Hydrogen‐bonded conformation of hyaluronate oligosaccharide fragments in aqueous solution
- 25 July 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 158 (2) , 305-309
- https://doi.org/10.1016/0014-5793(83)80601-2
Abstract
The hydrogen bonding in hyaluronate oligosaccharide fragments was studied in aqueous solution using hydrogen‐tritium exchange techniques. The data reveal an acetamido hydrogen exchange rate that is 5–6‐fold slower than that seen in model compounds. The magnitude of the slowing is interpreted as reflecting the participation of an acetamido hydrogen in a relatively labile intramolecular hydrogen bond.Keywords
This publication has 16 references indexed in Scilit:
- Hydrogen-bonded structure of the complex N-linked fetuin glycopeptideBiochemistry, 1981
- Preparation and circular dichroism analysis of sodium hyaluronate oligosaccharides and chondroitinBiochemistry, 1981
- Competitive inhibition evidence for specific intermolecular interactions in hyaluronate solutionsJournal of Molecular Biology, 1980
- Conformation and dynamic interactions in hyaluronate solutionsJournal of Molecular Biology, 1980
- Hydrogen Exchange Kinetics and Internal Motions in Proteins and Nucleic AcidsAnnual Review of Biophysics and Bioengineering, 1979
- Hydrogen ExchangeAnnual Review of Biochemistry, 1972
- [19] Hydrogen-tritium exchangePublished by Elsevier ,1972
- Hydrogen‐tritium exchange of the random chain polypeptideBiopolymers, 1969
- Hydrogen Exchange in ProteinsAdvances in Protein Chemistry, 1966
- Separation of acidic oligosaccharides by gel filtrationAnalytical Biochemistry, 1964