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Protein is the most exposed biomolecule in the aqueous environment of the cell. Its structure maintains a delicate balance between the rigidity and the flexibility that imparts binding specificity to its substrate/ligand, etc. Intramolecular interactions of polar and non-polar groups of amino acid residues and intermolecular weak interactions between these groups and shell-waters may contribute to the overall stability of the tertiary structure. However, the question as to what are the dynamicsdoi:10.6026/97320630014530 pmid:31223212 pmcid:PMC6563665 fatcat:cd4iqhr5erfwvdtfyftq7ltscu