Major histocompatibility complex class I protein conformation altered by transmembrane potential changes

Research output: Contribution to journalArticle

25 Citations (Scopus)


The nature of charge distributions in membrane-bound macromolecular structures renders them susceptible to interaction with transmembrane potential fields. As a result, conformational changes in such species may be expected to occur when this potential is altered. We have detected reversible conformational change in the major histocompatibility complex (MHC) class I antigen in the plasma membrane of human JY cells, as monitored by flow-cytometric resonance energy transfer, upon reduction of the transmembrane potential (depolarization). This change increased the intramolecular energy-transfer efficiency between fluorescent donor- and acceptor-labeled monoclonal antibodies directed, respectively, to epitopes on the light (β2-microglobulin) and the heavy chains of the MHC class I antigen. Repolarization of the depolarized samples restored the energy-transfer efficiency to the original values measured before depolarization, Depolarization caused similar relative changes in fluorescence resonance energy-transfer efficiency when Fab fragments were used for labeling MHC class I complex, suggesting that the observed phenomenon is not restricted to whole monoclonal antibodies.

Original languageEnglish
Pages (from-to)353-357
Number of pages5
Issue number4
Publication statusPublished - Apr 1 1997


  • Fluorescence resonance energy transfer
  • MHC conformation
  • Major histocompatibility complex (MHC) class I complex
  • Membrane potential

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Biophysics
  • Hematology
  • Endocrinology
  • Cell Biology

Fingerprint Dive into the research topics of 'Major histocompatibility complex class I protein conformation altered by transmembrane potential changes'. Together they form a unique fingerprint.

  • Cite this