Peptide, Stereochemistry, Protein structure, Circular dichroism and Peptide sequence are his primary areas of study. His Peptide research is multidisciplinary, incorporating perspectives in Amino acid, Chromatography and Antimicrobial. His Stereochemistry study integrates concerns from other disciplines, such as Side chain, Coiled coil, Gramicidin S and Beta sheet.
In his work, Protein engineering, Isoleucine, Folding and Antiparallel is strongly intertwined with Protein folding, which is a subfield of Protein structure. His Circular dichroism study combines topics from a wide range of disciplines, such as Guanidine, Alanine and Denaturation. His Peptide sequence study combines topics in areas such as Random coil, Lysine, Tropomyosin, Biological activity and Antibody.
His main research concerns Peptide, Stereochemistry, Biochemistry, Chromatography and Peptide sequence. His work deals with themes such as Amino acid, Crystallography, Protein structure and Pilin, which intersect with Peptide. His Crystallography research incorporates themes from Ionic bonding, Bilayer and Alanine.
His Stereochemistry research focuses on Circular dichroism in particular. His Circular dichroism research is multidisciplinary, relying on both Coiled coil, Heptad repeat, Guanidine, Denaturation and Hydrophobic effect. His Chromatography study incorporates themes from Phase and Analytical chemistry.
The scientist’s investigation covers issues in Peptide, Peptide sequence, Biochemistry, Microbiology and Antimicrobial peptides. The Peptide study combines topics in areas such as Amino acid, Crystallography, High-performance liquid chromatography, Chromatography and Stereochemistry. His research in Crystallography focuses on subjects like Protein structure, which are connected to Protein folding, Biophysics, Antiparallel and Plasma protein binding.
He studies Circular dichroism which is a part of Stereochemistry. His Circular dichroism research incorporates elements of Hydrophobic effect and Tropomyosin. The study incorporates disciplines such as Binding domain, Pilin, Molecular biology, Alanine and Biological activity in addition to Peptide sequence.
His primary areas of study are Peptide, Peptide sequence, Stereochemistry, Microbiology and Protein structure. His study in Peptide is interdisciplinary in nature, drawing from both Amino acid, Ion exchange, Crystallography and Antimicrobial. His work investigates the relationship between Peptide sequence and topics such as Biological activity that intersect with problems in Hemolysis, Structure–activity relationship, Cationic Antimicrobial Peptides and Alpha.
Circular dichroism is the focus of his Stereochemistry research. His research in Circular dichroism intersects with topics in Coiled coil and Guanidine. His Protein structure research includes themes of Biophysics and Protein folding.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects.
David S. Wishart;Colin G. Bigam;Arne Holm;Robert S. Hodges.
Journal of Biomolecular NMR (1995)
New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites.
J. M. R. Parker;D. Guo;R. S. Hodges.
Biochemistry (1986)
The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle
Elizabeth E. Zubrzycka-Gaarn;Dennis E. Bulman;George Karpati;Arthur H. M. Burghes.
Nature (1988)
Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide.
F. D. Sonnichsen;J. E. Van Eyk;R. S. Hodges;B. D. Sykes.
Biochemistry (1992)
Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils.
S Y Lau;A K Taneja;R S Hodges.
Journal of Biological Chemistry (1984)
Rational Design of α-Helical Antimicrobial Peptides with Enhanced Activities and Specificity/Therapeutic Index
Yuxin Chen;Colin T. Mant;Susan W. Farmer;Robert E. W. Hancock.
Journal of Biological Chemistry (2005)
Role of Peptide Hydrophobicity in the Mechanism of Action of α-Helical Antimicrobial Peptides
Yuxin Chen;Michael T. Guarnieri;Adriana I. Vasil;Michael L. Vasil.
Antimicrobial Agents and Chemotherapy (2007)
Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides
Ziqing Jiang;Adriana I. Vasil;John D. Hale;Robert E. W. Hancock.
Biopolymers (2008)
Synthetic model proteins. Positional effects of interchain hydrophobic interactions on stability of two-stranded alpha-helical coiled-coils.
N E Zhou;C M Kay;R S Hodges.
Journal of Biological Chemistry (1992)
Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
Oscar D. Monera;Cyril M. Kay;Robert S. Hodges.
Protein Science (1994)
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