𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Normal mode spectrum of the parallel-chain β-sheet

✍ Scribed by Jagdeesh Bandekar; S. Krimm

Publisher
Wiley (John Wiley & Sons)
Year
1988
Tongue
English
Weight
680 KB
Volume
27
Category
Article
ISSN
0006-3525

No coin nor oath required. For personal study only.

✦ Synopsis

Normal mode calculations have been carried out for parallel-chain 8-sheet structures. These include the parallel-chain pleated sheet of poly(L-alanine) and the parallel-chain rippled sheet of polyglycine. Dipole derivative coupling has been included for amide I and I1 modes, and the effects of parallel-sheet and antiparallel-sheet arrangements of varying separation have been examined for the poly(i-alanine) case. Some amide and nonamide modes are distinctly different from their antiparallel-chain counterparts, thus providing a basis for distinguishing between such structures from their i r and Raman spectra. As in our previous studies, these results emphasize the need for both kinds of spectral data in order to draw definitive conclusions about conformation.

*This is paper number 39 in a series on "Vibrational Analysis of Peptides, Polypeptides, and Proteins," of which paper number 38 is Ref. 19.

📜 SIMILAR VOLUMES

Infrared spectra and resonance interacti
Infrared spectra and resonance interaction of amide-I vibration of the parallel-chain pleated sheet
✍ Yu. N. Chirgadze; N. A. Nevskaya 📂 Article 📅 1976 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 403 KB 👁 2 views

## Abstract Resonance vibrational interactions of amide I for the parallel‐chain pleated‐sheet structure have been treated on the basis of the perturbation theory in a dipole–dipole approximation. The infinite sheet and finite fragments of different types have been considered. The possibility of ex

Raman and normal-mode studies of the ext
Raman and normal-mode studies of the extended-helix conformation in polypeptide chains
✍ P. K. Sengupta; S. Krimm 📂 Article 📅 1987 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 540 KB

The nature of the local main-chain conformation of polypeptides with charged side chains has been the subject of considerable discussion since Tiffany and Krimm first proposed [(l968) Bwpoljmers 6, 1379-13811 that, rather than being random, the chain is locally relatively regular, with conformations

Collapse of a polypeptide chain as a res
Collapse of a polypeptide chain as a result of the intramolecular formation of antiparallel β-sheets
✍ Luanne F. Tilstra; Wayne L. Mattice 📂 Article 📅 1988 🏛 Wiley (John Wiley & Sons) 🌐 English

The folded nature of an intramolecular antiparallel 8-sheet suggests that the introduction of this structure into a statistical coil might be accompanied by a contraction of the chain. The magnitude of the contraction, and the conditions that produce the maximum contraction, have been assessed by th

Basis for large differences in the coope
Basis for large differences in the cooperativity of the formation of antiparallel β-sheets and clusters of interacting α-helices in isolated chains
✍ Wayne L. Mattice; Luanne Tilstra 📂 Article 📅 1987 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 479 KB 👁 1 views

## Synopsis Configuration partition functions that describe the intramolecular formation of antiparallel /?-sheets and clusters of antiparallel interacting a-helices are very nearly of the same form. They can be interconverted by a simple change in notation and the addition of one weighting factor