You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis 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
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2353728
Page Count: 5
You can always find the topics here!Topics: Molecules, Crystals, Crystal structure, Nucleation, Oligomers, Hydrogen bonds, Amino acids, Biophysics, Molecular structure, Hydrophobicity
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
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.
Preview not available
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.
Proceedings of the National Academy of Sciences of the United States of America © 1990 National Academy of Sciences