Naturally occurring biodegradable polymers as the basis of chiral gels for the distinction of enantiomers by partially oriented NMR spectroscopy.
Int J Artif Organs. 2011 Feb;34(2):134-8
Authors: Büchler SS, Kummerlöwe G, Luy B
In modern, high resolution NMR spectroscopy, anisotropic parameters play an important role. They can be measured with the help of liquid crystalline mesophases or stretched polymer gels as so-called alignment media. Biologically occurring chiral polymers are of special interest as alignment media for this technique because they allow enantiomers to be distinguished.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Structure and alignment of the membrane-associated antimicrobial peptide arenicin by oriented solid-state NMR spectroscopy.
Biochemistry. 2011 May 10;50(18):3784-95
Authors: Salnikov ES, Aisenbrey C, Balandin SV, Zhmak MN, Ovchinnikova TV, Bechinger B
The antimicrobial arenicin peptides are cationic amphipathic sequences that strongly interact with membranes. Through a cystine ring closure a cyclic ?-sheet structure is formed...
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07-13-2011 06:42 PM
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
Structure and Alignment of the Membrane-Associated Antimicrobial Peptide Arenicin by Oriented Solid-State NMR Spectroscopy
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Biochemistry
DOI: 10.1021/bi1018732
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04-16-2011 02:04 AM
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Sci China Life Sci. 2011 Feb;54(2):101-11
Authors: Feng W, Pan L, Zhang M
NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes. Each method has unique strengths and...
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02-15-2011 07:17 PM
[NMR images] The basis of NMR spectroscopy
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The basis of NMR spectroscopy
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02-01-2011 06:40 PM
[NMR paper] Synthesis and analysis of the enantiomers of calmidazolium, and a 1H NMR demonstratio
Synthesis and analysis of the enantiomers of calmidazolium, and a 1H NMR demonstration of a chiral interaction with calmodulin.
Related Articles Synthesis and analysis of the enantiomers of calmidazolium, and a 1H NMR demonstration of a chiral interaction with calmodulin.
Chirality. 1996;8(8):545-50
Authors: Edwards AJ, Sweeney PJ, Reid DG, Walker JM, Elshourbagy N, Egwuagu CE, Young JF, Patton CL
Calmidazolium -3-ethyl]-1H-imidazolium chloride] is a potent calmodulin inhibitor. This paper describes the synthesis and properties of the...
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08-22-2010 02:27 PM
[NMR paper] Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: th
Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.
Related Articles Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.
J Biomol NMR. 1993 May;3(3):285-96
Authors: Stockman BJ, Euvrard A, Scahill TA
Human ubiquitin is a 76-residue protein that serves as a protein degradation signal when conjugated to another protein. Ubiquitin has been shown to exist in at least three states: native (N-state), unfolded (U-state), and,...