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Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry.

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...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.2000.4142

Authors


Nettleton, EJ More by this author
Robinson, CV More by this author
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

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