2013 - Harrison-Meldola Memorial Prize, Royal Society of Chemistry (UK)
Andrew J. Baldwin mainly investigates Biophysics, Protein structure, Structural biology, Crystallography and Protein aggregation. His work investigates the relationship between Biophysics and topics such as Nanotechnology that intersect with problems in Proteome. Protein structure is a subfield of Biochemistry that Andrew J. Baldwin explores.
His research in Structural biology intersects with topics in Biological system and Ion-mobility spectrometry. His Crystallography research includes themes of Chemical physics and Phase. Within one scientific family, Andrew J. Baldwin focuses on topics pertaining to Nuclear magnetic resonance spectroscopy under Protein dynamics, and may sometimes address concerns connected to Protein folding.
His primary areas of investigation include Biophysics, Nuclear magnetic resonance spectroscopy, Crystallography, Chemical physics and Environmental ethics. The study incorporates disciplines such as Protein structure, Biochemistry, Protein aggregation and Chaperone in addition to Biophysics. Many of his studies on Protein structure apply to Protein folding as well.
He has included themes like Conformational isomerism, Relaxation and Chemical shift in his Nuclear magnetic resonance spectroscopy study. His study looks at the intersection of Crystallography and topics like Fibril with Molecule. His Chemical physics research includes elements of Supramolecular chemistry and Structural biology.
His scientific interests lie mostly in Binding site, Cell biology, Biophysics, Oxidoreductase and Frustration. His work on Cytoplasm as part of general Cell biology study is frequently connected to Cellular homeostasis, Hsp27, Drosophila melanogaster and Caenorhabditis elegans, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. Andrew J. Baldwin combines subjects such as Protein dynamics and Protein aggregation with his study of Biophysics.
His Protein dynamics study introduces a deeper knowledge of Protein structure. His Protein aggregation research focuses on Dimer and how it relates to Chaperone. Andrew J. Baldwin has researched In vitro in several fields, including Fibril and Crystallography.
Andrew J. Baldwin focuses on Mobilities, Cell biology, Chaperone, Protein structure and Protein folding. The concepts of his Mobilities study are interwoven with issues in Mythology, Environmental ethics, Anthropocene and Darwinism. His work in the fields of Cell biology, such as Phosphorylation, intersects with other areas such as FLNC, Mechanosensitive channels, Protein domain and Stress granule.
His Chaperone study incorporates themes from Dimer, Nuclear magnetic resonance spectroscopy, Dissociation and Chemical shift. Andrew J. Baldwin interconnects Biophysics and Protein aggregation in the investigation of issues within Dimer. When carried out as part of a general Protein structure research project, his work on Protein dynamics is frequently linked to work in Unfolded protein response and Mutation, therefore connecting diverse disciplines of study.
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Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles
Timothy J. Nott;Timothy J. Nott;Evangelia Petsalaki;Patrick Farber;Dylan Jervis.
Molecular Cell (2015)
Membrane proteins bind lipids selectively to modulate their structure and function
Arthur Laganowsky;Eamonn Reading;Timothy M. Allison;Martin B. Ulmschneider.
NMR spectroscopy brings invisible protein states into focus
Andrew J Baldwin;Lewis E Kay.
Nature Chemical Biology (2009)
Metastability of native proteins and the phenomenon of amyloid formation.
Andrew J. Baldwin;Tuomas P. J. Knowles;Gian Gaetano Tartaglia;Anthony W. Fitzpatrick.
Journal of the American Chemical Society (2011)
Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.
Michael T. Marty;Andrew J. Baldwin;Erik G. Marklund;Georg K. A. Hochberg.
Analytical Chemistry (2015)
The role of interfacial lipids in stabilizing membrane protein oligomers
Kallol Gupta;Joseph A. C. Donlan;Jonathan T. S. Hopper;Povilas Uzdavinys.
HYDROLOGIC CHANGE AND VEGETATION OF TIDAL FRESHWATER MARSHES: FIELD, GREENHOUSE, AND SEED-BANK EXPERIMENTS
Andrew H. Baldwin;Michael S. Egnotovich;Ernest Clarke.
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function
Florian Stengel;Andrew J. Baldwin;Alexander J. Painter;Nomalie Jaya.
Proceedings of the National Academy of Sciences of the United States of America (2010)
The influence of vegetation, salinity, and inundation on seed banks of oligohaline coastal marshes
Andrew H. Baldwin;Karen L. McKee;Irving A. Mendelssohn.
American Journal of Botany (1996)
Membraneless organelles can melt nucleic acid duplexes and act as biomolecular filters.
Timothy J. Nott;Timothy D. Craggs;Andrew J. Baldwin.
Nature Chemistry (2016)
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