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Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape

Hetényi, Anasztázia and Szakonyi, Zsolt and Mándity, István and Szolnoki, Éva Tünde and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc (2009) Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape. CHEMICAL COMMUNICATIONS (2). pp. 177-179. ISSN 1359-7345

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Abstract

The long-range side-chain repulsion between the (1R, 2R, 3R, 5R)-2- amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers.

Item Type: Article
Subjects: Q Science / természettudomány > QD Chemistry / kémia
SWORD Depositor: MTMT SWORD
Depositing User: MTMT SWORD
Date Deposited: 10 Jun 2016 12:58
Last Modified: 10 Jun 2016 12:58
URI: http://real.mtak.hu/id/eprint/36252

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