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Your search keyword '"John A.M. Ramshaw"' showing total 7 results
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7 results on '"John A.M. Ramshaw"'

1. High resolution proton magnetic resonance studies of plastocyanin

Author

V. A. Norris, Hans C. Freeman, John A.M. Ramshaw, and Peter E. Wright

Subjects
Magnetic Resonance Spectroscopy, Chemistry, Protein Conformation, Biophysics, Magnetic resonance force microscopy, High resolution, Oxidation reduction, Cell Biology, Nuclear magnetic resonance spectroscopy, Biochemistry, Proton magnetic resonance, Nuclear magnetic resonance, Protein structure, Species Specificity, Structural Biology, Genetics, Spin echo, Plastocyanin, Molecular Biology, Oxidation-Reduction, Plant Proteins
Published
1978

2. Preliminary crystallographic data for a copper-containing protein, plastocyanin

Author

M. P. Venkatappa, Graeme V. Chapman, J. Michell Guss, Peter M. Colman, V. A. Norris, Hans C. Freeman, Murata Mitsuo, and John A.M. Ramshaw

Subjects
Chemistry, Protein Conformation, chemistry.chemical_element, Crystallographic data, Copper, Crystallography, X-Ray Diffraction, Structural Biology, Molecule, Deep blue, Plastocyanin, Molecular Biology, Plant Proteins
Abstract

A copper-containing protein, plastocyanin from poplar leaves, has been crystallized in the oxidized (i.e Cu(II)) state. The deep blue crystals are rhombic prisms with space group P212121 and cell dimensions a=29·6A, b=46·9A, c=57·6 A. The molecular weight is 10,500. There are four molecules of protein in the unit cell, and hence there is one molecule in the asymmetric unit.

Published
1977

6. Preliminary crystallographic data for a basic copper-containing protein from cucumber seedlings

Author

Peter M. Colman, M. P. Venkatappa, Hans C. Freeman, John A.M. Ramshaw, Mitsuo Murata, J. Mitchell Guss, V. A. Norris, and Larry E. Vickery

Subjects
Molecular Weight, Crystallography, X-Ray Diffraction, Structural Biology, Chemistry, X-ray crystallography, Molecule, chemistry.chemical_element, Crystallographic data, Molecular Biology, Copper, Plant Proteins
Abstract

A basic protein with a molecular weight of approximately 10,100 and having a single atom of Type I copper has been isolated from cucumber seedlings. The oxidized, cupric, form of the protein has been crystallized as thin olive-green plates with space group P 2 1 2 1 2 1 and cell dimensions a = 30.8 A, b = 45.6 A and c = 66.6 A. There is one protein molecule per asymmetric unit.

Published
1977
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7. Purification and properties of an acid protease from Phaseolus aureus

Author

John A.M. Ramshaw and John R. Viney

Subjects
chemistry.chemical_classification, Protease, biology, Mung bean, medicine.medical_treatment, Substrate (chemistry), Plant Science, General Medicine, Horticulture, biology.organism_classification, Biochemistry, Enzyme, chemistry, biology.protein, medicine, Phaseolus, Bovine serum albumin, Molecular Biology, Incubation
Abstract

An acid protease has been purified 470-fold from mung bean seedlings. With bovine serum albumin as substrate, the enzyme showed an optimum at pH 3·6 and at 45° or incubation for 1 hr. The enzyme was relatively stable after incubation for 20 hr between pH 3.·0 and pH 6·0 but lost activity on incubation at 15° for 15 min at pH 6°8.

Published
1975
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