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,
Conformation of Poly-L-methionine and Some of its Derivatives in Solution
✍ Scribed by Perlmann, Gertrude E.; Katchalski, Ephraim.
- Book ID
- 126976021
- Publisher
- American Chemical Society
- Year
- 1962
- Tongue
- English
- Weight
- 719 KB
- Volume
- 84
- Category
- Article
- ISSN
- 0002-7863
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## Abstract The conformational transition of poly‐L‐tyrosine 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 Infrared spectroscopy, X‐ray diffraction, and nuclear magnetic resonance spectroscopy have been used in investigating the conformation of two stereoregular polymethionines, poly(D‐methionyl‐L‐methionine) and poly(L‐methionyl‐D‐methionyl‐L‐methionine). When dissolved in a helicogenic sol
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.
## Abstract Absorption, circular dichroism (CD), and optical rotatory dispersion (ORD) measurements were carried out on poly‐L‐tyrosine in trimethyl phosphate solution over the spectral range 185–600 mμ. There is evidence in the CD spectrum for side chain‐side chain interactions in poly‐L‐tyrosine.