| Autor: |
Leszcynski, Jerzy, Sokalski, W. Andrzej, Renugopalakrishnan, V. |
| Zdroj: |
Molecular Materials with Specific Interactions - Modeling & Design; 2007, p433-451, 19p |
| Abstrakt: |
The folding and stability of bacteriorhodopsin remains of great interest in view of its technological importance. Single molecules of bacteriorhodopsin are unfolded by attaching them to the tip of an AFM probe and then applying force 50 pico Newtons can be pulled one or more at a time. These experiments provide force profiles of individual chains which exhibit dependence and independence on rest of the helices until all of them are unfolded. Unlike differential scanning calorimetric studies which provide the global thermodynamic profile of proteins, AFM dynamic force probe methods provide a wealth of force profiles of the individual chains at a single molecule level which can then be reconstituted to map the energy landscape of bacteriorhodopsin. Energy landscape of bacteriorhodopsin from dynamic force probe method using atomic force spectroscopy is reviewed in this chapter [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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