Atomic force microscopy reveals the mechanical design of a modular protein

Hongbin Li, Andres Oberhauser, Susan B. Fowler, Jane Clarke, Julio M. Fernandez

Research output: Contribution to journalArticle

229 Citations (Scopus)

Abstract

Tandem modular proteins underlie the elasticity of natural adhesives, cell adhesion proteins, and muscle proteins. The fundamental unit of elastic proteins is their individually folded modules. Here, we use protein engineering to construct multimodular proteins composed of Ig modules of different mechanical strength. We examine the mechanical properties of the resulting tandem modular proteins by using single protein atomic force microscopy. We show that by combining modules of known mechanical strength, we can generate proteins with novel elastic properties. Our experiments reveal the simple mechanical design of modular proteins and open the way for the engineering of elastic proteins with defined mechanical properties, which can be used in tissue and fiber engineering.

Original languageEnglish (US)
Pages (from-to)6527-6531
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume97
Issue number12
DOIs
StatePublished - Jun 6 2000
Externally publishedYes

Fingerprint

Atomic Force Microscopy
Proteins
Protein Engineering
Muscle Proteins
Elasticity
Tissue Engineering
Cell Adhesion
Adhesives

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Atomic force microscopy reveals the mechanical design of a modular protein. / Li, Hongbin; Oberhauser, Andres; Fowler, Susan B.; Clarke, Jane; Fernandez, Julio M.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 97, No. 12, 06.06.2000, p. 6527-6531.

Research output: Contribution to journalArticle

Li, Hongbin ; Oberhauser, Andres ; Fowler, Susan B. ; Clarke, Jane ; Fernandez, Julio M. / Atomic force microscopy reveals the mechanical design of a modular protein. In: Proceedings of the National Academy of Sciences of the United States of America. 2000 ; Vol. 97, No. 12. pp. 6527-6531.
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