, and covalent modifications involve changes in motion and conformational equilibrium in a manner that can be correlated with function. Thus, NMR provides a unique window into the role of protein dynamics in kinase regulation and catalysis with important implications for drug design.

Dataset Information

Molecular Dynamics of Jelly Candies by Means of Nuclear Magnetic Resonance Relaxometry.

Publications

Molecular Dynamics of Jelly Candies by Means of Nuclear Magnetic Resonance Relaxometry.

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