Higher Mortality Is Not a Universal Cost of Dispersal: A Case Study in African Wild Dogs.

AbstractMortality is considered one of the main costs of dispersal. A reliable evaluation of mortality, however, is often hindered by a lack of information about the fate of individuals that disappear under unexplained circumstances (i.e.

Circular-linear copulae for animal movement data.

Animal movement is often modelled in discrete time, formulated in terms of taken between successive locations at regular time intervals. Steps are characterized by the distance between successive locations () and changes in direction (). Animals commonly exhibit a mix of directed movements with large step lengths and turn angles near 0 when travelling between habitat patches and more wandering movements with small step lengths and uniform turn angles when foraging.

Discovery of Open Cubane Core Structures for Biomimetic LnCo (OR) Water Oxidation Catalysts.

Bio-mimetic catalysts such as LnCo (OR) (Ln=Er, Tm; OR=alkoxide) cubanes have recently been in the focus of research for artificial water oxidation processes. Previously, the remarkable adaptability with respect to ligand shell, nuclear structure as well as protonation and oxidation states of those catalysts has been shown to be beneficial for the water oxidation process. We further explored the structural flexibility of those catalysts and present here a series of novel structures in which one metal center is pulled out of the cubane cage.

Exploring Solvation Effects in Ligand-Exchange Reactions via Static and Dynamic Methods.

We investigate ligand-exchange reactions of a biomimetic Co(II)-based heterocubane complex in aqueous solution by means of various approaches for consideration of solvent effects. Static calculations based on geometry optimizations carried out in vacuum, with solvent continuum models, or with several explicit solvent molecules have been carried out as well as density functional theory (DFT)-based molecular dynamics simulations. In addition, reaction pathways and barriers have been elucidated via nudged elastic band calculations and metadynamics.

Dehydrogenation Free Energy of Co(aq) from Density Functional Theory-Based Molecular Dynamics.

Electron and proton transfers are important steps occurring in chemical reactions. The often used approach of calculating the energy differences of those steps using methods based on geometry optimizations neglects the influence of dynamic effects. To further investigate this issue and inspired by research in water oxidation, we calculate in the present study the dehydrogenation free energy of aqueous Co, which is the free energy change associated with the first step of the water oxidation reaction mechanism of recently investigated model Co(II)-aqua catalysts.

3d-4f {Co(II)3Ln(OR)4} Cubanes as Bio-Inspired Water Oxidation Catalysts.

Although the {CaMn4O5} oxygen evolving complex (OEC) of photosystem II is a major paradigm for water oxidation catalyst (WOC) development, the comprehensive translation of its key features into active molecular WOCs remains challenging. The [Co(II)3Ln(hmp)4(OAc)5H2O] ({Co(II)3Ln(OR)4}; Ln = Ho-Yb, hmp = 2-(hydroxymethyl)pyridine) cubane WOC series is introduced as a new springboard to address crucial design parameters, ranging from nuclearity and redox-inactive promoters to operational stability and ligand exchange properties. The {Co(II)3Ln(OR)4} cubanes promote bioinspired WOC design by newly combining Ln(3+) centers as redox-inactive Ca(2+) analogues with flexible aqua-/acetate ligands into active and stable WOCs (max.

Relative free enthalpies for point mutations in two proteins with highly similar sequences but different folds.

Enveloping distribution sampling was used to calculate free-enthalpy changes associated with single amino acid mutations for a pair of proteins, GA95 and GB95, that show 95% sequence identity yet fold into topologically different structures. Of the L → A, I → F, and L → Y mutations at positions 20, 30, and 45, respectively, of the 56-residue sequence, the first and the last contribute the most to the free-enthalpy difference between the native and non-native sequence-structure combinations, in agreement with the experimental findings for this protein pair. The individual free-enthalpy changes are almost sequence-independent in the four-strand/one-helix structure, the stable form of GB95, while in the three-helix bundle structure, the stable form of GA95, an interplay between residues 20 and 45 is observed.