| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Department of Biological Sciences, Columbia University, New York, New York 10027
Correspondence: Address reprint requests and inquiries to Atom Sarkar, E-mail: atom.sarkar{at}osumc.edu; or Julio M. Fernandez, E-mail: jfernandez{at}columbia.edu.
We use the GCN4 oligomerization domain to engineer a covalently linked parallel polyprotein dimer based on the well-studied I27 domain of titin. We use single molecule atomic force microscopy techniques to stretch single polyprotein fibers and verify their mechanical properties. We find that the engineered polyprotein dimers extend in perfect register, doubling the unfolding force and halving the persistence length while keeping the contour length increase unchanged. These experiments directly confirm the mechanical scaling laws proposed for parallel bundles of modular proteins.
This article has been cited by other articles:
![]() |
A. F. Oberhauser and M. Carrion-Vazquez Mechanical Biochemistry of Proteins One Molecule at a Time J. Biol. Chem., March 14, 2008; 283(11): 6617 - 6621. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |