Heterogeneities in gelatin film formation using single-sided NMR.
J Phys Chem B. 2010 Dec 16;114(49):16356-63
Authors: Ghoshal S, Mattea C, Denner P, Stapf S
Gelatin solutions were prepared in D(2)O. The drying process of cast solutions was followed with a single-sided nuclear magnetic resonance (NMR) scanner until complete solidification occurred. Spin-spin relaxation times (T(2)) were measured at different layers with microscopic resolution and were correlated with the drying process during film formation. Additionally, the evaporation of the gelatin solution was observed optically from the reduction of the sample thickness, revealing that at the macroscopic level, the rate of evaporation is not uniform throughout the experiment. A crossover in the spatial evolution of the drying process is observed from the NMR results. At the early stages, the gel appears to be drier in the upper layers near the evaporation front, while this tendency is inverted at the later stages, when drying is faster from the bottom. XRD (X-ray diffraction) data showed that a structural heterogeneity persists in the final film.
[NMR paper] NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric h
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FEBS Lett. 2002 Mar 27;515(1-3):165-70
Authors: Chang X, Keller D, O'Donoghue SI, Led JJ
Nuclear magnetic resonance (NMR) spectroscopy reveals that higher-order aggregates of glucagon-like peptide-1-(7-36)-amide (GLP-1) in pure water at pH 2.5 are disrupted by 35% 2,2,2-trifluoroethanol (TFE), and form a stable and highly symmetric...
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[NMR paper] 13C NMR chemical shifts can predict disulfide bond formation.
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J Biomol NMR. 2000 Oct;18(2):165-71
Authors: Sharma D, Rajarathnam K
The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded)...
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[NMR paper] Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's
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Biochemistry. 2000 Nov 14;39(45):13748-59
Authors: Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH(2), called A...
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[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
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J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
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[NMR paper] Conformational changes of the BS2 operator DNA upon complex formation with the Antenn
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J Mol Biol. 1999 Sep 24;292(3):609-17
Authors: Fernández C, Szyperski T, Billeter M, Ono A, Iwai H, Kainosho M, Wüthrich K
The NMR structures have been determined for a 13C/15N doubly labeled 14 base-pair DNA duplex comprising the BS2...
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[NMR paper] NMR and luminescence studies on the formation of ternary adducts between HSA and Ln(I
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Biochim Biophys Acta. 1998 Jun 11;1385(1):7-16
Authors: Aime S, Bettinelli M, Ferrari M, Razzano E, Terreno E
At physiological pH and in the presence of an excess of malonate ligand (MAL), the lanthanide ions (Ln=Eu(III), Gd(III) and Tb(III)) are under the form of -. Upon addition of human serum albumin (HSA),...
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[NMR paper] Thiol/disulfide formation associated with the redox activity of the [Fe3S4] cluster o
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J Biol Chem. 1994 Mar 18;269(11):8052-8
Authors: Macedo AL, Moura I, Surerus KK, Papaefthymiou V, Liu MY, LeGall J, Münck E, Moura JJ
Desulfovibrio gigas ferredoxin II (FdII) is a small protein (alpha 4 subunit...
Heterogeneities in gelatin film formation using single-sided NMR.
Linear Mode
