| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10537672 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2012 | 6 Pages |
Abstract
⺠Structural response of binding of different pA3X, including natural one, is uniform. ⺠Homodimer formation increases β-sheet and decreases α-helical content. ⺠α-β structural switch probably fixes domain positions during the homodimer formation. ⺠At least 3 Tyr, 5 Phe and 2 Trp participate in homodimer formation upon 2-5A binding.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Martin KÅÞ, Jan SnáÅ¡el, VladimÃr Jr., OndÅej Páv, Ivan Rosenberg, Josef Å tÄpánek,