## Abstract The normal modes have been calculated for structures having the dihedral angles of the four Ξ²βturns of insulin. Frequencies are predicted in the amide I region near 1652 and 1680 cm^β1^. The former overlaps the Ξ±βhelix band at 1658 cm^β1^ in the Raman spectrum, while the latter accounts
Vibrational analysis of conformation in peptides, polypeptides, and proteins
β Scribed by S. Krimm
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Tongue
- English
- Weight
- 408 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Synopsis
A vibrational force field for the polypeptide chain has been developed for normal-mode analysis of such molecules. It can reproduce observed frequencies of known structures to within about 5 cm-l. We review the application of this technique to conformational problems in peptides (@-turns and their model compounds), polypeptides [the aII-helix and crystalline poly(g1ycine II)], and proteins (bacteriorhodopsin and glucagon).
* This is paper number 16 in a series of which Ref. 20 is paper 15.
π SIMILAR VOLUMES
The topological aspects of the conformational transformations in a polypeptide chain are investigated in relation to the problem of selecting the minimum-energy pathways in protein folding.
Using potential energy formulas for variation of bond angles and for w-distortion, the conformation of minimum energy for the cis form of the petide unit has been worked out. This agrees very well with the corresponding set of atoms in the crystal structure of Leu-Pro-Gly and the dimensions of a sta
## Abstract The vibrational absorption and vibrational circular dichroism (VCD) spectra of melittin in D~2~O solutions at different pH values, different salt concentrations, or different 2,2,2βtrifluoroethanol (TFE) concentrations are recorded in the amide Iβ² (1850β1600 cm^β1^) region. Two models a