Point mutations alter the mechanical stability of immunoglobulin modules

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

Research output: Contribution to journalArticle

170 Citations (Scopus)

Abstract

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
Volume7
Issue number12
DOIs
StatePublished - 2000
Externally publishedYes

Fingerprint

Mechanical stability
Point Mutation
Cell Adhesion
Immunoglobulins
Connectin
Phenotype
Protein Engineering
Muscle Proteins
Protein Stability
Atomic Force Microscopy
Cell adhesion
Elasticity
Muscle Cells
Proteins
Mutation
Muscle
Atomic force microscopy
Molecules

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Li, H., Carrion-Vazquez, M., Oberhauser, A., 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

Point mutations alter the mechanical stability of immunoglobulin modules. / Li, H.; Carrion-Vazquez, M.; Oberhauser, Andres; Marszalek, P. E.; Fernandez, J. M.

In: Nature Structural Biology, Vol. 7, No. 12, 2000, p. 1117-1120.

Research output: Contribution to journalArticle

Li, H, Carrion-Vazquez, M, Oberhauser, A, Marszalek, PE & Fernandez, JM 2000, 'Point mutations alter the mechanical stability of immunoglobulin modules', Nature Structural Biology, vol. 7, no. 12, pp. 1117-1120. https://doi.org/10.1038/81964
Li, H. ; Carrion-Vazquez, M. ; Oberhauser, Andres ; Marszalek, P. E. ; Fernandez, J. M. / Point mutations alter the mechanical stability of immunoglobulin modules. In: Nature Structural Biology. 2000 ; Vol. 7, No. 12. pp. 1117-1120.
@article{46ffc92be15e42129df4a5e2c49e9918,
title = "Point mutations alter the mechanical stability of immunoglobulin modules",
abstract = "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.",
author = "H. Li and M. Carrion-Vazquez and Andres Oberhauser and Marszalek, {P. E.} and Fernandez, {J. M.}",
year = "2000",
doi = "10.1038/81964",
language = "English (US)",
volume = "7",
pages = "1117--1120",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "12",

}

TY - JOUR

T1 - Point mutations alter the mechanical stability of immunoglobulin modules

AU - Li, H.

AU - Carrion-Vazquez, M.

AU - Oberhauser, Andres

AU - Marszalek, P. E.

AU - Fernandez, J. M.

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0033669185&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033669185&partnerID=8YFLogxK

U2 - 10.1038/81964

DO - 10.1038/81964

M3 - Article

VL - 7

SP - 1117

EP - 1120

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 12

ER -