- Abstract:
-
We have examined the hydrogen exchange properties of bovine insulin under solution conditions that cause it to aggregate and eventually form amyloid fibrils. The results have been obtained at the residue-specific level using peptic digestion and mass spectrometry. A total of 19 peptides were assigned to regions of the protein and their exchange properties monitored for a period of 24 hours. The results of the peptic digestion show that residues A13 to A21 and B11 to B30 are more susceptible t...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1006/jmbi.2000.4142
-
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- Journal:
- Journal of molecular biology
- Volume:
- 303
- Issue:
- 2
- Pages:
- 267-278
- Publication date:
- 2000-10-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:0a888aeb-8a42-4dd8-af1d-b0176af4060f
- Source identifiers:
-
59230
- Local pid:
- pubs:59230
- Language:
- English
- Keywords:
- Copyright date:
- 2000
Journal article
Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry.
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