Journal
ORGANIC LETTERS
Volume 22, Issue 2, Pages 348-351Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.orglett.9b03528
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Funding
- Fonds der Chemischen Industrie (Germany)
- Swiss National Science Foundation [200020_169423]
- DFG cluster of excellence (EXC 114) Center for Integrative Protein Science Munich (CIPSM)
- Swiss National Science Foundation (SNF) [200020_169423] Funding Source: Swiss National Science Foundation (SNF)
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The effect of four- and six-membered ring-size analogs (azetidine- and piperidine-2-carboxylic acid, H-Aze-OH and H-Pip-OH) of proline on the stability of the collagen triple helix was examined. Computational and nuclear magnetic resonance spectroscopic studies with model compounds and thermal denaturation experiments with collagen peptides showed that the ring-size analogs destabilize the triple helix to a similar extent by either mismatching backbone dihedral angles phi and psi (Pip) or by an unfavorable trans/cis amide bond ratio (Aze).
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