The small transcriptional repressor CopG protein (45 amino acids) encoded by the streptococcal plasmid pMV158 was purified to near homogeneity. Gel filtration chromatography and analytical ultracentrifugation showed that the native protein is a spherical dimer of identical subunits. Circular dichroi
✦ LIBER ✦
Electric Field-Driven Disruption of a Native β-Sheet Protein Conformation and Generation of a Helix-Structure
✍ Scribed by Ojeda-May, Pedro; Garcia, Martin E.
- Book ID
- 119207316
- Publisher
- Biophysical Society
- Year
- 2010
- Tongue
- English
- Weight
- 531 KB
- Volume
- 99
- Category
- Article
- ISSN
- 0006-3495
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## Abstract The depsipeptides Boc‐Leu‐Lac‐OEt (1) and Boc‐(Leu‐Leu‐Lac)~__n__~‐OEt (__n__ = 1, 2) (**2** and **3**, respectively) (Boc = __tert__‐butyloxycarbonyl, Lac = L‐lactic acid residue) has been synthesized and studied by crystallographic, CD spectroscopic, and ESI‐MS analyses. In the packin