Atomic force microscopy captures length phenotypes in single proteins

Mariano Carrion-Vazquez, Piotr E. Marszalek, Andres Oberhauser, Julio M. Fernandez

Research output: Contribution to journalArticle

149 Citations (Scopus)

Abstract

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 Å 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.

Original languageEnglish (US)
Pages (from-to)11288-11292
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number20
DOIs
StatePublished - Sep 28 1999
Externally publishedYes

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Polyproteins
Atomic Force Microscopy
Phenotype
Crystallography
Proteins
Glycine
X-Rays
Amino Acids

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Atomic force microscopy captures length phenotypes in single proteins. / Carrion-Vazquez, Mariano; Marszalek, Piotr E.; Oberhauser, Andres; Fernandez, Julio M.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 20, 28.09.1999, p. 11288-11292.

Research output: Contribution to journalArticle

Carrion-Vazquez, Mariano ; Marszalek, Piotr E. ; Oberhauser, Andres ; Fernandez, Julio M. / Atomic force microscopy captures length phenotypes in single proteins. In: Proceedings of the National Academy of Sciences of the United States of America. 1999 ; Vol. 96, No. 20. pp. 11288-11292.
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