Member of the European Molecular Biology Organization (EMBO)
Richard N. Perham mostly deals with Biochemistry, Pyruvate dehydrogenase complex, Stereochemistry, Protein structure and Peptide sequence. His study in Biochemistry focuses on Escherichia coli, Dehydrogenase, Enzyme, NAD+ kinase and Protein primary structure. The Dihydrolipoyl transacetylase research Richard N. Perham does as part of his general Pyruvate dehydrogenase complex study is frequently linked to other disciplines of science, such as Pyruvate decarboxylase, therefore creating a link between diverse domains of science.
The study incorporates disciplines such as Dihydrolipoamide dehydrogenase and Protein subunit, Protein quaternary structure in addition to Stereochemistry. His studies in Protein structure integrate themes in fields like Pyruvate Dehydrogenase, Crystallography, Lysine, Nuclear magnetic resonance spectroscopy and Multifunctional Enzymes. His Peptide sequence research includes themes of Orientation, Geometry and Energy landscape.
Biochemistry, Pyruvate dehydrogenase complex, Stereochemistry, Escherichia coli and Dihydrolipoyl transacetylase are his primary areas of study. His research in the fields of Enzyme, Peptide sequence, Dehydrogenase and Protein subunit overlaps with other disciplines such as Glutathione reductase. His Enzyme study which covers Amino acid that intersects with Cysteine.
His studies in Pyruvate dehydrogenase complex integrate themes in fields like Enzyme complex and Branched-chain alpha-keto acid dehydrogenase complex. His study in Stereochemistry is interdisciplinary in nature, drawing from both Residue, Active site, Dimer, Alanine and Protein structure. His research in Protein structure tackles topics such as Crystallography which are related to areas like Capsid.
His primary areas of study are Pyruvate dehydrogenase complex, Biochemistry, Stereochemistry, Dihydrolipoyl transacetylase and Pyruvate decarboxylase. The study incorporates disciplines such as Crystallography, Icosahedral symmetry, Cofactor and Protein–protein interaction in addition to Pyruvate dehydrogenase complex. His work on Biochemistry deals in particular with Dehydrogenase, Branched-chain alpha-keto acid dehydrogenase complex, DNA ligase, Peptide sequence and Protein structure.
The concepts of his Dehydrogenase study are interwoven with issues in Oxidoreductase and Multiprotein complex. His Stereochemistry research includes elements of Escherichia coli, Catalysis, Active site and Pseudomonas putida. His research in Dihydrolipoyl transacetylase intersects with topics in Dihydrolipoyllysine-Residue Acetyltransferase, Acetyltransferase, Reverse transcriptase and Substrate.
Richard N. Perham mainly focuses on Pyruvate dehydrogenase complex, Stereochemistry, Biochemistry, Active site and Dihydrolipoyl transacetylase. The Pyruvate Dehydrogenase research Richard N. Perham does as part of his general Pyruvate dehydrogenase complex study is frequently linked to other disciplines of science, such as Scaffold protein, therefore creating a link between diverse domains of science. His work on Nuclear magnetic resonance spectroscopy is typically connected to Linker as part of general Stereochemistry study, connecting several disciplines of science.
His Escherichia coli, Lysine and Peptide sequence study in the realm of Biochemistry connects with subjects such as Lipoylation. Richard N. Perham combines subjects such as Icosahedral symmetry, Dehydrogenase, Oxidative decarboxylation, Citric acid cycle and Histidine with his study of Active site. His Dihydrolipoyl transacetylase study integrates concerns from other disciplines, such as Crystallography and Euclidean geometry.
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Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
Nigel S. Scrutton;Alan Berry;Richard N. Perham.
Swinging Arms and Swinging Domains in Multifunctional Enzymes: Catalytic Machines for Multistep Reactions
Richard N. Perham.
Annual Review of Biochemistry (2000)
Glyceraldehyde 3-phosphate dehydrogenases
J. Ieuan Harris;R.N. Perham.
Journal of Molecular Biology (1965)
Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein.
Richard N. Perham.
Reversible blocking of amino groups with citraconic anhydride.
H B F Dixon;R N Perham.
Biochemical Journal (1968)
Multiple display of foreign peptides on a filamentous bacteriophage: Peptides from Plasmodium falciparum circumsporozoite protein as antigens
Judith Greenwood;Anne E. Willis;Richard N. Perham.
Journal of Molecular Biology (1991)
Pulling geometry defines the mechanical resistance of a β-sheet protein
David J Brockwell;Emanuele Paci;Rebecca C Zinober;Godfrey S Beddard.
Nature Structural & Molecular Biology (2003)
A common structural motif in thiamin pyrophosphate-binding enzymes.
Christopher F. Hawkins;Adolfo Borges;Richard N. Perham.
FEBS Letters (1989)
Glutathione reductase from Escherichia coli: cloning and sequence analysis of the gene and relationship to other flavoprotein disulfide oxidoreductases.
Shaun Greer;Richard N. Perham.
Immunological properties of foreign peptides in multiple display on a filamentous bacteriophage
Anne E. Willis;Richard N. Perham;David Wraith.
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