Related Experiment Video
Updated: Jul 15, 2026

Designing Silk-silk Protein Alloy Materials for Biomedical Applications
Published on: August 13, 2014
Evidence for the preservation of specific intermolecular interactions in gaseous protein-oligosaccharide complexes
Elena N Kitova1, David R Bundle, John S Klassen
1Department of Chemistry, University of Alberta, Edmonton, Canada T6G 2G2.
Abstract:
Arrhenius parameters, obtained with the blackbody infrared radiative dissociation technique, are reported for the dissociation of a series of gaseous protonated complexes composed of mutants of a single chain variable fragment (scFv) of the monoclonal antibody Se155-4 and three trisaccharide ligands. Hydrogen bonding between a ligand and a particular amino acid residue is identified from a comparison of activation energies measured for the complex of the unmodified scFv and the corresponding mutant. It is shown that the specific hydrogen bond between His(101H) and Man C-4 OH is preserved in the gaseous complex.
Related Concept Videos
Chemistry of Carbohydrates
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Sugars as Energy Storage Molecules
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Sugars as Energy Storage Molecules

