## 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 (@-tur
Spectroscopic analysis of polypeptide conformation in polymethyl glutamate monolayers
✍ Scribed by G.I Loeb; R.E Baier
- Book ID
- 107786172
- Publisher
- Elsevier Science
- Year
- 1968
- Tongue
- English
- Weight
- 675 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0021-9797
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A detailed conformational analysis of homo-oligo-L-glutamates was carried out in aqueous solution using I H-nmr spectroscopy. Three series of side-chain protected (a-OMe) glutamate oligopeptides, attached to polyoxyethylene (POE) to enhance their solubility, were synthesized. The effect of the N-ter
## Abstract The electric birefringence of poly(L‐glutamic acid) (PLGA) in methanol, dimethyl sulfoxide, dimethylformamide, __N__‐methylacetamide, trifluoroacetic acid, dioxane–water mixtures (3:1 and 4:1 by volume), and dioxane–formamide mixture (1:1 by volume) has been measured by the use of the r
## Abstract The Zimm–Bragg parameters __s__ and σ were determined for poly(γ‐benzyl L‐glutamate) (PBLG) in __m__‐cresol and in dimethylformamide (DMF) from ORD data as a function of molecular weight. It was found that, within the temperature range between 10 and 55°C and on the average, __s__ = 1.6