2023 - Research.com Chemistry in Canada Leader Award
Crystallography, Biochemistry, Nuclear magnetic resonance spectroscopy, Protein structure and Stereochemistry are his primary areas of study. Brian D. Sykes interconnects Proton NMR, Beta sheet, Molecule and Antifreeze protein in the investigation of issues within Crystallography. His Biochemistry study combines topics in areas such as Molecular biology, Biophysics and Calcium.
Nuclear magnetic resonance spectroscopy is a subfield of Nuclear magnetic resonance that Brian D. Sykes investigates. His Protein structure research incorporates themes from Protein secondary structure, Receptor, Hydrogen bond, Binding site and Chemical shift. He has included themes like Dihedral angle, Chemical shift index and Analytical chemistry in his Protein secondary structure study.
Brian D. Sykes mainly investigates Nuclear magnetic resonance spectroscopy, Biochemistry, Troponin C, Stereochemistry and Crystallography. His study explores the link between Nuclear magnetic resonance spectroscopy and topics such as Analytical chemistry that cross with problems in Chemical shift. In his research, Muscle contraction is intimately related to Biophysics, which falls under the overarching field of Biochemistry.
His Troponin C research includes themes of Cardiac muscle, Calcium, Troponin complex, Actin and Binding site. He has researched Stereochemistry in several fields, including Protein secondary structure and Peptide. His Crystallography research integrates issues from Proton NMR, Molecule, Antifreeze protein and Dissociation constant.
His main research concerns Biochemistry, Troponin C, Biophysics, Peptide and Cardiac muscle. Brian D. Sykes interconnects Nuclear magnetic resonance spectroscopy and Acidosis in the investigation of issues within Biochemistry. His Nuclear magnetic resonance spectroscopy study combines topics in areas such as Protein structure and Chemical shift.
His Troponin C research is multidisciplinary, incorporating perspectives in Troponin complex, Histidine, Nuclear magnetic resonance and Actin. The study incorporates disciplines such as Heteronuclear single quantum coherence spectroscopy, Calcium and Muscle contraction in addition to Biophysics. The Peptide study combines topics in areas such as Crystallography, Stereochemistry and Transmembrane protein.
His primary areas of investigation include Biochemistry, Troponin C, Biophysics, Nuclear magnetic resonance spectroscopy and Stereochemistry. His Biochemistry research is multidisciplinary, incorporating elements of Levosimendan and Muscle contraction. His Biophysics research includes elements of Mutation, Mutant protein, Wild type and Chemical shift.
His biological study spans a wide range of topics, including Urea, Recombinant DNA, Peptide sequence, Protein structure and Heat capacity. Brian D. Sykes combines subjects such as Calmodulin and Peptide with his study of Stereochemistry. His research integrates issues of Crystallography and Binding site in his study of Actin.
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HMDB: The human metabolome database
David S. Wishart;Dan Tzur;Craig Knox;Roman Eisner.
Nucleic Acids Research (2007)
The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
D. S. Wishart;B. D. Sykes;F. M. Richards.
1H, 13C and 15N chemical shift referencing in biomolecular NMR
D S Wishart;C G Bigam;J Yao;F Abildgaard.
Journal of Biomolecular NMR (1995)
The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.
David S. Wishart;Brian D. Sykes.
Journal of Biomolecular NMR (1994)
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure.
D.S. Wishart;B.D. Sykes;F.M. Richards.
Journal of Molecular Biology (1991)
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects.
David S. Wishart;Colin G. Bigam;Arne Holm;Robert S. Hodges.
Journal of Biomolecular NMR (1995)
Chemical shifts as a tool for structure determination.
David S Wishart;Brian D Sykes.
Methods in Enzymology (1994)
Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1.
Matthew P. Crump;Jiang Hong Gong;Pius Loetscher;Krishna Rajarathnam.
The EMBO Journal (1997)
VADAR: a web server for quantitative evaluation of protein structure quality
Leigh Willard;Anuj Ranjan;Haiyan Zhang;Hassan Monzavi.
Nucleic Acids Research (2003)
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
F. D. Sonnichsen;J. E. Van Eyk;R. S. Hodges;B. D. Sykes.
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