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Atomic force microscopy captures length phenotypes in single proteins.

Publication ,  Journal Article
Carrion-Vazquez, M; Marszalek, PE; Oberhauser, AF; Fernandez, JM
Published in: Proceedings of the National Academy of Sciences of the United States of America
September 1999

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.

Duke Scholars

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

September 1999

Volume

96

Issue

20

Start / End Page

11288 / 11292

Related Subject Headings

  • Protein Kinases
  • Protein Folding
  • Protein Engineering
  • Muscle Proteins
  • Microscopy, Atomic Force
  • Connectin
 

Citation

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ICMJE
MLA
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Carrion-Vazquez, M., Marszalek, P. E., Oberhauser, A. F., & Fernandez, J. M. (1999). Atomic force microscopy captures length phenotypes in single proteins. Proceedings of the National Academy of Sciences of the United States of America, 96(20), 11288–11292. https://doi.org/10.1073/pnas.96.20.11288
Carrion-Vazquez, M., P. E. Marszalek, A. F. Oberhauser, and J. M. Fernandez. “Atomic force microscopy captures length phenotypes in single proteins.Proceedings of the National Academy of Sciences of the United States of America 96, no. 20 (September 1999): 11288–92. https://doi.org/10.1073/pnas.96.20.11288.
Carrion-Vazquez M, Marszalek PE, Oberhauser AF, Fernandez JM. Atomic force microscopy captures length phenotypes in single proteins. Proceedings of the National Academy of Sciences of the United States of America. 1999 Sep;96(20):11288–92.
Carrion-Vazquez, M., et al. “Atomic force microscopy captures length phenotypes in single proteins.Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 20, Sept. 1999, pp. 11288–92. Epmc, doi:10.1073/pnas.96.20.11288.
Carrion-Vazquez M, Marszalek PE, Oberhauser AF, Fernandez JM. Atomic force microscopy captures length phenotypes in single proteins. Proceedings of the National Academy of Sciences of the United States of America. 1999 Sep;96(20):11288–11292.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

September 1999

Volume

96

Issue

20

Start / End Page

11288 / 11292

Related Subject Headings

  • Protein Kinases
  • Protein Folding
  • Protein Engineering
  • Muscle Proteins
  • Microscopy, Atomic Force
  • Connectin