Structural analysis of the peptides temporin-Ra and temporin-Rb and interactions with model membranes
Author:
Funder
FAPESP
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
https://link.springer.com/content/pdf/10.1007/s00249-022-01615-y.pdf
Reference34 articles.
1. Anthis NJ, Clore GM (2013) Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm. Protein Sci 22(6):851–858
2. Asoodeh A, Zardini HZ, Chamani J (2012) Identification and characterization of two novel antimicrobial peptides, temporin-Ra and temporin-Rb, from skin secretions of the marsh frog (Rana ridibunda). J Pept Sci 18(1):10–16. https://doi.org/10.1002/psc.1409
3. Bürck J, Roth S, Wadhwani P, Afonin S, Kanithasen N, Strandberg E, Ulrich AS (2008) Conformation and membrane orientation of amphiphilic helical peptides by oriented circular dichroism. Biophys J 95(8):3872–3881. https://doi.org/10.1529/biophysj.108.136085
4. Bürck J, Wadhwani P, Ulrich FS, AS, (2016) Oriented circular dichroism: a method to characterize membrane-active peptides in oriented lipid bilayers. Acc Chem Res 49:184–192
5. Cammers-Goodwin A, Allen TJ, Oslick SL, Mcclure KF, Lee JH, Kemp DS (1996) Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J Am Chem Soc 118:3082–3090
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