What is he best known for?
The fields of study he is best known for:
Ivan Rayment mainly investigates Protein structure, Biochemistry, Stereochemistry, Myosin and Crystallography.
His Protein structure research is multidisciplinary, incorporating perspectives in ATP hydrolysis, Polyoma virus, Capsid, Resolution and Binding site.
His Stereochemistry research is multidisciplinary, relying on both Pyruvate carboxylase, Cofactor, Enzyme, Side chain and Biotin.
The Myosin study combines topics in areas such as Dictyostelium discoideum and Actin.
The concepts of his Actin study are interwoven with issues in Amino acid, Globular protein and Molecular mechanism.
His Crystallography research incorporates themes from Magnesium ion, Protein subunit, Active site, Cysteine and Hydrogen bond.
His most cited work include:
- Three-dimensional structure of myosin subfragment-1: a molecular motor (1744 citations)
- Structure of the actin-myosin complex and its implications for muscle contraction. (1444 citations)
- X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. (550 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of investigation include Stereochemistry, Biochemistry, Crystallography, Active site and Protein structure.
His Stereochemistry study combines topics from a wide range of disciplines, such as Dimer, Protein subunit, Transferase and Substrate.
His Crystallography research includes elements of X-ray crystallography, Crystallization and Molecule.
Adenosine triphosphate is closely connected to Binding site in his research, which is encompassed under the umbrella topic of Active site.
The various areas that Ivan Rayment examines in his Protein structure study include Biophysics and Myosin.
His work carried out in the field of Biophysics brings together such families of science as Kinesin, Microtubule and Actin.
He most often published in these fields:
- Stereochemistry (33.93%)
- Biochemistry (33.57%)
- Crystallography (29.64%)
What were the highlights of his more recent work (between 2009-2020)?
- Biochemistry (33.57%)
- Microtubule (7.14%)
- Biophysics (12.86%)
In recent papers he was focusing on the following fields of study:
His scientific interests lie mostly in Biochemistry, Microtubule, Biophysics, Kinesin and Protein structure.
His Biophysics research includes themes of Crystallography and Organelle.
His Icosahedral symmetry study in the realm of Crystallography connects with subjects such as Spectral line.
Protein structure and Antiparallel are commonly linked in his work.
His Enzyme research is multidisciplinary, relying on both Rhodopseudomonas palustris and Stereochemistry.
His Motor protein study combines topics in areas such as Computational biology, Myosin head, Actin and Myosin.
Between 2009 and 2020, his most popular works were:
- Structure of the tropomyosin overlap complex from chicken smooth muscle: insight into the diversity of N-terminal recognition,. (62 citations)
- Cryo-electron tomography of microtubule-kinesin motor complexes (37 citations)
- The molecular architecture of the yeast spindle pole body core determined by Bayesian integrative modeling (30 citations)
In his most recent research, the most cited papers focused on:
Microtubule, Biophysics, Kinesin, Coiled coil and Biochemistry are his primary areas of study.
The study incorporates disciplines such as Protein structure and Crystallography in addition to Biophysics.
His Protein structure study incorporates themes from ATPase, Helix and Organelle.
His Kinesin study integrates concerns from other disciplines, such as Microtubule nucleation and Molecular motor.
In the subject of general Biochemistry, his work in Enzyme, Escherichia coli and Substrate is often linked to Integral membrane protein and Sucrose synthase, thereby combining diverse domains of study.
His research investigates the connection between Binding site and topics such as Motor protein that intersect with problems in Antiparallel, Cardiac Myosins, Myosin head, Structural similarity and Myosin.
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