| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10763114 | Biochemical and Biophysical Research Communications | 2011 | 5 Pages |
Abstract
⺠Amyloid-beta (1-40) is partially folded at 15 °C, pH 7.3 in 50 mM NaCl. ⺠Amyloid-beta (1-40) forms a 310 helix from H13 to D23. ⺠N- and C-termini are unstructured but collapse against the helix. ⺠Low temperature and moderate salt conformations may favor helical conformations of amyloid-beta (1-40).
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Authors
Subramanian Vivekanandan, Jeffrey R. Brender, Shirley Y. Lee, Ayyalusamy Ramamoorthy,