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Hydrophobicity of amino acid residues: Differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin

✍ Scribed by Chi-Hao Luan; Timothy M. Parker; D. Channe Gowda; Dan W. Urry

Publisher
Wiley (John Wiley & Sons)
Year
1992
Tongue
English
Weight
928 KB
Volume
32
Category
Article
ISSN
0006-3525

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Differential scanning calorimetry studie
Differential scanning calorimetry studies of the inverse temperature transition of the polypentapeptide of elastin and its analogues
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## Abstract Differential scanning calorimetry studies have been carried out on the sequential polypeptide of elastin, (L‐Val^1^–L‐Pro^2^–Gly^3^–L‐Val^4^–Gly^5^)~__n__,~ abrreviated as PPP, and its more hydrophobic analogues (L‐Val^1^–L‐Pro^2^–Gly^3^–L‐Val^4^–Gly^5^)~__n__~, referred to as Leu^1^‐PP

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Differential scanning calorimetry studies of the effect of NaCl on protein-based polymer self-assembly has been carried out on six elastin-based synthetic sequential polypeptidesi.e., the polypentapeptide (~-Val'-~-Pro~-Gly~-~-Val'-GlyS), and its more hydrophobic analogues (~-Leu'-~-Pro~-Gly~-~-Val~

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## Abstract The preparation of the co‐oligopeptides of the series H‐Gly‐Trp‐(Gly)~__n__~‐Trp‐Gly‐OH (__n__ = 0, 1, and 2) and of a number of other unprotected co‐oligopeptides of glycine and tryptophan is reported. The syntheses have been carried out by conventional methods, using, in general, __N_

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## Abstract Several N‐protected peptide amides, containing two aromatic residues spaced by one glycyl residue, have been enzymatically synthesized starting from P‐Ar‐OH and H‐Gly‐Ar‐NH~2~ (P is the protecting group and Ar is the aromatic residue) and using α‐chymotrypsin as the catalyst for the cou