Acid-Induced Denaturation of Myoglobin Studied by Time-Resolved Electrospray Ionization Mass Spectrometry †
✍ Scribed by Konermann, L.; Rosell, F. I.; Mauk, A. G.; Douglas, D. J.
- Book ID
- 127319044
- Publisher
- American Chemical Society
- Year
- 1997
- Tongue
- English
- Weight
- 154 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0006-2960
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
Application of electrospray mass spectrometry (ES/MS) to a protein refolding study was demonstrated. Acid denaturation of equine myoglobin was reversed by adding various amounts of ammonium hydroxide to the protein that was unfolded in 10% acetic acid. The protein refolding process was followed by E
## Abstract The association properties of natural and non‐natural amino acids were studied in detail using electrospray ionization mass spectrometry. The results show a highly diverse cluster formation behavior of amino acids. There are differences regarding the degree of clustering (average cluste
The thermal stability of ribonuclease S (RNase S), an enzymatically active noncovalent complex composed of a 2166-u peptide (S-peptide) and a 11,534-u protein (S-protein), was investigated by electrospray ionization mass spectrometry (ESI-MS) and capillary electrophoresis ESI-MS (CE-ESI-MS). The int