The effect of the number of methylene groups in the side chains on the conformation of polypeptides is assessed for three poly(L-lysine) homologs with R = -(CHz),,NHz. Circular dichroism studies show a pH-induced helix-coil transition in 0.05 M KCl with midpoints a t 9.6, 9.0, and 8.7 for n = 5, 6,
Conformations of poly-L-valine in solution
β Scribed by Raquel F. Epand; Harold A. Scheraga
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1969
- Tongue
- English
- Weight
- 59 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
β¦ Synopsis
On page 1533, in the last term of eq. (2), (alm[O) should be (alml0).
On page 1538, in line 3 of the Results section, R,,* should be Rn,*; in the next line, RB should also be Rn,*, and the first "in" should be "is.
π SIMILAR VOLUMES
## Abstract The conformational transition of polyβLβtyrosine in 0.1__M__ KCl was investigated by ORD and infrared spectroscopy, potentiometric titration, and sedimentation velocity experiments. It is shown that the fully ordered conformer is obtained by slow titration of the random coil with 0.1__N
## Abstract Raman spectroscopic studies have been carried out on polymers of Lβvaline ranging in degree of polymerization (__DP__) from 2 to 930. The spectrum of the hexapeptide (__DP__ = 6) is closely similar over the entire range 40β1750 cm^β1^ to those of polymers with much higher __DP__, and th
## Abstract Absorption, circular dichroism (CD), and optical rotatory dispersion (ORD) measurements were carried out on polyβLβtyrosine in trimethyl phosphate solution over the spectral range 185β600 mΞΌ. There is evidence in the CD spectrum for side chainβside chain interactions in polyβLβtyrosine.
The specific heat a t low temperatures depends on long-range order of the solid because only the long-wavelength phonons are involved. We have recently shown that in biopolymers the secondary and tertiary structures can be studied by such an investigation.' To confirm the results found on L-alanine