Imaging and detecting molecular interactions of single transmembrane proteins

Harald Janovjak, Alexej Kedrov, David A. Cisneros, K. Tanuj Sapra, Jens Struckmeier, Daniel J. Muller

Research output: Contribution to journalReview articlepeer-review

32 Citations (Scopus)


Single-molecule atomic force microscopy (AFM) provides novel ways to characterize structure-function relationships of native membrane proteins. High-resolution AFM-topographs allow observing substructures of single membrane proteins at sub-nanometer resolution as well as their conformational changes, oligomeric state, molecular dynamics and assembly. Complementary to AFM imaging, single-molecule force spectroscopy experiments allow detecting molecular interactions established within and between membrane proteins. The sensitivity of this method makes it possible to detect the interactions that stabilize secondary structures such as transmembrane α-helices, polypeptide loops and segments within. Changes in temperature or protein-protein assembly do not change the position of stable structural segments, but influence their stability established by collective molecular interactions. Such changes alter the probability of proteins to choose a certain unfolding pathway. Recent examples have elucidated unfolding and refolding pathways of membrane proteins as well as their energy landscapes. We review current and future potential of these approaches to reveal insights into membrane protein structure, function, and unfolding as we recognize that they could help answering key questions in the molecular basis of certain neuro-pathological dysfunctions.

Original languageEnglish
Pages (from-to)546-561
Number of pages16
JournalNeurobiology of Aging
Issue number4
Publication statusPublished - Apr 2006
Externally publishedYes


  • Antiporter
  • Aquaporin-1
  • Atomic force microscopy
  • Bacteriorhodopsin
  • Folding
  • Force spectroscopy
  • Membrane proteins
  • Single-molecule experiments
  • Unfolding


Dive into the research topics of 'Imaging and detecting molecular interactions of single transmembrane proteins'. Together they form a unique fingerprint.

Cite this