Point mutations alter the mechanical stability of immunoglobulin modules

H. Li, M. Carrion-Vazquez, A. F. Oberhauser, P. E. Marszalek, J. M. Fernandez

Research output: Contribution to journalArticlepeer-review

193 Scopus citations


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 β-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.

Original languageEnglish (US)
Pages (from-to)1117-1120
Number of pages4
JournalNature Structural Biology
Issue number12
StatePublished - 2000
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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