## 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.
Synthesis of sequential polypeptides containing lysine and tyrosine
✍ Scribed by S. St. Pierre; R. T. Ingwall; M. Goodman
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1978
- Tongue
- English
- Weight
- 513 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
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 polytripeptide and polytetrapeptide were prepared by fragment condensation, using the mixed carbonic anhydride coupoling method. Moderately high molecular weight polypeptides were obtained.
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## 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 chemistry of phosphoserine [Ser(P)] containing peptides and polypeptides was extensively investigated to explore a new biomineralization material science. The selective cleavage of the __O__,__O′__‐diphenyl phospho‐protecting groups of Ser(PO~3~Ph~2~) was examined using hydrogenolys
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 sequential polytetrapeptides containing equimolar amounts of tyrosine, glutamic acid, alanine, and glycine were characterized by CD and difference spectroscopy over a wide range of pH. As the pH was lowered from physiological values, each of the polymers underwent pH‐sensitive trans