Chalcogen bond interactions involving sulphur atoms of methionine or cysteine residues and backbone carbonyl oxygen atoms in protein structures

P. R. SINGH; V. Ramanathan; Ramasubbu Sankararamakrishnan

doi:10.1039/d5cp04735h

January 1, 2026Physical Chemistry Chemical Physics

Chalcogen bond interactions involving sulphur atoms of methionine or cysteine residues and backbone carbonyl oxygen atoms in protein structures

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Key Points

This research aims to explore chalcogen bond interactions involving sulfur atoms from methionine and cysteine residues and their interactions with carbonyl oxygen atoms in proteins.
Analyzed structural data of proteins to identify chalcogen bond formations.
Examined interactions of sulfur atoms in selected amino acids with backbone carbonyl groups.
Identified significant chalcogen bond interactions impacting protein stability and function.
Demonstrated the role of methionine and cysteine residues in forming stable non-covalent interactions.

Implication

Investigates chalcogen bonds affecting protein structures, indicating their significance in molecular interactions.

Abstract

Chalcogen bonds (ChBs) are attractive non-covalent interactions that occur between group 16 elements and nucleophiles and many studies have investigated ChBs in various chemical systems. The strength and significance of...

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Cite This Study

SINGH et al. (2026) studied this question.

synapsesocial.com/papers/69ec5ae988ba6daa22dac731 https://doi.org/10.1039/d5cp04735h

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Chalcogen bond interactions involving sulphur atoms of methionine or cysteine residues and backbone carbonyl oxygen atoms in protein structures

Key Points

Implication

Abstract

Discussion

Cite This Study

Chalcogen bond interactions involving sulphur atoms of methionine or cysteine residues and backbone carbonyl oxygen atoms in protein structures

Key Points

Implication

Abstract

Discussion

Cite This Study

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