Related ArticlesDetermination of Structure and Micellar Interactions of Small Antimicrobial Peptides by Solution-State NMR.
Methods Mol Biol. 2017;1548:73-88
Authors: Wimmer R, Uggerhøj LE
Abstract
NMR spectroscopy is a well-established technique to determine the structure of peptides and small proteins in solution, also when bound to detergent micelles or phospholipid bicelles. The structure of the peptide alone is, however, not conveying the full picture, if the peptide is bound to a micelle, since it does not tell anything about the orientation of the peptide in the micelle. This article describes how to obtain that information together with information on peptide structure.
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
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01-29-2016 12:59 PM
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
nmrlearner
Journal club
0
09-29-2015 02:39 PM
[NMR paper] (19)F-NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids.
(19)F-NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids.
(19)F-NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids.
Biochim Biophys Acta. 2014 Mar 31;
Authors: Afonin S, Glaser RW, Sachse C, Salgado J, Wadhwani P, Ulrich AS
Abstract
Many amphiphilic antimicrobial peptides permeabilize bacterial membranes via successive steps of binding, re-alignment and/or oligomerization. Here, we have systematically...
nmrlearner
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04-06-2014 02:01 AM
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
nmrlearner
Journal club
0
01-09-2013 04:20 PM
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
nmrlearner
Journal club
0
11-15-2012 06:46 PM
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
nmrlearner
Journal club
0
10-12-2012 09:58 AM
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
nmrlearner
Journal club
0
08-24-2012 08:01 PM
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Solution and Solid-State NMR Structural Studies of Antimicrobial Peptides LPcin-I and LPcin-II.
Biophys J. 2011 Sep 7;101(5):1193-201
Authors: Park TJ, Kim JS, Ahn HC, Kim Y
Abstract
Lactophoricin (LPcin-I) is an antimicrobial, amphiphatic, cationic peptide with 23-amino acid residues isolated from bovine milk. Its analogous peptide, LPcin-II, lacks six N-terminal amino acids compared to LPcin-I. Interestingly, LPcin-II does not display any...