90282-71-6Relevant academic research and scientific papers
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
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.
Studies of Bitter Peptides from Casein Hydrolyzate. IV. Relationship between Bitterness and Hydrophobic Amino Acids Moiety in the C-Terminal of BPIa (Arg-Gly-Pro-Pro-Phe-Ile-Val)
Otagiri, Ken,Shigenaga, Toshiaki,Kanehisa, Hidenori,Okai, Hideo
, p. 90 - 96 (2007/10/02)
In the synthetic studies of bitter peptide BPIa (Arg-Gly-Pro-Pro-Phe-Ile-Val), we sythesized several BPIa analogs to elucidate the participation of the hydrophobic amino acids moiety in the C-terminal in the bitter taste exhibited by BPIa.The syntheses of
