Atomic force microscopy reveals the mechanical design of a modular protein

Citation
Hb. Li et al., Atomic force microscopy reveals the mechanical design of a modular protein, P NAS US, 97(12), 2000, pp. 6527-6531
Citations number
24
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN journal
00278424 → ACNP
Volume
97
Issue
12
Year of publication
2000
Pages
6527 - 6531
Database
ISI
SICI code
0027-8424(20000606)97:12<6527:AFMRTM>2.0.ZU;2-4
Abstract
Tandem modular proteins underlie the elasticity of natural adhesives, cell adhesion proteins, and muscle proteins. The fundamental unit of elastic pro teins is their individually folded modules. Here, we use protein engineerin g to construct multimodular proteins composed of Ig modules of different me chanical strength. We examine the mechanical properties of the resulting ta ndem modular proteins by using single protein atomic force microscopy. We s how 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 i n tissue and fiber engineering.