Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/8060
Title: The Realm of Unconventional Noncovalent Interactions in Proteins: Their Significance in Structure and Function
Authors: ADHAV, VISHAL ANNASAHEB
KAYARAT, SAIKRISHNAN
Dept. of Biology
Keywords: Molecular interactions
Monomers
Noncovalent interactions
Peptides and proteins
Protein structure
2023-JUN-WEEK4
TOC-JUN-2023
2023
Issue Date: Jun-2023
Publisher: American Chemical Society
Citation: ACS Omega, 8(25), 22268–22284.
Abstract: Proteins and their assemblies are fundamental for living cells to function. Their complex three-dimensional architecture and its stability are attributed to the combined effect of various noncovalent interactions. It is critical to scrutinize these noncovalent interactions to understand their role in the energy landscape in folding, catalysis, and molecular recognition. This Review presents a comprehensive summary of unconventional noncovalent interactions, beyond conventional hydrogen bonds and hydrophobic interactions, which have gained prominence over the past decade. The noncovalent interactions discussed include low-barrier hydrogen bonds, C5 hydrogen bonds, C–H···π interactions, sulfur-mediated hydrogen bonds, n → π* interactions, London dispersion interactions, halogen bonds, chalcogen bonds, and tetrel bonds. This Review focuses on their chemical nature, interaction strength, and geometrical parameters obtained from X-ray crystallography, spectroscopy, bioinformatics, and computational chemistry. Also highlighted are their occurrence in proteins or their complexes and recent advances made toward understanding their role in biomolecular structure and function. Probing the chemical diversity of these interactions, we determined that the variable frequency of occurrence in proteins and the ability to synergize with one another are important not only for ab initio structure prediction but also to design proteins with new functionalities. A better understanding of these interactions will promote their utilization in designing and engineering ligands with potential therapeutic value.
URI: https://doi.org/10.1021/acsomega.3c00205
http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/8060
ISSN: 2470-1343
Appears in Collections:JOURNAL ARTICLES

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