Structure of the Antimicrobial Peptide Tritrpticin Bound to Micelles: A Distinct Membrane-Bound Peptide Fold,
- 1 December 1999
- journal article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 38 (51) , 16749-16755
- https://doi.org/10.1021/bi990701c
Abstract
WwPDB: Worldwide Protein Data BankKeywords
This publication has 26 references indexed in Scilit:
- Folding of amphipathic α-helices on membranes: energetics of helix formation by melittin 1 1Edited by D. ReesJournal of Molecular Biology, 1999
- Antimicrobial activity of a 13 amino acid tryptophan‐rich peptide derived from a putative porcine precursor protein of a novel family of antibacterial peptidesFEBS Letters, 1996
- MOLMOL: A program for display and analysis of macromolecular structuresJournal of Molecular Graphics, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Cathelicidins: a novel protein family with a common proregion and a variable C‐terminal antimicrobial domainFEBS Letters, 1995
- The solution structure of the active domain of CAP18 — a lipopolysaccharide binding protein from rabbit leukocytesFEBS Letters, 1995
- Peptide Antibiotics and Their Role in Innate ImmunityAnnual Review of Immunology, 1995
- A review: The active peptide of lactoferrinPediatrics International, 1994
- Molecular cloning of a putative homolog of proline/arginine‐rich antibacterial peptides from porcine bone marrowFEBS Letters, 1993
- Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipidsBiochemistry, 1987