| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10537175 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 11 Pages |
Abstract
⺠We studied the structure-function of the Hsp90 of L. braziliensis (LbHsp90). ⺠LbHsp90 is an elongated dimer in solution. ⺠The N-domain and NM-domains constructions of the LbHsp90 were monomers. ⺠The LbHsp90 affinity for adenosine nucleotides and geldanamycin were determined. ⺠ATPase activity depends on LbHsp90 as dimer and was inhibited by geldanamycin.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
K.P. Silva, T.V. Seraphim, J.C. Borges,