Point mutations alter the mechanical stability of immunoglobulin modules.

Journal Article, Research Support, Non-U.S. Gov't

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.

Full Text

Duke Authors

Cited Authors

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

Published Date

  • December 2000

Published In

Volume / Issue

  • 7 / 12

Start / End Page

  • 1117 - 1120

PubMed ID

  • 11101892

International Standard Serial Number (ISSN)

  • 1072-8368

Digital Object Identifier (DOI)

  • 10.1038/81964

Language

  • eng

Citation Source

  • PubMed