What is he best known for?
The fields of study he is best known for:
Ronald T. Raines mainly investigates Stereochemistry, Biochemistry, Protein structure, Bovine pancreatic ribonuclease and RNase P. His Stereochemistry research is multidisciplinary, relying on both Peptide bond and Protein folding. His study in Ribonuclease, Enzyme, Protein disulfide-isomerase, Thioredoxin and Thiol are all subfields of Biochemistry.
His work carried out in the field of Ribonuclease brings together such families of science as Ribonuclease III and RNase MRP. His work is dedicated to discovering how Protein structure, Polyproline helix are connected with Stereoelectronic effect and other disciplines. Ronald T. Raines interconnects Molecular biology, RNA Cleavage and Cytotoxicity in the investigation of issues within RNase P.
His most cited work include:
- Collagen Structure and Stability (1683 citations)
- Simple Chemical Transformation of Lignocellulosic Biomass into Furans for Fuels and Chemicals (1143 citations)
- Bright Ideas for Chemical Biology (822 citations)
What are the main themes of his work throughout his whole career to date?
Ronald T. Raines mainly focuses on Biochemistry, Stereochemistry, Ribonuclease, RNase P and Enzyme. The Stereochemistry study combines topics in areas such as Peptide bond, Protein structure and Hydrogen bond. Ronald T. Raines has included themes like Proline and Amide in his Peptide bond study.
His Protein structure research includes elements of Crystallography and Protein folding. In his research on the topic of Ribonuclease, Cancer research is strongly related with Cancer cell. His RNase P study combines topics from a wide range of disciplines, such as Molecular biology and Cytotoxicity.
He most often published in these fields:
- Biochemistry (36.27%)
- Stereochemistry (26.94%)
- Ribonuclease (24.47%)
What were the highlights of his more recent work (between 2015-2021)?
- Biochemistry (36.27%)
- Stereochemistry (26.94%)
- Enzyme (15.49%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Biochemistry, Stereochemistry, Enzyme, Ribonuclease and Combinatorial chemistry. As a part of the same scientific family, Ronald T. Raines mostly works in the field of Biochemistry, focusing on Triple helix and, on occasion, Sticky and blunt ends. His Stereochemistry research is multidisciplinary, relying on both Covalent bond, Transthyretin, Wild type, Boronic acid and Hydrogen bond.
His Enzyme research integrates issues from Metabolite and Chemical biology. His studies deal with areas such as Cytotoxic T cell, RNase P, Cancer research and Cytosol as well as Ribonuclease. His studies examine the connections between Combinatorial chemistry and genetics, as well as such issues in Cycloaddition, with regards to Click chemistry, Hyperconjugation and Photochemistry.
Between 2015 and 2021, his most popular works were:
- The n→π* Interaction (115 citations)
- Enzyme-Activated Fluorogenic Probes for Live-Cell and in Vivo Imaging (58 citations)
- Diazo Compounds: Versatile Tools for Chemical Biology. (57 citations)
In his most recent research, the most cited papers focused on:
His scientific interests lie mostly in Stereochemistry, Ribonuclease, Biochemistry, Cell biology and Diazo. He combines subjects such as Covalent bond, Non-covalent interactions, Hydrogen bond, Amyloidosis and Homotetramer with his study of Stereochemistry. His research in Hydrogen bond intersects with topics in Protein structure, Carbonyl group, Protein folding and Amide.
His work carried out in the field of Ribonuclease brings together such families of science as HeLa, RNase P and Cytosol. His is doing research in Enzyme, Green fluorescent protein, Cofactor, Hydroxylation and Proline, both of which are found in Biochemistry. His Enzyme study combines topics in areas such as Chemical biology and Vitamin C.
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