What is he best known for?
The fields of study he is best known for:
- Enzyme
- Biochemistry
- Amino acid
Mark C. Manning focuses on Circular dichroism, Crystallography, Protein structure, Chromatography and Protein secondary structure.
His Circular dichroism research is multidisciplinary, incorporating elements of Sucrose, Biophysics, Denaturation, Protein folding and Native state.
His Crystallography research includes themes of Side chain and Stereochemistry.
The Protein structure study combines topics in areas such as Protein tertiary structure and Rational design.
His studies deal with areas such as Solubility, Pulmonary surfactant, Hydrophobic effect, Drug carrier and Chloride as well as Chromatography.
His biological study spans a wide range of topics, including Differential scanning calorimetry, Turn and Infrared spectroscopy, Analytical chemistry.
His most cited work include:
- Stability of Protein Pharmaceuticals (1149 citations)
- Stability of Protein Pharmaceuticals: An Update (754 citations)
- Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions (255 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of study are Circular dichroism, Chromatography, Protein structure, Protein secondary structure and Biochemistry.
His research in Circular dichroism tackles topics such as Native state which are related to areas like Sucrose.
The study incorporates disciplines such as Deamidation, Biophysics and Aqueous solution in addition to Chromatography.
Mark C. Manning combines subjects such as Protein aggregation and Infrared spectroscopy, Analytical chemistry with his study of Protein structure.
His Protein secondary structure research integrates issues from Enzyme and Protein folding.
His research on Biochemistry frequently connects to adjacent areas such as Chemical stability.
He most often published in these fields:
- Circular dichroism (30.00%)
- Chromatography (23.57%)
- Protein structure (22.86%)
What were the highlights of his more recent work (between 2008-2020)?
- Biophysics (13.57%)
- Chromatography (23.57%)
- Protein structure (22.86%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Biophysics, Chromatography, Protein structure, Analytical chemistry and Second derivative.
His work deals with themes such as Ionic strength, Aqueous solution, Protein aggregation and Chemical stability, which intersect with Biophysics.
Mark C. Manning has researched Protein aggregation in several fields, including Solubility, Human serum albumin, Virial coefficient and Circular dichroism.
Biochemistry is closely connected to Dry ice in his research, which is encompassed under the umbrella topic of Solubility.
He interconnects Trehalose, Deamidation, Glass transition and Peptide in the investigation of issues within Chromatography.
His Protein structure study combines topics in areas such as Plasticizer and Protein secondary structure.
Between 2008 and 2020, his most popular works were:
- Stability of Protein Pharmaceuticals: An Update (754 citations)
- Role of Buffers in Protein Formulations (69 citations)
- Product development issues for PEGylated proteins (48 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Biochemistry
- Amino acid
Mark C. Manning mainly focuses on Protein stability, Biochemistry, Chromatography, Pharmaceutical technology and Biophysics.
His studies in Protein stability integrate themes in fields like Dry ice, Drug and Solubility.
Mark C. Manning combines subjects such as Protein structure, Deamidation and Mannitol with his study of Chromatography.
His Deamidation study integrates concerns from other disciplines, such as Sequence dependence, Asparagine, Peptide and Chemometrics.
His Pharmaceutical technology research includes themes of Amino acid, Polymer science, Protein stabilization, Proteins metabolism and Pharmacology toxicology.
The concepts of his Biophysics study are interwoven with issues in Conformational stability, Chemical stability and Physical stability.
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