His scientific interests lie mostly in Mass spectrometry, Protein structure, Analytical chemistry, Ion and Biophysics. The study incorporates disciplines such as Structural biology and Macromolecule in addition to Mass spectrometry. His Structural biology research is multidisciplinary, incorporating perspectives in Computational chemistry and Biological system.
Brandon T. Ruotolo works mostly in the field of Protein structure, limiting it down to concerns involving Plasma protein binding and, occasionally, Peptide, Reactivity and Two-dimensional nuclear magnetic resonance spectroscopy. His studies deal with areas such as Microfluidics and Denaturation as well as Analytical chemistry. His Ion research includes themes of Nanotechnology and Hybrid mass spectrometer.
His primary areas of study are Mass spectrometry, Ion, Analytical chemistry, Ion-mobility spectrometry and Biophysics. His Mass spectrometry research integrates issues from Crystallography, Structural biology, Dissociation, Resolution and Protein structure. He studied Ion and Chemical physics that intersect with Characterization.
His Analytical chemistry research is multidisciplinary, relying on both Adduct and Matrix-assisted laser desorption/ionization. His work focuses on many connections between Ion-mobility spectrometry and other disciplines, such as Peptide, that overlap with his field of interest in Stereochemistry. His Biophysics study deals with Biochemistry intersecting with Zinc and Amyloid.
Brandon T. Ruotolo focuses on Biophysics, Mass spectrometry, Ion, Collision and Membrane protein. His research in Biophysics intersects with topics in Biotin, Protein–protein interaction and Protein folding. His work is dedicated to discovering how Protein folding, Chaperone are connected with Neurodegeneration and Nucleation and other disciplines.
The various areas that Brandon T. Ruotolo examines in his Mass spectrometry study include Tetramer and Peptide. His work carried out in the field of Tetramer brings together such families of science as Apolipoprotein E, Dissociation and Electrospray ionization. His work in Ion addresses subjects such as Chemical physics, which are connected to disciplines such as Ion transporter.
His primary scientific interests are in Biophysics, Unfolded protein response, Mass spectrometry, Membrane and Membrane protein. His biological study spans a wide range of topics, including Size-exclusion chromatography, Ion-mobility spectrometry and Resolution. Unfolded protein response overlaps with fields such as Chemical physics, Gas phase, Structural biology, Dimer and Translocator protein in his research.
Brandon T. Ruotolo specializes in Mass spectrometry, namely Mass spectrum. In general Membrane, his work in Lipid composition is often linked to Model lipid bilayer linking many areas of study.
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Ion mobility-mass spectrometry analysis of large protein complexes.
Brandon T. Ruotolo;Justin L.P. Benesch;Alan M. Sandercock;Suk Joon Hyung.
Nature Protocols (2008)
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
Summer L. Bernstein;Nicholas F. Dupuis;Noel D. Lazo;Thomas Wyttenbach.
Nature Chemistry (2009)
Collision Cross Sections of Proteins and Their Complexes: A Calibration Framework and Database for Gas-Phase Structural Biology
Matthew F. Bush;Zoe Hall;Kevin Giles;John Hoyes.
Analytical Chemistry (2010)
Evidence for macromolecular protein rings in the absence of bulk water.
Brandon T. Ruotolo;Kevin Giles;Iain Campuzano;Alan M. Sandercock.
Protein complexes in the gas phase: technology for structural genomics and proteomics.
Justin L. P. Benesch;Brandon T. Ruotolo;Douglas A. Simmons;Carol V. Robinson.
Chemical Reviews (2007)
Ion mobility–mass spectrometry: a new paradigm for proteomics
John A. McLean;Brandon T. Ruotolo;Kent J. Gillig;David H. Russell.
International Journal of Mass Spectrometry (2005)
Mass spectrometry: come of age for structural and dynamical biology
Justin L P Benesch;Brandon T Ruotolo.
Current Opinion in Structural Biology (2011)
Ion mobility-mass spectrometry reveals long-lived, unfolded intermediates in the dissociation of protein complexes.
Brandon T. Ruotolo;Suk Joon Hyung;Paula M. Robinson;Kevin Giles.
Angewandte Chemie (2007)
Aspects of native proteins are retained in vacuum.
Brandon T Ruotolo;Carol V Robinson.
Current Opinion in Chemical Biology (2006)
Coupling microdroplet microreactors with mass spectrometry: reading the contents of single droplets online.
Luis M Fidalgo;Graeme Whyte;Brandon T Ruotolo;Justin L P Benesch.
Angewandte Chemie (2009)
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