Chain-length dependence for secondary structure formation of homo-oligopep tides fromε-tert.-butyloxycarbonyl-L-lysine with a lipophilic C-terminal group
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1984.tb02691.x/fullpdf
Reference28 articles.
1. Conformation of linear homo-oligoprolines
2. The chain length dependence of the conformation for oligomers ofL-lysine in aqueous solution: Optical rotatory dispersion studies
3. Estimation of the circular dichroism exhibited by statistical coils of poly(L-alanine) and unionized poly(L-lysine) in water
4. CONFORMATIONAL CHARACTERISTICS OF THE N-ACETYL-N‘-METHYLAMIDES OF THE FOUR (LYS, TYR) DIPEPTIDES
5. Chain-length dependence for secondary structure formation of poly(ethylene glycol)-bound homooligopeptides of .epsilon.-benzyloxycarbonyl-L-lysine in the solid state and in solution
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1. Sequence-dependence of secondary structure formation;International Journal of Peptide and Protein Research;2009-01-12
2. Synthetic homo-oligomethionine chemoattractants;International Journal of Peptide and Protein Research;2009-01-12
3. Physical Data of Oligomers;The Wiley Database of Polymer Properties;1999-02-22
4. (Cholestanyloxycarbonyl)benzyl esters as peptide substituents: Conformational properties of fully protected oligo-L-lysines with C-terminal (cholestanyloxycarbonyl)benzyl and benzyl ester moieties;Helvetica Chimica Acta;1986-03-19
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