The scientist’s investigation covers issues in Nuclear magnetic resonance spectroscopy, Biophysics, Phospholamban, Crystallography and Protein structure. The various areas that Gianluigi Veglia examines in his Nuclear magnetic resonance spectroscopy study include Micelle, Metal binding and Molecular dynamics. His Biophysics research incorporates elements of Biochemistry, Allosteric regulation, Systematic evolution of ligands by exponential enrichment and Biological membrane.
His study in Phospholamban is interdisciplinary in nature, drawing from both Integral membrane protein, SERCA and Transmembrane domain. His studies deal with areas such as Structural biology, Bilayer, Lipid bilayer and Chemical biology as well as Crystallography. His Lipid bilayer research includes elements of Membrane fluidity, Solid-state nuclear magnetic resonance and Cell membrane.
Gianluigi Veglia spends much of his time researching Biophysics, Phospholamban, Biochemistry, SERCA and Nuclear magnetic resonance spectroscopy. His studies deal with areas such as Protein kinase A, Protein subunit, Sarcolipin, Protein structure and Allosteric regulation as well as Biophysics. His work carried out in the field of Phospholamban brings together such families of science as Integral membrane protein, Lipid bilayer and Mutant.
His Lipid bilayer study integrates concerns from other disciplines, such as Crystallography, Solid-state nuclear magnetic resonance, Membrane protein and Transmembrane domain. His biological study spans a wide range of topics, including Calcium-binding protein and Calcium. His Nuclear magnetic resonance spectroscopy study combines topics in areas such as Helix, Two-dimensional nuclear magnetic resonance spectroscopy and NMR spectra database.
His scientific interests lie mostly in Biophysics, Protein kinase A, Phospholamban, Solid-state nuclear magnetic resonance and Cell biology. The Biophysics study combines topics in areas such as Cysteine, Circular dichroism and Sarcolipin. His study in Protein kinase A is interdisciplinary in nature, drawing from both Protein subunit and Stereochemistry.
His Phospholamban research is multidisciplinary, incorporating elements of Sarcoplasmic reticulum calcium, SERCA, Sarcoplasmic reticulum membrane, Protein x and Computational biology. His Solid-state nuclear magnetic resonance research includes elements of Magic angle spinning, Nuclear magnetic resonance spectroscopy, Endoplasmic reticulum and Membrane protein. His studies in Peptide integrate themes in fields like Protein structure and Active site.
Gianluigi Veglia mainly focuses on Solid-state nuclear magnetic resonance, Protein kinase A, Magic angle spinning, Cell biology and Analytical chemistry. As part of one scientific family, Gianluigi Veglia deals mainly with the area of Solid-state nuclear magnetic resonance, narrowing it down to issues related to the Membrane protein, and often Lipid bilayer, Chemical physics, Macromolecule, Self-assembly and Molecular dynamics. The various areas that Gianluigi Veglia examines in his Protein kinase A study include Protein subunit and Allosteric regulation.
His research in Allosteric regulation intersects with topics in Biophysics, Conformational entropy and Cooperativity. His Peptide research integrates issues from Protein structure, Peptide sequence, Stereochemistry and Binding site. His Deconvolution research is multidisciplinary, incorporating perspectives in Nuclear magnetic resonance spectroscopy and NMR spectra database.
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Direct Observation of the Three Regions in α-Synuclein that Determine its Membrane-Bound Behaviour
Giuliana Fusco;Alfonso De Simone;Tata Gopinath;Vitaly Vostrikov.
Nature Communications (2014)
Using low-E resonators to reduce RF heating in biological samples for static solid-state NMR up to 900 MHz
Peter L. Gor’kov;Eduard Y. Chekmenev;Eduard Y. Chekmenev;Conggang Li;Myriam Cotten.
Journal of Magnetic Resonance (2007)
Dynamics connect substrate recognition to catalysis in protein kinase A
Larry R Masterson;Cecilia Cheng;Tao Yu;Marco Tonelli.
Nature Chemical Biology (2010)
NMR Solution Structure and Topological Orientation of Monomeric Phospholamban in Dodecylphosphocholine Micelles
Jamillah Zamoon;Alessandro Mascioni;David D. Thomas;Gianluigi Veglia.
Biophysical Journal (2003)
Structures of Rat and Human Islet Amyloid Polypeptide IAPP1−19 in Micelles by NMR Spectroscopy†
Ravi Prakash Reddy Nanga;Jeffrey R. Brender;Jiadi Xu;Gianluigi Veglia.
NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles
Fernando Porcelli;Raffaello Verardi;Lei Shi;Katherine A. Henzler-Wildman.
Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach
Nathaniel J. Traaseth;Lei Shi;Raffaello Verardi;Daniel G. Mullen.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Allosteric cooperativity in protein kinase A.
Larry R. Masterson;Alessandro Mascioni;Nathaniel J. Traaseth;Susan S. Taylor.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Structure and Orientation of Pardaxin Determined by NMR Experiments in Model Membranes
Fernando Porcelli;Bethany Buck;Dong-Kuk Lee;Kevin J. Hallock.
Journal of Biological Chemistry (2004)
Structural basis of synaptic vesicle assembly promoted by α-synuclein
Giuliana Fusco;Tillmann Pape;Amberley D. Stephens;Pierre Mahou;Pierre Mahou.
Nature Communications (2016)
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