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.
Simulation Studies of Force-Induced Unfolding / Yew Z.T.; Paci E.. - STAMPA. - 3:(2012), pp. 138-147. [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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
