## Abstract Sequential polypeptides with the repeating units L‐tyrosyl‐L‐lysyl, L‐tyrosyl‐(L‐lysyl)~2~, and L‐tyrosyl‐(L‐lysyl)~3~ have been synthesized by solution polymerization of the __N__‐hydroxy‐succinimide esters of the corresponding di‐, tri‐, and tetrapeptides. The monomers for the polytri
Conformational studies of sequential polypeptides containing lysine and tyrosine
✍ Scribed by S. St. Pierre; R. T. Ingwall; M. S. Verlander; M. Goodman
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 635 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The conformation of three sequential copolypeptides, poly(L‐tyrosyl‐L‐lysine), poly(L‐tyrosyl‐L‐lysyl‐L‐lysine), and poly[L‐tyrosyl‐(L‐lysyl)~2~‐L‐lysine] have been studied by a variety of techniques, including CD, ir spectroscopy, analytical ultracentrifugation, and x‐ray diffraction. Depending upon the pH and sovent composition, poly(L‐tyrosyl‐Llysyl‐L‐lysine) and poly [L‐tyrosyl‐(Llysyl)~2~‐L‐lysine] can adopt either the α‐helical or random‐coil conformation, while poly(L‐tyrosyl‐L‐lysine) forms either inter‐ or intramolecular β‐structures.
📜 SIMILAR VOLUMES
The sequential polypeptides (L-Arg-X-Gly),, where X represents amino acid residues Ala, Val, and Leu, were prepared as models of argininerich histones to be used in studying their structure and their interactions with DNA. The polymerization was carried out on the pentachlorophenyl active esters of
Alternating poly(Arg-Leu) and copolypeptides with Arg-Leu and His-Leu sequences were prepared by condensation of the corresponding p-nitrophenyl dipeptide esters in the presence of 1-hydroxybenzotriazole. Arginine was used without any protection and histidine side chains were protected using r-benzy
## Abstract Six different sequential polypeptides with the repeating units L‐lysyl‐L‐DOPA, L‐DOPA‐L‐lysine, L‐lysyl‐L‐lysyl‐L‐DOPA, L‐DOPA‐L‐DOPA‐L‐lysine, L‐lysyl‐L‐lysyl‐L‐lysyl‐L‐DOPA, and L‐DOPA‐L‐DOPA‐L‐DOPA‐L‐lysine have been synthesized by solution polymerization of the __p__‐nitrophyenyl es
## Abstract The α‐helix–coil transition of poly‐L‐leucine, poly‐L‐alanine and poly‐L‐methionine in chloroform–trifluoroacetic acid system was studied by nuclear magnetic resonance (NMR) and optical rotatory dispersion (ORD). The kinetics of the hydrogen–deuterium exchange in the peptide was also fo