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Seminar

Recording of Folding /unfolding Reactions in Single Proteins by AFM Techniques

Julio M. Fernandez, Ph.D.
Department of Physiology and Biophysics
Mayo Clinic
Rochester, MN 55905

Monday, April 13, 1998
3:00 pm
3269 Beckman Institute

We combine biophysical and molecular biological techniques in order to examine the molecular basis of the elasticity of modular proteins. Towards this aim we use recently developed Atomic Force Microscopy (AFM) techniques that are capable of observing conformational changes in single proteins. We have studied the elastic properties of tandem repeats of immunoglobulin and fibronectin type III (FN-III) domains isolated from the proteins titin and tenascin, respectively. Our measurements examine the conformational changes that allow these domains to reversibly extend under an applied force. We reproduce our experimental observations of the elasticity of Ig and FN-III domains with a simple Monte Carlo simulation of a tandem repeat of Markovian elements that follow the worm like chain model of polymer elasticity.