Short Sequences of Non-Proline Residues Can Adopt the Polyproline II Helical Conformation

Brian W. Chellgren, Trevor P. Creamer

Research output: Contribution to journalArticlepeer-review

94 Scopus citations

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 languageEnglish
Pages (from-to)5864-5869
Number of pages6
JournalBiochemistry
Volume43
Issue number19
DOIs
StatePublished - May 18 2004

ASJC Scopus subject areas

  • Biochemistry

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