Analysis of the structure of empty and peptide-loaded major histocompatibility complex molecules at the cell surface
We compared the conformation of empty and peptide-loaded class I major histocompatibility complex (MHC) molecules at the cell surface. Molecular conformations were analyzed by fluorescence resonance energy transfer (FRET) between fluorescent-labeled Fab fragments bound to the alpha 2 domain of the M...
Format: | Online |
---|---|
Language: | English |
Published: |
The Rockefeller University Press
1994
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191740/ |