Stepwise solution syntheses are described of the homo-oligomers Z-(Thr) n -NHCH 3 (n1ยฑ4, Members of the III 1ยฑ5 series were obtained by de-acetylation of the corresponding oligomers of the II 1ยฑ5 series. The conformational preferences of the terminally protected homo-peptides of the three series we
Influence of glycosylation on the conformational preferences of folded oligopeptides
โ Scribed by Marina Gobbo; Alessia Nicotra; Raniero Rocchi; Marco Crisma; Claudio Toniolo
- Book ID
- 108371126
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- French
- Weight
- 204 KB
- Volume
- 57
- Category
- Article
- ISSN
- 0040-4020
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๐ SIMILAR VOLUMES
The folded native state of a globular protein is noted to be marginally stabilized over the structureless unfolded state by various atomic/group interactions. Quantitative enumeration of these factors remains to be a difficult task to workers in the field. In this work we collect experimental inform
We have observed that the rate of folding of the enzymatically hydroxylated form of poly(G1y-Pro-Pro) into the triple-helical conformation is considerably higher than that of the unhydroxylated polypeptide [R. K. Chopra and V. S. Ananthanarayanan (1982) Proc. Nutl. Acud. Sci. USA 79, 7180-71841. In
The decapeptidepBrBz-( Aib)lo-OtBu, synthesized by the 5 ( 4 H ) -oxazolone method, crystallizes in the monoclinic space group C2/c with a = 43.901(2), b = 9.289(2), and c = 34.746(3) A; p = 114.69(3) O ; and 2 = 8. The crystals contain one molecule of water associated with each peptide. The structu