Author: "Beamer, Lesa J." / Database: Gale General OneFile - Searchworks@Jio Institute Digital Library Search Results

Author: Goldraij, Ariel, Beamer, Lesa J., and Polacco, Joe C.
Subjects: Soybean -- Physiological aspects, Hydrolases -- Research, Enzymes -- Research, Foliar diagnosis, Biological sciences, Science and technology
Published: 2003

Author: Beamer, Lesa J., Carroll, Stephen F., and Eisenberg, David
Subjects: Proteins -- Structure, Antibacterial agents -- Physiological aspects, Endotoxins -- Physiological aspects, Science and technology, Physiological aspects
Abstract: Bactericidal/permeability-increasing protein (BPI), a potent antimicrobial protein of 456 residues, binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria. At a resolution of 2.4 angstroms, the crystal [...]
Published: 1997

Author: Clarke, Neil D., Beamer, Lesa J., Goldberg, Harry R., Berkower, Carol, and Pabo, Carl O.
Subjects: DNA-ligand interactions -- Research, Bacteriophage lambda -- Research, X-ray crystallography -- Research, DNA binding proteins -- Research, Science and technology, Research
Abstract: ALTHOUGH THE WELL-CHARACTERized DNA binding motifs (helix-turn-helix, zinc finger, and so forth) use stably folded units of secondary structure for recognition, flexible regions can also contribute to site-specific recognition. Unfortunately, [...]
Published: 1991

Author: Pabo, Carl O., Aggarwal, Aneel K., Jordan, Steven R., Beamer, Lesa J., Obeysekare, Upul R., and Harrison, Stephen C.
Subjects: Crystallography -- Research, DNA -- Research -- Genetic aspects, Bacteria -- Genetic aspects -- Research, Amino acid sequence -- Research -- Genetic aspects, Escherichia coli -- Genetic aspects -- Research, Science and technology, Genetic aspects, Research
Abstract: Conserved Residues Make Similar Contacts in Two Repressor-Operator Complexes THE λ AND 434 REPRESSORS, WHICH are produced by related Escherichia coli phages [1], recognize very distinct operator sites, but both [...]
Published: 1990

Author: Schramm, Andrew M., Mehra-Chaudhary, Ritcha, Furdui, Cristina M., and Beamer, Lesa J.
Subjects: Mutagenesis -- Analysis, Protein folding -- Analysis, Pseudomonas aeruginosa -- Genetic aspects, Enzyme binding -- Analysis, Biological sciences, Chemistry
Abstract: The site-directed mutagenesis, structural, kinetic, and thermodynamic characterization of enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) from the bacterium Pseudomonas aeruginosa is reported. The results help to better understand the backbone flexibility and conformational changes in the PMM/PGM reaction and the role of hinges in enzyme catalysis.
Published: 2008

Author: Naught, Laura E., Regni, Catherine, Beamer, Lesa J., and Tipton, Peter A.
Subjects: Enzymes -- Physiological aspects, Phosphates -- Physiological aspects, Pseudomonas aeruginosa -- Physiological aspects, Biochemistry -- Research, Biological sciences, Chemistry
Abstract: Research has been conducted on Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase. Results demonstrate that phosphomannomutase/phosphoglucomutase is a very elastic and resilient enzyme.
Published: 2003

Author: Snook, Christopher F., Tipton, Peter A., and Beamer, Lesa J.
Subjects: Bacterial proteins, Binding sites (Biochemistry) -- Analysis, Pseudomonas aeruginosa -- Research, Oxidoreductases, Biological sciences, Chemistry
Abstract: The 1.55 angsrom crystal structure of GDP-mannose dehydrogenase complexed with its cofactor NAD)H) and GDP-mannuronic acid product shows that the enzyme exhibits a domain-swapped dimer consisting of two polypeptide chains that contribute to each active site. Data indicate that the dimer interface is extensive and facilitates intersubunit communication.
Published: 2003

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