Mechanical unfolding studies of protein molecules

• Taniguchi Yukinori

  School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST)

• Kobayashi Akiko

  School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST)

• Kawakami Masaru

  School of Materials Science, Japan Advanced Institute of Science and Technology (JAIST)

Abstract

Atomic force microscopy (AFM) enables the pick up of a single protein molecule to apply a mechanical force. This technique, called “force spectroscopy,” provides unique information about the intermediates and free energy landscape of the mechanical unfolding of proteins. In this review, we introduce the AFM-based single molecule force spectroscopy of proteins and describe recent studies that answer some fundamental questions such as “is the mechanical resistance of proteins isotropic?”, “what is the structure of the transition state in mechanical unfolding?”, and “is mechanical unfolding related to biological functions?”<br>

Journal

• BIOPHYSICS

  BIOPHYSICS 8 51-58, 2012

  The Biophysical Society of Japan

Keywords

• protein folding
• dynamic force spectroscopy
• free energy landscape
• φ-value analysis
• single-molecule measurement

Details

• CRID: 1390001205223139584
• NII Article ID: 130002061597
• DOI: 10.2142/biophysics.8.51
• ISSN: 13492942
• Web Site: http://www.jstage.jst.go.jp/article/biophysics/8/0/8_0_51/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed