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- W99120698 abstract "Temperature has a profound effect on the structure and function of proteins. Studies on enzymes suggest that over evolutionary time, adaptation to temperature occurs through modification of the molecular flexibility of the protein, especially in hinge regions around which catalytically important mobile structures rotate or slide. Changes in flexibility can arise through substitutions that alter the numbers and types of weak interactions among amino acids. Cold adaptation usually involves a localized decrease in the strength of these interactions, leading to greater molecular flexibility. Increased stability, induced by greater numbers of weak interactions, characterizes warm adaptation. Because more flexibility leads to increased catalytic rate but decreased substrate affinity, it is difficult for an enzyme to function optimally across a broad range of temperatures." @default.
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- W99120698 date "2011-01-01" @default.
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- W99120698 title "TEMPERATURE | Proteins and Temperature" @default.
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- W99120698 doi "https://doi.org/10.1016/b978-0-12-374553-8.00192-1" @default.
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