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 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.
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.
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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Stability of Protein Pharmaceuticals
Mark C. Manning;Kamlesh Patel;Ronald T. Borchardt.
Pharmaceutical Research (1989)
Stability of Protein Pharmaceuticals: An Update
Mark Cornell Manning;Danny K. Chou;Brian M. Murphy;Robert W. Payne.
Pharmaceutical Research (2010)
Theoretical CD studies of polypeptide helices: examination of important electronic and geometric factors.
Mark C. Manning;Robert W. Woody.
Sustained-release composition including amorphous polymer
Theodore W. Randolph;Mark C. Manning;Richard F. Falk.
Tween protects recombinant human growth hormone against agitation-induced damage via hydrophobic interactions
Narendra B. Bam;Jeffrey L. Cleland;Janet Yang;Mark C. Manning.
Journal of Pharmaceutical Sciences (1998)
Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns.
Mark C. Manning;Mali Illangasekare;Robert W. Woody.
Biophysical Chemistry (1988)
Effects of Tween 20® and Tween 80® on the Stability of Albutropin During Agitation
Danny K. Chou;Rajesh Krishnamurthy;Theodore W. Randolph;John F. Carpenter.
Journal of Pharmaceutical Sciences (2005)
Effect of Tween 20 on freeze-thawing- and agitation-induced aggregation of recombinant human factor XIII.
Lotte Krielgaard;Latoya S. Jones;Latoya S. Jones;Theodore W. Randolph;Sven Frokjaer.
Journal of Pharmaceutical Sciences (1998)
The helix-coil transition in heterogeneous peptides with specific side-chain interactions: theory and comparison with CD spectral data.
Paul J. Gans;Pingchiang C. Lyu;Mark C. Manning;Robert W. Woody.
Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state
Brent S. Kendrick;Byeong S. Chang;Tsutomu Arakawa;Brian Peterson.
Proceedings of the National Academy of Sciences of the United States of America (1997)
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