What is he best known for?
The fields of study he is best known for:
The scientist’s investigation covers issues in Biochemistry, Protein structure, Stereochemistry, Biophysics and Protein tertiary structure.
His study in Biochemistry is interdisciplinary in nature, drawing from both Beta-sandwich and Sequence alignment.
The study incorporates disciplines such as Crystallography, ATPase, eIF4A and DEAD box in addition to Protein structure.
As a part of the same scientific family, David B. McKay mostly works in the field of ATPase, focusing on Phosphotransferase and, on occasion, Conformational change and Chaperone.
His Stereochemistry research incorporates themes from Tetraloop, Base pair, Nucleic acid tertiary structure, Group I catalytic intron and Terminal loop.
His Protein tertiary structure research includes themes of Interleukin 2, Angstrom, Resolution and Effector.
His most cited work include:
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein (911 citations)
- Three-dimensional structure of a hammerhead ribozyme (804 citations)
- The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. (580 citations)
What are the main themes of his work throughout his whole career to date?
Biochemistry, Stereochemistry, ATPase, Crystallography and Protein structure are his primary areas of study.
In most of his Biochemistry studies, his work intersects topics such as Wild type.
The concepts of his Stereochemistry study are interwoven with issues in Hydrolase, Active site, Sequence motif, eIF4A and DEAD box.
His ATPase research is multidisciplinary, incorporating elements of Conformational change and Serine.
David B. McKay works mostly in the field of Crystallography, limiting it down to topics relating to Ribozyme and, in certain cases, Phosphodiester bond, as a part of the same area of interest.
His Protein structure research incorporates elements of Biophysics and Protein folding.
He most often published in these fields:
- Biochemistry (51.32%)
- Stereochemistry (26.32%)
- ATPase (23.68%)
What were the highlights of his more recent work (between 2002-2014)?
- Biochemistry (51.32%)
- Molecular biology (10.53%)
- Protein family (7.89%)
In recent papers he was focusing on the following fields of study:
David B. McKay spends much of his time researching Biochemistry, Molecular biology, Protein family, Helicase and Protein structure.
His work deals with themes such as Periplasmic space, 50S, Ribosome, 5.8S ribosomal RNA and Stem-loop, which intersect with Biochemistry.
His work on RNA Helicase A as part of general Helicase study is frequently linked to Bacillus subtilis, therefore connecting diverse disciplines of science.
His work carried out in the field of Protein structure brings together such families of science as S-tag, Endoribonuclease, RNase MRP, RNase P and RNase PH.
His research in DEAD box intersects with topics in Hydrolase and Stereochemistry.
He mostly deals with Conformational change in his studies of Stereochemistry.
Between 2002 and 2014, his most popular works were:
- The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. (580 citations)
- Structure of the Escherichia coli FlhDC complex, a prokaryotic heteromeric regulator of transcription. (126 citations)
- The Periplasmic Molecular Chaperone Protein SurA Binds a Peptide Motif That Is Characteristic of Integral Outer Membrane Proteins (125 citations)
In his most recent research, the most cited papers focused on:
His primary areas of study are Biochemistry, Protein structure, Peptide, Periplasmic space and Molecular biology.
When carried out as part of a general Biochemistry research project, his work on Collagenase is frequently linked to work in Protein family and Adamalysin, therefore connecting diverse disciplines of study.
David B. McKay has included themes like Binding domain, Protein folding, Aromatic amino acids and Binding selectivity in his Protein structure study.
His Phage display and Tripeptide study in the realm of Peptide interacts with subjects such as Peptide binding.
Periplasmic space and Amino acid are commonly linked in his work.
His Molecular biology study incorporates themes from Helicase, Footprinting, Protein Data Bank, Operon and Protomer.
This overview was generated by a machine learning system which analysed the scientist’s
body of work. If you have any feedback, you can
contact us
here.
