Host-guest scale of left-handed polyproline II helix formation

Despite the clear importance of the left‐handed polyproline II (PPII) helical conformation in many physiologically important processes as well as its potential significance in protein unfolded states, little is known about the physical determinants of this conformation. We present here a scale of re...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2003-10, Vol.53 (1), p.68-75
Main Authors: Rucker, Adam L., Pager, Cara T., Campbell, Margaret N., Qualls, Joseph E., Creamer, Trevor P.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Hydrogen-Ion Concentration
Peptides - chemistry
proline-rich sequences
Protein Structure, Secondary
protein-protein interactions
unfolded proteins
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Summary:Despite the clear importance of the left‐handed polyproline II (PPII) helical conformation in many physiologically important processes as well as its potential significance in protein unfolded states, little is known about the physical determinants of this conformation. We present here a scale of relative PPII helix‐forming propensities measured for all residues, except tyrosine and tryptophan, in a proline‐based host peptide system. Proline has the highest measured propensity in this system, a result of strong steric interactions that occur between adjacent prolyl rings. The other measured propensities are consistent with backbone solvation being an important component in PPII helix formation. Side chain to backbone hydrogen bonding may also play a role in stabilizing this conformation. The PPII helix‐forming propensity scale will prove useful in future studies of the conformational properties of proline‐rich sequences as well as provide insights into the prevalence of PPII helices in protein unfolded states. Proteins 2003. © 2003 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/prot.10477