Fluorescent hydrophobic peptide fragments of emerimicin. Models for the study of peptide aggregation and interactions with lipids and proteins
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. High resolution and field desorption mass spectrometry studies and revised structures of alamethicins I and II
2. Chemical nature and sequence of alamethicin
3. Reptaibophol antibiotics. 2. Structures of the peptide antibiotics emerimicins III and IV
4. Structure of antiamoebin I from high resolution field desorption and gas chromatographic mass spectrometry studies
5. Structural and membrane modifying properties of suzukacillin, a peptide antibiotic related to alamethicin
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1. Research Contributions from India on Membrane-Modifying Peptides: Motivations from Fungal Peptaibiotics;Progress in Mycology;2021
2. Spectroscopic Investigations of Metalloporphyrin−Oligopeptide Systems: Evidence for Peptide Aggregation;Langmuir;2005-09-30
3. Studies of fluorescence depolarization at high pressures of dimyristoylphosphatidylcholine liposomes containing poly(γ-benzyl-l-glutamate);Chemistry and Physics of Lipids;1988-10
4. Conformations and mitochondrial uncoupling activity of synthetic emerimicin fragments;Biopolymers;1988-04
5. Depth-dependent fluorescent quenching of a tryptophan residue located at defined positions on a rigid 21-peptide helix in liposomes;Biochimica et Biophysica Acta (BBA) - Biomembranes;1987-01
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