His scientific interests lie mostly in Crystallography, Neutron scattering, Protein structure, Scattering and Genetics. His biological study spans a wide range of topics, including Sedimentation coefficient, Stereochemistry, Protein secondary structure and Protein folding. The various areas that he examines in his Stereochemistry study include Amino acid, Low protein and Chemical shift.
With his scientific publications, his incorporates both Neutron scattering and Radius of gyration. Within one scientific family, Stephen J. Perkins focuses on topics pertaining to Lysozyme under Protein structure, and may sometimes address concerns connected to Aromatic amino acids, Nuclear magnetic resonance spectroscopy, Triclinic crystal system and Physical chemistry. His Scattering research integrates issues from Conformational isomerism, Neutron, Resolution and Fragment crystallizable region.
Stephen J. Perkins focuses on Crystallography, Scattering, Neutron scattering, Protein structure and Radius of gyration. His research integrates issues of Complement system, Sedimentation coefficient, Protein secondary structure and Stereochemistry in his study of Crystallography. His Complement system research is multidisciplinary, relying on both Biochemistry and Complement.
Stephen J. Perkins has researched Stereochemistry in several fields, including Amino acid, Alternative complement pathway, Binding site and Lysozyme. Stephen J. Perkins interconnects Analytical Ultracentrifugation, Neutron, X-ray and Molecular physics in the investigation of issues within Scattering. His Small-angle neutron scattering study in the realm of Neutron scattering connects with subjects such as Gyration.
His primary areas of investigation include Crystallography, Biophysics, Scattering, Radius of gyration and Neutron scattering. The Crystallography study combines topics in areas such as Heparin, Dimer, Sedimentation coefficient and Macroglobulin. The concepts of his Biophysics study are interwoven with issues in Alternative complement pathway, Solution structure, Heparan sulfate, Small-angle neutron scattering and Binding site.
His research on Binding site also deals with topics like
Crystallography, Neutron scattering, Protein structure, Molecular model and Radius of gyration are his primary areas of study. Stephen J. Perkins combines Crystallography and Computational science in his research. Neutron scattering is a subfield of Scattering that Stephen J. Perkins studies.
His Protein structure research includes elements of Complement factor I, Complement system, Genetics, Gene and Mutation database. His work in Complement factor I addresses issues such as Missense mutation, which are connected to fields such as Alternative complement pathway. His Molecular model study incorporates themes from Complement C3c, Carbohydrate conformation, Sedimentation coefficient and Heparin.
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Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences.
Stephen J. Perkins.
FEBS Journal (1986)
The fab and fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling
Mark K Boehm;Jenny M Woof;Michael A Kerr;Stephen J Perkins.
Journal of Molecular Biology (1999)
The interactive Factor H-atypical hemolytic uremic syndrome mutation database and website: update and integration of membrane cofactor protein and Factor I mutations with structural models.
Rebecca E. Saunders;Cynthia Abarrategui-Garrido;Véronique Frémeaux-Bacchi;Elena Goicoechea de Jorge.
Human Mutation (2007)
Autosomal dominant reticuloendothelial iron overload associated with a 3–base pair deletion in the ferroportin 1 gene(SLC11A3)
Vinod Devalia;Kymberley Carter;Ann P. Walker;Stephen J. Perkins.
Deletion of Lys224 in regulatory domain 4 of Factor H reveals a novel pathomechanism for dense deposit disease (MPGN II)
C. Licht;S. Heinen;M. Józsi;I. Löschmann.
Kidney International (2006)
Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling.
Mohammed Aslam;Stephen J Perkins.
Journal of Molecular Biology (2001)
Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation.
Stephen J. Perkins;Adam S. Nealis;Brian J. Sutton;Arnold Feinstein.
Journal of Molecular Biology (1991)
His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form.
Simon J. Clark;Victoria A. Higman;Barbara Mulloy;Stephen J. Perkins.
Journal of Biological Chemistry (2006)
High resolution1H- and13C-N.M.R spectra ofD-glucopyranose, 2-acetamido-2-deoxy-D-glucopyranose, and related compounds in aqueous media
Stephen J. Perkins;Louise N. Johnson;David C. Phillips;Raymond A. Dwek.
Carbohydrate Research (1977)
Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome C
Iain D. Campbell;Christopher M. Dobson;Geoffrey R. Moore;Stephen J. Perkins.
FEBS Letters (1976)
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