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Low-Frequency Protein Motions Coupled to Catalytic Sites
Journal article   Open access   Peer reviewed

Low-Frequency Protein Motions Coupled to Catalytic Sites

Christopher M Cheatum
Annual review of physical chemistry, Vol.71(1), pp.267-288
04/20/2020
DOI: 10.1146/annurev-physchem-050317-014308
PMID: 32312192
url
https://doi.org/10.1146/annurev-physchem-050317-014308View
Published (Version of record) Open Access

Abstract

This review examines low-frequency vibrational modes of proteins and their coupling to enzyme catalytic sites. That protein motions are critical to enzyme function is clear, but the kinds of motions present in proteins and how they are involved in function remain unclear. Several models of enzyme-catalyzed reaction suggest that protein dynamics may be involved in the chemical step of the catalyzed reaction, but the evidence in support of such models is indirect. Spectroscopic studies of low-frequency protein vibrations consistently show that there are underdamped modes of the protein with frequencies in the tens of wavenumbers where overdamped behavior would be expected. Recent studies even show that such underdamped vibrations modulate enzyme active sites. These observations suggest that increasingly sophisticated spectroscopic methods will be able to unravel the link between low-frequency protein vibrations and enzyme function.
 Catalysis Catalytic Domain Enzymes - chemistry Enzymes - metabolism Humans Models, Chemical Molecular Dynamics Simulation Protein Conformation Protein Folding Proteins - chemistry Proteins - metabolism

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