Starch is a major contributor to the carbohydrate portion of our diet. When it is present with water, it undergoes several transformations during heating and/or cooling making it an essential structure-forming component in starch-rich food systems (e.g., bread and cake). Time domain proton nuclear magnetic resonance (TD š H NMR) is a useful technique to study starch-water interactions by evaluation of molecular mobility and water distribution. The data obtained correspond to changes in starch...
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study
Abstract
The C-terminal domain of histone H1.0 (C-H1.0) is involved in DNA binding and is a main determinant of the chromatin condensing properties of histone H1.0. Phosphorylation at the (S/T)-P-X-(K/R) motifs affects DNA binding and is crucial for regulation of C-H1.0 function. Since C-H1.0 is an intrinsically disordered domain, solution NMR is an excellent approach to characterize the...
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Journal Highlight: A review of NMR methods used in the study of the structure and dynamics of ionic liquids
Journal Highlight: A review of NMR methods used in the study of the structure and dynamics of ionic liquids
http://www.spectroscopynow.com/common/images/thumbnails/1613355a2ed.jpgThis mini-review presents a brief research summary of the applications of NMR spectroscopy to the structure and dynamics of pure ionic liquids and their mixtures with lithium salts.
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[NMR paper] Influence of the incorporation of fibers in biscuit dough on proton mobility characterized by time domain NMR.
Influence of the incorporation of fibers in biscuit dough on proton mobility characterized by time domain NMR.
Influence of the incorporation of fibers in biscuit dough on proton mobility characterized by time domain NMR.
Food Chem. 2016 Feb 1;192:950-7
Authors: Serial MR, Blanco Canalis MS, Carpinella M, Valentinuzzi MC, León AE, Ribotta PD, Acosta RH
Abstract
The effect of fiber addition on the distribution and mobility of protons in biscuits is studied by using low resolution time domain nuclear magnetic resonance (TD-NMR)....
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08-26-2015 10:21 AM
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase.
J Mol Biol. 2011 Jul 23;
Authors: Sugimoto H, Noda Y, Segawa SI
A thermally unfolded disulfide-deficient mutant of the starch-binding domain of glucoamylase refolds into a kinetically trapped metastable intermediate when subjected to a rapid lowering of temperature. We attempted to characterise...
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08-02-2011 11:40 AM
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Dynamics of heme in hemoproteins: proton NMR study of myoglobin reconstituted with iron 3-ethyl-2-methylporphyrin.
Biochim Biophys Acta. 2011 May 6;
Authors: Juillard S, Chevance S, Bondon A, Simonneaux G
The asymmetric 3-ethyl-2-methylporphyrin iron complex was synthetized and inserted into apomyoglobin. UV-visible spectroscopic studies demonstrated the capacity of iron to coordinate different exogenous axial ligands in ferrous and...
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[NMR paper] Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high
Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high-resolution NMR.
Related Articles Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high-resolution NMR.
Magn Reson Chem. 2005 Apr;43(4):309-15
Authors: Khallouk M, Rutledge DN, Silva AM, Delgadillo I
The study of protein hydration by time-domain NMR is complicated by the great number of interactions involved, resulting from the presence of several amino acids and the possible modifications produced by the various structures....
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[NMR paper] Proton NMR study of the comparative electronic/magnetic properties and dynamics of th
Proton NMR study of the comparative electronic/magnetic properties and dynamics of the acid in equilibrium with alkaline transition in a series of ferricytochromes c'.
Related Articles Proton NMR study of the comparative electronic/magnetic properties and dynamics of the acid in equilibrium with alkaline transition in a series of ferricytochromes c'.
J Biol Chem. 1990 Sep 25;265(27):16173-80
Authors: La Mar GN, Jackson JT, Dugad LB, Cusanovich MA, Bartsch RG
The proton NMR spectra of ferricytochrome c' from Rhodopseudomonas palustris,...
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[NMR paper] Internal motion time scales of a small, highly stable and disulfide-rich protein: a 1
Internal motion time scales of a small, highly stable and disulfide-rich protein: a 15N, 13C NMR and molecular dynamics study.
Related Articles Internal motion time scales of a small, highly stable and disulfide-rich protein: a 15N, 13C NMR and molecular dynamics study.
J Biomol NMR. 1999 May;14(1):47-66
Authors: Guenneugues M, Gilquin B, Wolff N, MĂŠnez A, Zinn-Justin S
Motions of the backbone C alpha H alpha and threonine C beta H beta bonds of toxin alpha were investigated using natural abundance 13C NMR and molecular dynamics. Measurement...
The use of time domain 1 H NMR to study proton dynamics in starch-rich foods: A review
Linear Mode
