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-Structure paper
| Title | Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability. |
|---|---|
| Journal, issue, pages | Sci Rep, Vol. 6, Page 25559-25559, Year 2016 |
| Publish date | Jul 8, 2015 (structure data deposition date) |
Authors | Camilloni, C. / Sala, B.M. / Sormanni, P. / Porcari, R. / Corazza, A. / De Rosa, M. / Zanini, S. / Barbiroli, A. / Esposito, G. / Bolognesi, M. ...Camilloni, C. / Sala, B.M. / Sormanni, P. / Porcari, R. / Corazza, A. / De Rosa, M. / Zanini, S. / Barbiroli, A. / Esposito, G. / Bolognesi, M. / Bellotti, V. / Vendruscolo, M. / Ricagno, S. |
External links | Sci Rep / PubMed:27150430 |
| Methods | X-ray diffraction |
| Resolution | 1.49 - 1.75 Å |
| Structure data | ![]() PDB-5cfh: ![]() PDB-5cka: ![]() PDB-5ckg: |
| Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-GOL: ![]() ChemComp-ACT: ![]() ChemComp-PEG: |
| Source |
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Keywords | IMMUNE SYSTEM / Aggregation propensity / Amyloid / beta-sandwitch / fold stability |
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homo sapiens (human)
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