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Abstract

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY (NMR): A COMPREHENSIVE REVIEW

Anjanalakshmi*, Mitali Dalwadi and Umesh Upadhyay

Abstract

A physicochemical method called nuclear magnetic resonance (NMR) spectroscopy which is used to identify the structural characteristics of molecules. The development of nuclear magnetic resonance (NMR) spectroscopy during the past few decades has been one of the most important developments in analytical methods. NMR has been used to examine a wide variety of biological and nonbiological applications, from a single cell through organs and tissues. Numerous facets of this method are still being investigated, and many NMR functions still need to be clarified and acknowledged. Solid‐state NMR has the ability to characterize motions across a wide range of length and time, as well as to offer structural information with atomic resolution. Molecular dynamics, rotational and translational motions of the constituent parts, as well as the motion of the functional species themselves, such as protons or ions, are all examples of these movements. NMR investigations at high temperatures are used to examine the functional dynamics of ligand and partner protein complexes in a realistic membrane environment. NMR spectroscopy is a relatively new development, yet it is one that has great potential for the future. The method is significant because it offers a methodical way to identify and assess the thermodynamic stability of highenergy substates in proteins for the first time ever. In order to analyze complicated systems, such as membrane proteins, metabolically complex samples, or even biological tissues, scientists have created a wide range of unique approaches. One of the most effective methods for determining the structures of chemical species as well as for researching molecular dynamics and interactions is NMR spectroscopy.

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