NDLI: Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Bujalowski, Paul J. Oberhauser, Andres F.
Description	Country affiliation: United States Author Affiliation: Bujalowski PJ ( Department of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, TX 77555, USA.)
Abstract	During the last two decades single-molecule manipulation techniques such as atomic force microscopy (AFM) has risen to prominence through their unique capacity to provide fundamental information on the structure and function of biomolecules. Here we describe the use of single-molecule AFM to track protein unfolding and refolding pathways, enzymatic catalysis and the effects of osmolytes and chaperones on protein stability and folding. We will outline the principles of operation for two different AFM pulling techniques: length clamp and force-clamp and discuss prominent applications. We provide protocols for the construction of polyproteins which are amenable for AFM experiments, the preparation of different coverslips, choice and calibration of AFM cantilevers. We also discuss the selection criteria for AFM recordings, the calibration of AFM cantilevers, protein sample preparations and analysis of the obtained data.
File Format	HTM / HTML
ISSN	10462023
e-ISSN	10959130
DOI	10.1016/j.ymeth.2013.03.010
Journal	Methods
Issue Number	2
Volume Number	60
Language	English
Publisher	Elsevier
Publisher Date	2013-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Life sciences, Biochemistry Microscopy, Atomic Force Polyproteins Chemistry Protein Refolding Protein Unfolding Calibration Computer Simulation Immobilized Proteins Ultrastructure Mechanical Phenomena Models, Molecular Osmolar Concentration Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Molecular Biology

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Tracking Unfolding and Refolding Reactions of Single Proteins using Atomic Force Microscopy Methods

Monte Carlo simulation of mechanical unfolding of proteins based on a simple two-state model.

Elasticity, structure, and relaxation of extended proteins under force.

Atomic force microscopy with sub-picoNewton force stability for biological applications.

Stepwise unfolding of titin under force-clamp atomic force microscopy.

Probing osmolyte participation in the unfolding transition state of a protein.

Protein structure by mechanical triangulation.

Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.

Mechanical biochemistry of proteins one molecule at a time.

Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.

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Tracking Unfolding and Refolding Reactions of Single Proteins using Atomic Force Microscopy Methods

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