Publication date: Available online 28 February 2014 Source:Coordination Chemistry Reviews
Author(s): Riccardo De Ricco , Slawomir Potocki , Henryk Kozlowski , Daniela Valensin
Essential main-group elements [e.g., Na(I) and Ca(II)] and transition metal ions [e.g., Cu(II)/Cu(I), Fe(III)/Fe(II), Zn(II), and Ni(II)] play key roles in the structural organization and biological function of many macromolecules such as proteins, DNA, and RNA. Healthy conditions require tight regulation of metal concentrations inside and outside cells, and both metal deficiency and overload can lead to cellular dysfunction. Altered metabolism of transition metal ions is implicated in severe and chronic diseases, including cancer, neurodegenerative disorders, and microbial infection. Nature has developed a sophisticated machinery to balance the content of transition metal ions. Many enzymes, transporters, and chaperones are involved in these complex processes and control metal uptake and delivery to specific cellular domains. Many efforts have been devoted to clarifying metal interactions with amyloidogenic proteins, metal transporters, and metal storage proteins via different spectroscopic techniques. In this review we describe the application of NMR to determine the metal coordination spheres and structural features of flexible and disordered regions of proteins that are either involved in neurodegenerative processes or are derived from metal chaperones. The systems investigated include (i) copper, iron, and zinc binding to unstructured regions of prion protein, a-synuclein, and amyloid ß; (ii) zinc binding to extracellular domains of ZIP proteins; and (iii) zinc and nickel binding to the loop region of HypA, HspA, and SlyD proteins. The NMR behavior of these systems is compared and discussed. The benefits and drawbacks of the methodology are addressed by stressing the tricks and pitfalls encountered.
[NMR paper] Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106.
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Chem Phys Lipids. 2013 Sep 24;
Authors: Zhang L, Liu L, Maltsev S, Lorigan GA, Dabney-Smith C
Abstract
The chloroplast twin arginine translocation...
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Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Solid-State NMR Investigations of Peptide-Lipid Interactions of the Transmembrane Domain of A Plant-Derived Protein, Hcf106
Publication date: Available online 24 September 2013
Source:Chemistry and Physics of Lipids</br>
Author(s): Lei Zhang , Lishan Liu , Sergey Maltsev , Gary A. Lorigan , Carole Dabney-Smith</br>
The chloroplast twin arginine translocation system transports highly folded precursor proteins across the thylakoid using the protonmotive force as its only energy source. Hcf106 and another thylakoid protein, cpTatC compose the precursor receptor...
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[NMR paper] NMR investigations of structural and dynamics features of natively unstructured drug peptide - salmon calcitonin: implication to rational design of potent sCT analogs.
NMR investigations of structural and dynamics features of natively unstructured drug peptide - salmon calcitonin: implication to rational design of potent sCT analogs.
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J Pept Sci. 2013 Jan;19(1):33-45
Authors: Rawat A, Kumar D
...
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[NMR paper] NMR investigations of protein-carbohydrate interactions: insights into the topology o
NMR investigations of protein-carbohydrate interactions: insights into the topology of the bound conformation of a lactose isomer and beta-galactosyl xyloses to mistletoe lectin and galectin-1.
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Biochim Biophys Acta. 2001 Dec 19;1568(3):225-36
Authors: Alonso-Plaza JM, Canales MA, Jiménez M, Roldán JL, García-Herrero A, Iturrino L, Asensio JL,...
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[NMR paper] NMR investigations of protein-carbohydrate interactions binding studies and refined t
NMR investigations of protein-carbohydrate interactions binding studies and refined three-dimensional solution structure of the complex between the B domain of wheat germ agglutinin and N,N', N"-triacetylchitotriose.
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Eur J Biochem. 2000 Jul;267(13):3965-78
Authors: Espinosa JF, Asensio JL, García JL, Laynez J, Bruix M, Wright...
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[NMR paper] NMR investigations of protein-carbohydrate interactions: studies on the relevance of
NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N"-triacetylchitotriose.
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[NMR paper] NMR investigations of protein-carbohydrate interactions: refined three-dimensional st
NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside.
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Glycobiology. 1998 Jun;8(6):569-77
Authors: Asensio JL, Cañada FJ, Bruix M, González C, Khiar N, Rodríguez-Romero A, Jiménez-Barbero J
The specific interaction of hevein with GlcNAc-containing oligosaccharides has been...
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[NMR paper] Yeast heat shock transcription factor N-terminal activation domains are unstructured
Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
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Protein Sci. 1996 Feb;5(2):262-9...
NMR investigations of metal interactions with unstructured soluble protein domains
Linear Mode
