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Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy

Title: Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy
Authors: Marc Rico-Pasto; Annamaria Zaltron; Sebastian J. Davis; Silvia Frutos; Felix Ritort
Contributors: Rico-Pasto, Marc; Zaltron, Annamaria; Davis, Sebastian J.; Frutos, Silvia; Ritort, Felix
Publisher Information: National Academy of Sciences
Publication Year: 2022
Collection: Padua Research Archive (IRIS - Università degli Studi di Padova)
Subject Terms: folding; molten globule; protein; thermodynamic; transition state
Description: Understanding how proteins fold into their native structure is a fundamental problem in biophysics, crucial for protein design. It has been hypothesized that the formation of a molten globule intermediate precedes folding to the native conformation of globular proteins; however, its thermodynamic properties are poorly known. We perform single-molecule pulling experiments of protein barnase in the range of 7 ◦C to 37 ◦C using a temperature-jump optical trap. We derive the folding free energy, entropy and enthalpy, and heat capacity change (ΔCp = 1,050 ± 50 cal/mol·K) at low ionic strength conditions. From the measured unfolding and folding kinetic rates, we also determine the thermodynamic properties of the transition state, finding a significant change in ΔCp (∼90%) between the unfolded and the transition states. In contrast, the major change in enthalpy (∼80%) occurs between the transition and native states. These results highlight a transition state of high energy and low configurati.
Document Type: article in journal/newspaper
Language: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/35271392; info:eu-repo/semantics/altIdentifier/wos/WOS:000772224400005; volume:119; issue:11; journal:PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA; https://hdl.handle.net/11577/3439497
DOI: 10.1073/pnas.2112382119
Availability: https://hdl.handle.net/11577/3439497; https://doi.org/10.1073/pnas.2112382119
Rights: info:eu-repo/semantics/openAccess
Accession Number: edsbas.EA8548C5
Database: BASE