Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR
✍ Scribed by Evonne W. Chung; Ewan J. Nettleton; Charles J. Morgan; Michael Groß; Andrew Miranker; Sheena E. Radford; Christopher M. Dobson; Carol V. Robinson
- Book ID
- 118285875
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 1997
- Tongue
- English
- Weight
- 913 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0961-8368
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The rates at which hydrogens located at peptide amide linkages in proteins undergo isotopic exchange when a protein is exposed to depend on whether these amide hydrogens are hydrogen bonded and whether they are D 2 O accessible to the aqueous solvent. Hence, amide hydrogen exchange rates are a sensi
Apocytochrome c, the in vivo precursor to active cytochrome c, was analyzed by amide hydrogen exchange and mass spectrometry to search for fixed, non-covalent structure. The protein was incubated in H 2 O at pH 3.3 or 6.7 for various times, then exposed to D 2 O to initiate isotope labeling of unfol