Atomic force microscopy captures length phenotypes in single proteins.


Journal Article

We use single-protein atomic force microscopy techniques to detect length phenotypes in an Ig module. To gain amino acid resolution, we amplify the mechanical features of a single module by engineering polyproteins composed of up to 12 identical repeats. We show that on mechanical unfolding, mutant polyproteins containing five extra glycine residues added to the folded core of the module extend 20 A per module farther than the wild-type polyproteins. By contrast, similar insertions near the N or C termini have no effect. Hence, our atomic force microscopy measurements readily discriminate the location of the insert and measure its size with a resolution similar to that of NMR and x-ray crystallography.

Full Text

Duke Authors

Cited Authors

  • Carrion-Vazquez, M; Marszalek, PE; Oberhauser, AF; Fernandez, JM

Published Date

  • September 1999

Published In

Volume / Issue

  • 96 / 20

Start / End Page

  • 11288 - 11292

PubMed ID

  • 10500169

Pubmed Central ID

  • 10500169

Electronic International Standard Serial Number (EISSN)

  • 1091-6490

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.96.20.11288


  • eng