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Point mutations alter the mechanical stability of immunoglobulin modules.

Publication ,  Journal Article
Li, H; Carrion-Vazquez, M; Oberhauser, AF; Marszalek, PE; Fernandez, JM
Published in: Nature structural biology
December 2000

Immunoglobulin-like modules are common components of proteins that play mechanical roles in cells such as muscle elasticity and cell adhesion. Mutations in these proteins may affect their mechanical stability and thus may compromise their function. Using single molecule atomic force microscopy (AFM) and protein engineering, we demonstrate that point mutations in two beta-strands of an immunoglobulin module in human cardiac titin alter the mechanical stability of the protein, resulting in mechanical phenotypes. Our results demonstrate a previously unrecognized class of phenotypes that may be common in cell adhesion and muscle proteins.

Duke Scholars

Published In

Nature structural biology

DOI

ISSN

1072-8368

Publication Date

December 2000

Volume

7

Issue

12

Start / End Page

1117 / 1120

Related Subject Headings

  • Thermodynamics
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Renaturation
  • Protein Kinases
  • Protein Folding
  • Protein Denaturation
  • Proline
  • Point Mutation
  • Phenotype
 

Citation

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MLA
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Li, H., Carrion-Vazquez, M., Oberhauser, A. F., Marszalek, P. E., & Fernandez, J. M. (2000). Point mutations alter the mechanical stability of immunoglobulin modules. Nature Structural Biology, 7(12), 1117–1120. https://doi.org/10.1038/81964
Li, H., M. Carrion-Vazquez, A. F. Oberhauser, P. E. Marszalek, and J. M. Fernandez. “Point mutations alter the mechanical stability of immunoglobulin modules.Nature Structural Biology 7, no. 12 (December 2000): 1117–20. https://doi.org/10.1038/81964.
Li H, Carrion-Vazquez M, Oberhauser AF, Marszalek PE, Fernandez JM. Point mutations alter the mechanical stability of immunoglobulin modules. Nature structural biology. 2000 Dec;7(12):1117–20.
Li, H., et al. “Point mutations alter the mechanical stability of immunoglobulin modules.Nature Structural Biology, vol. 7, no. 12, Dec. 2000, pp. 1117–20. Epmc, doi:10.1038/81964.
Li H, Carrion-Vazquez M, Oberhauser AF, Marszalek PE, Fernandez JM. Point mutations alter the mechanical stability of immunoglobulin modules. Nature structural biology. 2000 Dec;7(12):1117–1120.

Published In

Nature structural biology

DOI

ISSN

1072-8368

Publication Date

December 2000

Volume

7

Issue

12

Start / End Page

1117 / 1120

Related Subject Headings

  • Thermodynamics
  • Protein Structure, Tertiary
  • Protein Structure, Secondary
  • Protein Renaturation
  • Protein Kinases
  • Protein Folding
  • Protein Denaturation
  • Proline
  • Point Mutation
  • Phenotype