What is he best known for?
The fields of study he is best known for:
- DNA
- Amino acid
- Biochemistry
Martin Blackledge spends much of his time researching Protein structure, Intrinsically disordered proteins, Crystallography, Nuclear magnetic resonance spectroscopy and Protein folding.
His Protein structure study combines topics from a wide range of disciplines, such as Chemical physics, Protein secondary structure, Characterization, Statistical physics and Binding site.
His Intrinsically disordered proteins research integrates issues from Structural biology and Conformational sampling.
His research integrates issues of Polyproline helix, Small-angle X-ray scattering, Scattering, Residual dipolar coupling and Relaxation in his study of Crystallography.
His Nuclear magnetic resonance spectroscopy research incorporates elements of Phosphorylation sites and Human heart.
The Nuclear magnetic resonance study combines topics in areas such as Skeletal muscle, Dipole and Molecular dynamics.
His most cited work include:
- Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering (854 citations)
- Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data. (409 citations)
- A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering (326 citations)
What are the main themes of his work throughout his whole career to date?
Martin Blackledge mainly investigates Crystallography, Intrinsically disordered proteins, Nuclear magnetic resonance spectroscopy, Protein structure and Chemical physics.
His Crystallography study integrates concerns from other disciplines, such as Protein tertiary structure, Small-angle X-ray scattering, Scattering, Polyproline helix and Molecule.
His studies deal with areas such as Structural biology and Computational biology as well as Intrinsically disordered proteins.
His study in Nuclear magnetic resonance spectroscopy is interdisciplinary in nature, drawing from both Computational chemistry, Molecular dynamics and Protein–protein interaction.
His research in Protein structure focuses on subjects like Protein folding, which are connected to Folding.
He combines subjects such as Protein dynamics, Dipole, Relaxation and Chemical shift with his study of Chemical physics.
He most often published in these fields:
- Crystallography (31.45%)
- Intrinsically disordered proteins (32.26%)
- Nuclear magnetic resonance spectroscopy (27.42%)
What were the highlights of his more recent work (between 2015-2021)?
- Intrinsically disordered proteins (32.26%)
- Biophysics (17.74%)
- Nuclear magnetic resonance spectroscopy (27.42%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Intrinsically disordered proteins, Biophysics, Nuclear magnetic resonance spectroscopy, Molecular dynamics and Nucleoprotein.
His studies in Intrinsically disordered proteins integrate themes in fields like Chemical physics, Spectroscopy, Relaxation and Protein structure.
His work carried out in the field of Chemical physics brings together such families of science as Molecule and Nuclear magnetic resonance.
His Biophysics research includes elements of Microtubule-associated protein, Nucleoporin and Binding site.
The concepts of his Nuclear magnetic resonance spectroscopy study are interwoven with issues in EIF4G, Cover, Protein folding and Protein–protein interaction.
He has researched Molecular dynamics in several fields, including Single-molecule experiment, Dynamics, Crystallography, Nuclear pore and Receptor.
Between 2015 and 2021, his most popular works were:
- Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment (61 citations)
- Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation (48 citations)
- Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation (44 citations)
In his most recent research, the most cited papers focused on:
- DNA
- Amino acid
- Biochemistry
The scientist’s investigation covers issues in Intrinsically disordered proteins, Chemical physics, Molecular dynamics, Relaxation and Biophysics.
The study incorporates disciplines such as Spectroscopy, Plasma protein binding, Nuclear magnetic resonance spectroscopy and Computational biology in addition to Intrinsically disordered proteins.
His Nuclear magnetic resonance spectroscopy research is multidisciplinary, incorporating perspectives in Mutagenesis and Protein folding.
His study focuses on the intersection of Chemical physics and fields such as Molecule with connections in the field of Ion, Ionic bonding and Small-angle X-ray scattering.
Martin Blackledge has included themes like Crystallography, Neutron diffraction, Hydrogen bond and Dynamics in his Molecular dynamics study.
His Relaxation research is multidisciplinary, incorporating elements of Protein dynamics, Protein structure and Solvent.
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.
