Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Force mode microscopy can be used to examine the effect of mechanical manipulation on the noncovalent interactions that stabilize proteins and their complexes. Here we describe the effect of complexation by the high affinity protein ligand E9 on the mechanical resistance of the simple four-helical protein, Im9. When concatenated into a construct of alternating I27 domains, Im9 unfolded below the thermal noise limit of the instrument ( approximately 20 pN). Complexation of E9 had little effect on the mechanical resistance of Im9 (unfolding force approximately 30 pN) despite the high avidity of this complex (K(d) approximately 10 fM).

Original publication

DOI

10.1529/biophysj.106.102475

Type

Journal article

Journal

Biophys J

Publication Date

01/05/2007

Volume

92

Pages

L79 - L81

Keywords

Biomechanical Phenomena, Colicins, Elasticity, Escherichia coli Proteins, Microscopy, Atomic Force, Multiprotein Complexes, Protein Conformation, Protein Denaturation, Stress, Mechanical