Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy

Alexej Kedrov, Harald Janovjak, K. Tanuj Sapra, Daniel J. Müller

Research output: Contribution to journalReview ArticleResearchpeer-review

102 Citations (Scopus)

Abstract

Molecular interactions are the basic language of biological processes. They establish the forces interacting between the building blocks of proteins and other macromolecules, thus determining their functional roles. Because molecular interactions trigger virtually every biological process, approaches to decipher their language are needed. Single-molecule force spectroscopy (SMFS) has been used to detect and characterize different types of molecular interactions that occur between and within native membrane proteins. The first experiments detected and localized molecular interactions that stabilized membrane proteins, including how these interactions were established during folding of α-helical secondary structure elements into the native protein and how they changed with oligomerization, temperature, and mutations. SMFS also enables investigators to detect and locate molecular interactions established during ligand and inhibitor binding. These exciting applications provide opportunities for studying the molecular forces of life. Further developments will elucidate the origins of molecular interactions encoded in their life-times, interaction ranges, interplay, and dynamics characteristic of biological systems.

Original languageEnglish
Pages (from-to)233-260
Number of pages28
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume36
DOIs
Publication statusPublished - 2007
Externally publishedYes

Keywords

  • Atomic force microscopy
  • Ligand binding
  • Protein folding
  • Protein unfolding
  • Structure-function

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