Abstract
Reports concerning anomalous rates of exchange of some amides in oxytocin, alumichrome, and gramicidin S are reexamined through systematic analysis of the exchange data as a function of pH and primary structure. It is shown that such an analysis can provide useful information on secondary structure when the degree of hydrogen bonding to both the NH undergoing exchange and the neighboring carbonyl group are taken into consideration.
Original language | English (US) |
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Pages (from-to) | 42-47 |
Number of pages | 6 |
Journal | International Journal of Peptide and Protein Research |
Volume | 17 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1981 |
Externally published | Yes |
Keywords
- alumichrome
- base catalysis of hydrogen exchange
- effect of hydrogen‐bonding on peptide hydrogen exchange
- gramicidin S
- hydrogen exchange rates
- oxytocin
- peptide conformation
ASJC Scopus subject areas
- Biochemistry