Abstract
The left-handed polyproline II (PII) helix is a structure that has been given a great deal of attention lately because of its role in a wide variety of physiologically important processes and potential significance in protein unfolded states. Recent work by several authors has shown that residues besides proline can adopt this structure. A scale of relative P II-helix-forming propensities has been generated but only for single guest residues in a proline-based host system. Here, we present multiple guest residues in a proline-based host system. Using circular dichroism spectroscopy, we have shown that not only single residues, but also short sequences of non-proline residues can adopt the PII conformation.
Original language | English |
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Pages (from-to) | 5864-5869 |
Number of pages | 6 |
Journal | Biochemistry |
Volume | 43 |
Issue number | 19 |
DOIs | |
State | Published - May 18 2004 |
ASJC Scopus subject areas
- Biochemistry