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Role of water molecules in the crystal structure of gly-L-ala-L-phe: A possible sequence preference for nucleation of α-helix?

✍ Scribed by N. Ramasubbu; R. Parthasarathy

Publisher: Wiley (John Wiley & Sons)
Year: 1989
Tongue: English
Weight: 567 KB
Volume: 28
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360280707

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✦ Synopsis

2H,O; GAT crystallizes in the monoclinic space group P2,, with a = 5.879(1), b = 7.966(1), c = 17.754(2) A, 8 = 95.14(2)O, 0 , = 1.321 g ~m -~, and 2 = 2. The crystal structure was solved by direct methods using the program SHELXS-86 and refined to an R value of 0.031 for 1425 reflections ( > 30). The tripeptide exists as a zwitterion in the crystal and assumes a near a-helical backbone conformation with the following torsion angles:

📜 SIMILAR VOLUMES

A sequence preference for nucleation of

A sequence preference for nucleation of α-helix—crystal structure of Gly-L-Ala-L-Val and Gly-L-Ala-L-Leu: Some comments on the geometry of leucine zippers

✍ Sanjeev Chaturvedi; Kuantee Go; R. Parthasarathy 📂 Article 📅 1991 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 723 KB

The synthetic peptide Gly-L-Ala-L-Val ( CloH19N,0, \* 3H20; GAV) crystallizes in the monoclinic space group P21, with a = 8.052( 2), b = 6.032(2), c = 15.779(7) A, ( 3 = 98.520( l)', V = 757.8 A3, D, = 1.312 g ~m -~, and 2 = 2. The peptide Gly-L-Ala-L-Leu ( C,,HplN30, \* 3H20; GAL) crystallizes in t