✦ LIBER ✦

Appendix: Raman spectrum and structure of elastin in relation to type-II β-turns

✍ Scribed by B. Prescott; V. Renugopalakrishnan; G. J. Thomas Jr.

Publisher: Wiley (John Wiley & Sons)
Year: 1987
Tongue: English
Weight: 152 KB
Volume: 26
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.360260612

No coin nor oath required. For personal study only.

✦ Synopsis

Nuclear magnetic resonance' and Raman2 studies have shown that the linear polypentapeptide, (VPGVG),, and the cyclopentadecapeptide, c(VPGVG),, exhibit similar peptide group conformations. Since the crystal structure of the latter reveals a cyclic network of three type-I1 p -t u r n ~, ~ and since the former is related to repeating peptide sequences of tr~poelastin,~ the question arises as to whether p(I1)turns may also be an important conformational component of native elastin. We have employed Raman spectroscopy to examine this question in light of R m a n data available from the p(I1)tw-n *To whom correspondence may be addressed.

📜 SIMILAR VOLUMES

Raman amide bands of type-II β-turns in

Raman amide bands of type-II β-turns in cyclo-(VPGVG)3 and poly-(VPGVG), and implications for protein secondary-structure analysis

✍ George J. Thomas Jr.; Betty Prescott; Dan W. Urry 📂 Article 📅 1987 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 855 KB

The cyclopentadecapeptide, c(VPGVG),, a model structure for protein type-I1 8-turns [W. J. Cook et al. (1980) J. Am. Chem. SOC. 102, 5502-55051, has been investigated by laser Raman spectroscopy. Data obtained from both normal and deuterated crystals identify amide I, 111, 1', and 111' bands charact