What is he best known for?
The fields of study he is best known for:
The scientist’s investigation covers issues in Stereochemistry, Biochemistry, Peptide, Protein structure and Azobenzene.
His Stereochemistry research is multidisciplinary, incorporating elements of Proteasome, Cystine and Active site.
The study incorporates disciplines such as Peptide sequence, Binding site and Cleavage in addition to Peptide.
Luis Moroder interconnects Chemical physics, Relaxation, Protein folding, Mass spectrometry and Histone in the investigation of issues within Protein structure.
His biological study spans a wide range of topics, including Crystallography and Genetics.
He has researched Azobenzene in several fields, including Photochemistry, Chromophore and Isomerization, Photoisomerization.
His most cited work include:
- Structure of TPR Domain–Peptide Complexes: Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine (1023 citations)
- A gated channel into the proteasome core particle. (659 citations)
- Single-Molecule Optomechanical Cycle (599 citations)
What are the main themes of his work throughout his whole career to date?
Luis Moroder mostly deals with Stereochemistry, Biochemistry, Peptide, Biophysics and Combinatorial chemistry.
His research in Stereochemistry intersects with topics in Protein structure, Amino acid and Cystine, Cysteine.
Luis Moroder combines subjects such as Peptide sequence and Protein folding with his study of Protein structure.
His work on Biochemistry deals in particular with Receptor, Gastrin, Cholecystokinin, Binding site and Biological activity.
His Peptide research incorporates themes from Crystallography, Moiety, Azobenzene and Isomerization.
His work carried out in the field of Azobenzene brings together such families of science as Cyclic peptide, Photochemistry, Chromophore and Photoisomerization.
He most often published in these fields:
- Stereochemistry (36.42%)
- Biochemistry (25.20%)
- Peptide (20.81%)
What were the highlights of his more recent work (between 2004-2020)?
- Stereochemistry (36.42%)
- Biochemistry (25.20%)
- Peptide (20.81%)
In recent papers he was focusing on the following fields of study:
His scientific interests lie mostly in Stereochemistry, Biochemistry, Peptide, Azobenzene and Biophysics.
His study of Nuclear magnetic resonance spectroscopy is a part of Stereochemistry.
His study ties his expertise on Insulin together with the subject of Biochemistry.
Peptide is often connected to Tryptophan in his work.
His research integrates issues of Cyclic peptide, Crystallography, Collagen helix, Chromophore and Isomerization in his study of Azobenzene.
His research in Biophysics intersects with topics in Folding and Cell adhesion.
Between 2004 and 2020, his most popular works were:
- Iodoacetamide-induced artifact mimics ubiquitination in mass spectrometry. (219 citations)
- Azobenzene as conformational switch in model peptides. (200 citations)
- Isosteric replacement of sulfur with other chalcogens in peptides and proteins. (127 citations)
In his most recent research, the most cited papers focused on:
His primary scientific interests are in Stereochemistry, Biochemistry, Protein structure, Peptide and Azobenzene.
His Stereochemistry study combines topics from a wide range of disciplines, such as Proline, Cyclic peptide, Cysteine, Selenocysteine and Peptide sequence.
In his study, which falls under the umbrella issue of Biochemistry, Drug, Chemical synthesis, Diabetes mellitus and Semisynthesis is strongly linked to Insulin.
His Protein structure research is multidisciplinary, incorporating elements of Protein secondary structure, Crystallography, Protein folding, Peptide bond and Protein engineering.
In his research on the topic of Peptide, Stereoisomerism, Integrin binding and Thioredoxin is strongly related with Cis–trans isomerism.
His Azobenzene study incorporates themes from Nuclear magnetic resonance spectroscopy and Isomerization, Photoisomerization.
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