We have measured vibrational CD spectra in the 3600-1250 cm-I region of two monodisperse, protected octapeptides, which form right-handed 3,,-helices in CDC13 solution. The spectra are similar in sign pattern to those obtained for right-handed a-helices in solution but are smaller in magnitude and,
Vibrational CD of polypeptides. X. A study of α-helical oligopeptides in solution
✍ Scribed by S. C. Yasui; T. A. Keiderling; Ryoichi Katakai
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1987
- Tongue
- English
- Weight
- 310 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Synopsis
We have measured the vibrational CD (VCD) of a series of hetermligopeptides-onitrophenylsulfenyl(L-Met-L-Met-L-Leu),-OEt, n = 6,8,10,11--in the amide A, I, and I1 regions.
These spectra are identical in shape and magnitude, within our signal to noise limits. The VCD in each band are of exactly the shape expected for a right-handed a-helix and imply that VCD of the polypeptide a-helix is relatively unaffected by chain length down to the 18-subunit level.
📜 SIMILAR VOLUMES
## Abstract Vibrational CD (VCD) of amides A, I, and II vibrations of a variety of polypeptide films have been measured. VCD of films of α‐helical and β‐sheet structures are compared in the three regions. Reproducible spectra could only be obtained for thin films free of orientation dependence. The
Absorption spectra and induced CD have been measured on aqueous solutions of watersoluble porphyrins with a-helical poly (L-glutamic acid) or a-helical poly (L-lysine) a t different mixing ratios. For the former, porphyrin is porphine-meso-tetra (4-N-methylpyridinium) (TMpyP) , and for the latter, i
We have measured the VCD of polytyrosine in the amide I and I1 regions in dimethyl sulfoxide (DMSO) and in 8020 mixtures of DMSO with trifluoroethanol, trifluoroacetic acid (TFA), and dichloroacetic acid and in 50:50 mixtures of DMSO and trimethyl phosphate (TMP). Additionally, VCD was obtained for