Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Design of Crystalline Helices of Short Oligopeptides as a Possible Model for Nucleation of α-Helix: Role of Water Molecules in Stabilizing Helices

R. Parthasarathy, Sanjeev Chaturvedi and Kuantee Go
Proceedings of the National Academy of Sciences of the United States of America
Vol. 87, No. 3 (Feb., 1990), pp. 871-875
Stable URL: http://www.jstor.org/stable/2353728
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Design of Crystalline Helices of Short Oligopeptides as a Possible Model for Nucleation of α-Helix: Role of Water Molecules in Stabilizing Helices
Preview not available

Abstract

We have designed, synthesized, crystallized, and performed x-ray analysis of several hydrophobic tripeptides that show an extended near α-helical structure in the crystalline state. All of the tripeptides that show this remarkably stable helix crystallize with two or three water molecules; they all have glycine at the N terminus and have increasing hydrophobicity as one moves from the N to C terminus. Even though three residues in the oligomer are not sufficient to complete a turn, one of the water molecules acts as an added residue and links up adjacent tripeptide segments along the helix axis so that in the crystal, the helix appears effectively as one long continuous helix. Two of these tripeptides are stabilized by two water molecules that enable the peptides to complete a turn of the helix and extend the helical structure throughout the crystal by linking translationally related peptides by hydrogen bonds. In two other peptides, these roles are played by three rather than two water molecules. Though these tripeptides have different crystal symmetry, they all show the basic pattern of hydrated helix and packing, indicating the strong conformational preference for a stable structure even for these tripeptides. Such conformationally stable hydrated structures for short specific related sequences illustrate their possible importance in nucleating protein folding and in the role water molecules play in such events.

Page Thumbnails

  • Thumbnail: Page 
871
    871
  • Thumbnail: Page 
872
    872
  • Thumbnail: Page 
873
    873
  • Thumbnail: Page 
874
    874
  • Thumbnail: Page 
875
    875