title: The detective and the Sagas: Erlendur in the novels of Arnaldur Indriðason

authors: Bydder, Jillene

subjects: Arnaldur Indriðason, Icelandic crime fiction, Icelandic sagas, Detective Erlendur Sveinsson, fate in literature

abstract: Arnaldur Indriðason’s Erlendur novels are popular crime fiction stories set in Iceland. Detective Erlendur Sveinsson’s team deals with serious crimes, murders, and missing persons. Their cases are contemporary, but Indriðason has always said that he is influenced as a writer by the medieval Icelandic sagas. How is this illustrated by his crime fiction? The sagas, like crime fiction, contain stories of murder, revenge, love, loss and family conflicts. The paper uses examples from the novels and the sagas to examine the links between them. These links include the importance of traditional and local stories and the significance of fate. The paper also describes how Erlendur’s character develops over the series until he becomes an archetypical saga hero.

text: The detective and the Sagas: Erlendur in the novels of Arnaldur Indriðason Arnaldur Indriðason’s Erlendur novels are popular crime fiction stories set in Iceland. Detective Erlendur Sveinsson’s team deals with serious crimes, murders, and missing persons. Their cases are contemporary, but Indriðason has always said that he is influenced as a writer by the medieval Icelandic sagas. How is this illustrated by his crime fiction? The sagas, like crime fiction, contain stories of murder, revenge, love, loss and family conflicts. The paper uses examples from the novels and the sagas to examine the links between them. These links include the importance of traditional and local stories and the significance of fate. The paper also describes how Erlendur’s character develops over the series until he becomes an archetypical saga hero.

year: 2016-12

title: Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed ratesnzyme Catalyzed Rates

authors: Hobbs, Joanne K.

abstract: The increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This account persists despite many investigators noting that denaturation is insufficient to explain the decline in enzymatic rates above Topt. Here we show that it is the change in heat capacity associated with enzyme catalysis (ΔC‡p) and its effect on the temperature dependence of ΔG‡ that determines the temperature dependence of enzyme activity. Through mutagenesis, we demonstrate that the Topt of an enzyme is correlated with ΔC‡p and that changes to ΔC‡p are sufficient to change Topt without affecting the catalytic rate. Furthermore, using X-ray crystallography and molecular dynamics simulations we reveal the molecular details underpinning these changes in ΔC‡p. The influence of ΔC‡p on enzymatic rates has implications for the temperature dependence of biological rates from enzymes to ecosystems.

text: Change in heat capacity for enzyme catalysis determines temperature dependence of enzyme catalyzed ratesnzyme Catalyzed Rates The increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This account persists despite many investigators noting that denaturation is insufficient to explain the decline in enzymatic rates above Topt. Here we show that it is the change in heat capacity associated with enzyme catalysis (ΔC‡p) and its effect on the temperature dependence of ΔG‡ that determines the temperature dependence of enzyme activity. Through mutagenesis, we demonstrate that the Topt of an enzyme is correlated with ΔC‡p and that changes to ΔC‡p are sufficient to change Topt without affecting the catalytic rate. Furthermore, using X-ray crystallography and molecular dynamics simulations we reveal the molecular details underpinning these changes in ΔC‡p. The influence of ΔC‡p on enzymatic rates has implications for the temperature dependence of biological rates from enzymes to ecosystems.

year: 2013

title: He Maimai Aroha mō Nātana Waka Takurua

authors: Manuirirangi, Hōri

subjects: Poroporoaki

abstract: He kupu whakamānawa nā Hōri Manuirirangi ki a Nātana Waka Takurua i tana matenga.

text: He Maimai Aroha mō Nātana Waka Takurua He kupu whakamānawa nā Hōri Manuirirangi ki a Nātana Waka Takurua i tana matenga.

year: 2012-05