D. J. Nicholls

Publication List Details

Period

1994 - 1998

Number

14

Co-Authors

An Examination of the Reasons for the Discrepancy Between Long and Small Fatigue Cracks in Al-Li Alloys. (1998)

Nicholls, D. J., Martin, J. W.

Small-fatigue-crack growth data have been compared with long-fatigue- crack data generated in the Al-Li-Cu-Mg-Zr alloy 8090; not unexpectedly, small fatigue cracks were observed to grow significantly...

A Comparison of Small Fatigue Crack Growth, Low Cycle Fatigue and Long Fatigue Crack Growth in Al-Li Alloys. (1998)

Nicholls, D. J., Martin, J. W.

A study of small fatigue crack properties in aluminum alloy 8090 was conducted. It was found that the growth rate of small fatigue cracks was proportional to delta K squared. This equation has been...

Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.

Alldread, R M, Halsall, D M, Clarke, A R, Sundaram, T K, Atkinson, T, Scawen, M D, ...

The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the...

Erwinia chrysanthemi L-asparaginase: epitope mapping and production of antigenically modified enzymes.

Moola, Z B, Scawen, M D, Atkinson, T, Nicholls, D J

This study shows that the antigenicity of Erwinia chrysanthemi L-asparaginase can be reduced by site-directed mutagenesis. Ten B-cell epitopes of the enzyme were identified using synthetic...

Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase.

Nobbs, T J, Cortés, A, Gelpi, J L, Holbrook, J J, Atkinson, T, Scawen, M D, ...

The X-ray structure of lactate dehydrogenase (LDH) shows the side-chain carboxylate group of Asp-143 to be buried in the hydrophobic interior of the enzyme, where it makes hydrogen-bonding...

Tetrameric malate dehydrogenase from a thermophilic Bacillus: cloning, sequence and overexpression of the gene encoding the enzyme and isolation and characterization of the recombinant enzyme.

Wynne, S A, Nicholls, D J, Scawen, M D, Sundaram, T K

The gene encoding the tetrameric malate dehydrogenase (MDH) in a thermophilic Bacillus species (BI) has been cloned in an Escherichia coli plasmid. The nucleotide sequence of the gene, the first to...

Catalytic-rate improvement of a thermostable malate dehydrogenase by a subtle alteration in cofactor binding.

Alldread, R M, Halsall, D M, Clarke, A R, Sundaram, T K, Atkinson, T, Scawen, M D, ...

The nucleotide-binding fold of many NAD(+)-dependent dehydrogenases contains a conserved acidic amino acid residue which hydrogen-bonds with the 2'- and 3'-hydroxy groups of the adenine-ribose of the...

Erwinia chrysanthemi L-asparaginase: epitope mapping and production of antigenically modified enzymes.

Moola, Z B, Scawen, M D, Atkinson, T, Nicholls, D J

This study shows that the antigenicity of Erwinia chrysanthemi L-asparaginase can be reduced by site-directed mutagenesis. Ten B-cell epitopes of the enzyme were identified using synthetic...

Contribution of a buried aspartate residue towards the catalytic efficiency and structural stability of Bacillus stearothermophilus lactate dehydrogenase.

Nobbs, T J, Cortés, A, Gelpi, J L, Holbrook, J J, Atkinson, T, Scawen, M D, ...

The X-ray structure of lactate dehydrogenase (LDH) shows the side-chain carboxylate group of Asp-143 to be buried in the hydrophobic interior of the enzyme, where it makes hydrogen-bonding...

Tetrameric malate dehydrogenase from a thermophilic Bacillus: cloning, sequence and overexpression of the gene encoding the enzyme and isolation and characterization of the recombinant enzyme.

Wynne, S A, Nicholls, D J, Scawen, M D, Sundaram, T K

The gene encoding the tetrameric malate dehydrogenase (MDH) in a thermophilic Bacillus species (BI) has been cloned in an Escherichia coli plasmid. The nucleotide sequence of the gene, the first to...

Malate dehydrogenase: a model for structure, evolution, and catalysis.

Goward, C. R., Nicholls, D. J.

Malate dehydrogenases are widely distributed and alignment of the amino acid sequences show that the enzyme has diverged into 2 main phylogenetic groups. Multiple amino acid sequence alignments of...