Single molecule 'force spectroscopy' techniques (e.g., atomic force microscopy) that measure the force required to unfold a protein and the associated length changes upon unfolding are increasingly utilized to investigate the kinetics and mechanism of protein unfolding. Although force spectroscopy techniques are capable of discerning subnanometer differences in molecular lengths, they are not able to provide a detailed structural view of the unfolding process. The interpretation of force measurements heavily relies on atomistic simulations. In this chapter, we review some of the major contributions of atomistic simulations to the interpretation of force spectroscopy measurements of single domain protein unfolding. © 2012 Elsevier B.V. All rights reserved.

Yew Z.T., Paci E. (2012). Simulation Studies of Force-Induced Unfolding. Oxford : Academic Press [10.1016/B978-0-12-374920-8.00308-8].

Simulation Studies of Force-Induced Unfolding

Paci E.
2012

Abstract

Single molecule 'force spectroscopy' techniques (e.g., atomic force microscopy) that measure the force required to unfold a protein and the associated length changes upon unfolding are increasingly utilized to investigate the kinetics and mechanism of protein unfolding. Although force spectroscopy techniques are capable of discerning subnanometer differences in molecular lengths, they are not able to provide a detailed structural view of the unfolding process. The interpretation of force measurements heavily relies on atomistic simulations. In this chapter, we review some of the major contributions of atomistic simulations to the interpretation of force spectroscopy measurements of single domain protein unfolding. © 2012 Elsevier B.V. All rights reserved.
2012
Comprehensive Biophysics
138
147
Yew Z.T., Paci E. (2012). Simulation Studies of Force-Induced Unfolding. Oxford : Academic Press [10.1016/B978-0-12-374920-8.00308-8].
Yew Z.T.; Paci E.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/885229
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