Structural highlights
Publication Abstract from PubMed
Lasso peptides are fascinating natural products with a unique structural fold that can exhibit tremendous thermal stability. Here, we investigate factors responsible for the thermal stability of caulosegnin II. By employing X-ray crystallography, mutational analysis and molecular dynamics simulations, the ring residue proline 8 was proven to be crucial for thermal stability.
The ring residue proline 8 is crucial for the thermal stability of the lasso peptide caulosegnin II.,Hegemann JD, Fage CD, Zhu S, Harms K, Di Leva FS, Novellino E, Marinelli L, Marahiel MA Mol Biosyst. 2016 Feb 11. PMID:26863937[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hegemann JD, Fage CD, Zhu S, Harms K, Di Leva FS, Novellino E, Marinelli L, Marahiel MA. The ring residue proline 8 is crucial for the thermal stability of the lasso peptide caulosegnin II. Mol Biosyst. 2016 Feb 11. PMID:26863937 doi:http://dx.doi.org/10.1039/c6mb00081a
