90282-69-2Relevant articles and documents
Hydrophobicity profile of amino acid residues: A differential scanning calorimetry and circular dichroism study of leucine and isoleucine co-polypeptides of the protein-based polymers of elastin
Gowda, D. Channe,Baba, A. Ramesha,Luan, Chi-Hao
, p. 2606 - 2613 (2007/10/03)
The inverse temperature transition of hydrophobic folding and assembly of a "host-guest" model system based on the elastin derived polypentapeptide, poly(VPGVG), is employed to determine the relative hydrophobicity of amino acid residues of proteins and p
ATRIOPEPTINS. II. SYNTHESIS OF N-TERMINAL FRAGMENTS
Ovchinnikov, Mikhail V.,Bespalova, Zhanna D.,Molokoedov, Aleksandr S.,Revenko, Inna V.,Sepetov, Nikolai F.,et al
, p. 784 - 795 (2007/10/02)
Peptides, corresponding to the N-terminal sequence in atriopeptins, were synthesized by classical methods of peptide chemistry in solutions.The obtained peptides were characterized by various physicochemical methods.The scheme and methods of the synthesis are discussed.
SYNTHESE EINES XYLOSE-HALTIGEN GLYCOPEPTIDES, DAS DIE AMINOSAEURE-SEQUENZ 4 BIS 7 DES NH2-TERMINUS DER PROTEIN-CORE-STRUCTUR DES RINDERHAUT-PROTODERMATAN-SULFATS ENTHAELT
Garg, Hari G.,Hasenkamp, Thomas,Paulsen, Hans
, p. 225 - 232 (2007/10/02)
The synthesis is described of α-β-D-xylopyranosyl-L-serylglycyl-L-isoleucyl-glycine (7), a glycopeptide containing the amino acid sequence of the protein core-structure of beef-skin protodermatan sulfate; coupling of N-protected O-XylpSer with protected GlyIleuGly followed by deprotection afforded 7.