Raman spectroscopic studies of pig skin proteodermatan sulfate in H,O are indicative of a well defined secondary structure consisting of a-helical, P-turn, and possibly "random" structures. The above conclusion is surprisingly close to the secondary structure of the "core" protein of pig skin proteo
Conformational Modularity of an Abiotic Secondary-Structure Motif in Aqueous Solution
✍ Scribed by Andrew J. Zych; Brent L. Iverson
- Publisher
- John Wiley and Sons
- Year
- 2002
- Tongue
- German
- Weight
- 164 KB
- Volume
- 85
- Category
- Article
- ISSN
- 0018-019X
No coin nor oath required. For personal study only.
✦ Synopsis
Dedicated to Dieter Seebach on the occasion of his 65th birthday
We have investigated an abiotic secondary structure based on the stacking of alternating electron-rich (1,5dialkoxynaphthalene (Dan)) and electron-deficient (1,4,5,8-naphthalene-tetracarboxylic diimide (Ndi) benzo [lmn][3,8]phenanthroline-1,3,6,8(2H,7H)-tetrone) aromatic units. Previously, the specifics of conformational behavior were uncovered in the minimal folding unit, namely the dimer, consisting of one Dan and one Ndi unit linked through various amino acid residues. Here is reported the investigation of a series of larger oligomers (trimers and tetramers) composed of selected dimer units. We determined that some of the larger oligomers displayed conformational modularity, that is, the persistence of subunit-conformational propensities when those subunits were used as components of larger structures. Conformational modularity can be viewed as a desirable property of folding molecules because it simplifies not only the design of larger, more complex oligomers, but also the structural analyses of such species.
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