AFM of biological complexes: What can we learn?

Research output: Contribution to journalReview articlepeer-review

49 Scopus citations


The term "biological complexes" broadly encompasses particles as diverse as multisubunit enzymes, viral capsids, transport cages, molecular nets, ribosomes, nucleosomes, biological membrane components and amyloids. The complexes represent a broad range of stability and composition. Atomic force microscopy offers a wealth of structural and functional data about such assemblies. For this review, we choose to comment on the significance of AFM to study various aspects of biology of selected non-membrane protein assemblies. Such particles are large enough to reveal many structural details under the AFM probe. Importantly, the specific advantages of the method allow for gathering dynamic information about their formation, stability or allosteric structural changes critical for their function. Some of them have already found their way to nanomedical or nanotechnological applications. Here we present examples of studies where the AFM provided pioneering information about the biology of complexes, and examples of studies where the simplicity of the method is used toward the development of potential diagnostic applications.

Original languageEnglish (US)
Pages (from-to)351-367
Number of pages17
JournalCurrent Opinion in Colloid and Interface Science
Issue number5
StatePublished - Oct 2008


  • Allostery
  • Amyloid
  • Atomic force microscopy
  • GroEL
  • Nanomedicine
  • Protein complexes
  • Protein structure
  • proteasome

ASJC Scopus subject areas

  • Polymers and Plastics
  • Surfaces and Interfaces
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry


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