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What measurements of energy transfer across non-covalent contacts in proteins reveal about the energy landscape
Date
2023-11-27Type
ArticleAbstract
Determining rates of energy transfer across non-covalent contacts in a protein can provide information about dynamics of the contact at equilibrium. We investigate the relation between rates of energy transfer across polar contacts and contact dynamics for the WW domain, dominated by beta-strands, and compare with previous results for the helical villin headpiece subdomain, HP36. Overall, rates of energy transfer across hydrogen bonded contacts are found to be inversely proportional to the variance of the length of the contact. Due to the proportionality, change in dynamics of a non-covalent contact, and entropy associated with the dynamics, arising from change in state of the protein or mutation can be estimated from the measurement of change in the rate of energy transfer across the contact.