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Differences in Structure and Stability Between Normal and Deuterated Proteins (Phycocyanin) by Chang-Hwei Chen; I-Wen Liu; Robert MacColl; Donald S. Berns is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Differences in Structure and Stability Between Normal and Deuterated Proteins (Phycocyanin) about?

Differential scanning microcalorimetry was used to investigate the enthalpy ( A H d ) and the temperature (td) of thermal denaturation of normal and deuterated phycocyanins isolated from two blue-green algae, Plectonerna calothrieoides and Phwmidium luridurn. Values of td in deuterated proteins are about 5°C lower than those in normat proteins. The magnitudes of A H d in deuterated proteins are 1%36% lower than in normal proteins. The heatcapacity change (AC,) in protein unfolding is essentially the same (2 kcal/mol/K) for deuterated and normal proteins within the experimental error. A t close to physiological temperature (27"C), the differences in thermodynamic functions in the native and denatured states are much higher in normal proteins than in deuterated proteins. CD was employed to evaluate both the secondary structures and urea denaturation of these two types of proteins. In P. luridurn, deuterated protein is about 8% higher in a-helix content; in P. calothricoides it is not significantly higher. Deuterated proteins are less resistant to the denaturant urea than are normal proteins: the denaturant concentration at the midpoint of the denaturation curve is 0.6-1.2 mol/L lower

Who reads Differences in Structure and Stability Between Normal and Deuterated Proteins (Phycocyanin)?

Author

Chang-Hwei Chen; I-Wen Liu; Robert MacColl; Donald S. Berns

Publisher

Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0006-3525)

Published

1983

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)