Modular Design of Synthetic Protein Mimics. Characterization of the Helical Conformation of a 13-Residue Peptide in Crystals

Karle, Isabella L and Flippen-Anderson, Judith L and Uma, K and Balaram, P (1989) Modular Design of Synthetic Protein Mimics. Characterization of the Helical Conformation of a 13-Residue Peptide in Crystals. In: Biochemistry, 28 (16). pp. 6696-6701.

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Abstract

The incorporation of \alpha-aminoisobutyryl (Aib) residues into peptide sequences facilitates helical folding. Aib-containing sequences have been chosen for the design of rigid helical segments in a modular approach to the construction of a synthetic protein mimic. The helical conformation of the synthetic peptide Boc-Aib-$(Val-Ala-Leu-Aib)_3$-OMe in crystals is established by X-ray diffraction. The 13-residue apolar peptide adopts a helical form in the crystal with seven \alpha-type hydrogen bonds in the middle and $3_{10}$-type hydrogen bonds at either end. The helices stack in columns, zigzag rather than linear, by means of direct NH…OC head to tail hydrogen bonds. Leucyl side chains are extended on one side of the helix and valyl side chains on the other side. Water molecules form hydrogen bonds with several backbone carbonyl oxygens that also participate in \alpha-helix hydrogen bonds. There is no apparent distortion of the helix caused by hydration. The space group is $P2_12_12_1$, with a = 9.964 (3) A, b = 20.1 17 (3) A, c = 39.31 1 (6) A, Z = 4, and $d_x$ = 1.127 g/$cm^3$ for $C_{64}H_{106}N_{l3}O_{16}$.1.33$H_2O$. The final agreement factor R was 0.089 for 3667 data observed >3\sigma(F) with a resolution of 0.9 A.

Item Type:	Journal Article
Publication:	Biochemistry
Publisher:	American Chemical Society
Additional Information:	Copyright for this article belongs to American Chemical Society.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	14 Feb 2005
Last Modified:	19 Sep 2010 04:18
URI:	http://eprints.iisc.ac.in/id/eprint/2783

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