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Updated: Jul 26, 2026
11:37
Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Energetic asymmetry among hydrogen bonds in MHC class II*peptide complexes
B J McFarland1, J F Katz, C Beeson
1Department of Chemistry, University of Washington, Seattle, WA 98195, USA.
Summary
Hydrogen bonds at the amino terminus of peptides profoundly stabilize their interaction with MHC class II molecules. This binding network is crucial for regulating peptide dissociation, impacting immune responses.
Area of Science:
- Immunology
- Structural Biology
- Biochemistry
Background:
- Peptide binding to MHC class II molecules involves side chain interactions and hydrogen bonds.
- Conserved hydrogen bonds are observed at both ends of the MHC class II antigen-binding groove.
Purpose of the Study:
- To investigate the contribution of peripheral hydrogen bonds to the kinetic stability of peptide-MHC class II complexes.
- To determine the specific role of hydrogen bonds at the peptide's amino terminus.
Main Methods:
- Conservative amino acid substitutions were introduced into the I-A(d) protein to disrupt hydrogen bonding.
- Kinetic stability of diverse peptides bound to modified I-A(d) proteins was measured.
Main Results:
- All tested hydrogen bonds contribute to peptide binding.
- Hydrogen bonds at the peptide's amino terminus disproportionately enhance the stability of peptide-MHC class II interactions.
- These terminal hydrogen bonds form a critical regulatory network for peptide dissociation.
Conclusions:
- The amino-terminal hydrogen bonding network is essential for the stability of peptide binding to MHC class II.
- This network plays a critical role in regulating the dissociation kinetics of peptides from MHC class II molecules.
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