Proton momentum distribution in a protein hydration shell

The momentum distribution of protons in the hydration shell of a globular protein has been measured through deep inelastic neutron scattering at 180 and 290 K, below and above the crossover temperature T-c=1.23T(g), where T-g=219 K is the glass transition temperature. It is found that the mean kinetic energy of the water hydrogens shows no temperature dependence, but the measurements are accurate enough to indicate a sensible change of momentum distribution and effective potential felt by protons, compatible with the transition from a single to a double potential well. This could support the presence of tunneling effects even at room temperature, playing an important role in biological function

LCA to Estimate the Environmental Impact of Dairy Farms: A Case Study

Intensive farming is responsible for extreme environmental impacts under different aspects, among which global warming represents a major reason of concern. This is a quantitative problem linked to the farm size and a qualitative one, depending on farming methods and land management. The dairy sector is particularly relevant in terms of environmental impact, and new approaches to meeting sustainability goals at a global scale while meeting society's needs are necessary. The present study was carried out to assess the environmental impact of dairy cattle farms based on a life cycle assessment (LCA) model applied to a case study. These preliminary results show the possibility of identifying the most relevant impacts in terms of supplied products, such as animal feed and plastic packaging, accounting for 19% and 15% of impacts, respectively, and processes, in terms of energy and fuel consumption, accounting for 53% of impacts overall. In particular, the local consumption of fossil fuels for operations within the farm represents the most relevant item of impact, with a small margin for improvement. On the other hand, remarkable opportunities to reduce the impact can be outlined from the perspective of stronger partnerships with suppliers to promote the circularity of packaging and the sourcing of animal feed. Future studies may include the impact of drug administration and the analysis of social aspects of LCA

Spread rates on fragmented landscapes: the interacting roles of demography, dispersal and habitat availability

This work was supported by the award of the Natural Environment Research Council grant NE/J008001/1 to JMJT.Peer reviewedPublisher PD

A trait-based approach for predicting species responses to environmental change from sparse data : how well might terrestrial mammals track climate change?

Acknowledgements LS was supported by two STSMs by the COST Action ES1101 ”Harmonising Global Biodiversity Modelling“ (Harmbio), supported by COST (European Cooperation in Science and Technology). JMB and SMW were funded by CEH projects NEC05264 and NEC05100. JMJT and SCFP are grateful for the support of the Natural Environment Research Council UK (NE/J008001/1). LS, JAH and JMJT conceived the original idea. LS, JAH, JMB, TC & JMJT designed the study; LS collected the data; LS and TC performed the statistical analyses; LS conducted the integrodifference modelling assisted by JMB and SMW. LS conducted the individual-based modelling assisted by SCFP. LS led the writing supported by JMJT, JMB, SCFP, SMW, TC, JAH and GB.Peer reviewedPublisher PD

Prospecting and informed dispersal : Understanding and predicting their joint eco-evolutionary dynamics

ACKNOWLEDGMENTS AP was funded by a European Union's Horizon 2020 research and innovation program under the Marie Sklodowska-Curie grant agreement no. 753420 (EcoEvoProspectS project). JMJT and AS were funded by the Biotechnology and Biological Sciences Research Council, project grant BB/S507349/1.Peer reviewedPublisher PD

RangeShiftR : an R package for individual-based simulation of spatial eco-evolutionary dynamics and species' responses to environmental changes

Acknowledgements – We are grateful for valuable feedback from many users who tested previous versions of the package. The Figures 1 and 2 were created using the draw.io app. We acknowledge the support of the Open Access Publishing Fund of the Univ. of Potsdam. Funding – AM and DZ were supported by Deutsche Forschungsgemeinschaft (DFG) under grant agreement No. ZU 361/1-1. GB was supported by a Royal Society University Research Fellowship (UF160614).Peer reviewedPublisher PD

Ultra-rapid glutathionylation of chymotrypsinogen in its molten globule-like conformation: a comparison to archaeal proteins

Chymotrypsinogen, when reduced and taken to its molten globule-like conformation, displays a single cysteine with an unusual kinetic propensity toward oxidized glutathione (GSSG) and other organic thiol reagents. A single residue, identified by mass spectrometry like Cys1, reacts with GSSG about 1400 times faster than an unperturbed protein cysteine. A reversible protein-GSSG complex and a low pK(a) (8.1 +/- 0.1) make possible such astonishing kinetic property which is absent toward other natural disulfides like cystine, homocystine and cystamine. An evident hyper-reactivity toward 5,5 ' -dithiobis-(2-nitrobenzoic acid) (DTNB) and 1-chloro-2,4-dinitrobenzene (CDNB) was also found for this specific residue. The extraordinary reactivity toward GSSG is absent in two proteins of the thermophilic archaeon Sulfolobus solfataricus, an organism lacking glutathione: the Protein Disulphide Oxidoreductase (SsPDO) and the Bacterioferritin Comigratory Protein 1 (Bcp1) that displays Cys residues with an even lower pK(a) value (7.5 +/- 0.1) compared to chymotrypsinogen. This study, which also uses single mutants in Cys residues for Bcp1, proposes that this hyper-reactivity of a single cysteine, similar to that found in serum albumin, lysozyme, ribonuclease, may have relevance to drive the "incipit" of the oxidative folding of proteins from organisms where the glutathione/oxidized glutathione (GSH/GSSG) system is present

Coupled land use and ecological models reveal emergence and feedbacks in socio-ecological systems

Acknowledgements: This work was supported by an EPSRC Doctoral Training Centre grant (EP/G03690X/1). Supplementary material (Appendix ECOG‐04039 at ). Appendix 1.Peer reviewedPublisher PD

The Insulin-Degrading Enzyme from Structure to Allosteric Modulation: New Perspectives for Drug Design

The insulin-degrading enzyme (IDE) is a Zn2+ peptidase originally discovered as the main enzyme involved in the degradation of insulin and other amyloidogenic peptides, such as the β-amyloid (Aβ) peptide. Therefore, a role for the IDE in the cure of diabetes and Alzheimer’s disease (AD) has been long envisaged. Anyway, its role in degrading amyloidogenic proteins remains not clearly defined and, more recently, novel non-proteolytic functions of the IDE have been proposed. From a structural point of view, the IDE presents an atypical clamshell structure, underscoring unique enigmatic enzymological properties. A better understanding of the structure–function relationship may contribute to solving some existing paradoxes of IDE biology and, in light of its multifunctional activity, might lead to novel therapeutic approaches

Reducing persecution is more effective for restoring large carnivores than restoring their prey

We gratefully acknowledge funding by the Federal State of Berlin, Germany (Elsa Neumann Scholarship to BB), and the German Research Foundation (GH 149/1-1 and ZU 361/1-1). We further thank all participants of the workshop on the revi- sion of the Strategy for Leopard Conservation in the Caucasus in Tbilisi, Georgia in 2017. We are grateful to J. Buchner, A. Heidelberg, V.C. Radeloff, and H. Yin for fruitful discussions, and F. Poetzschner for help with preparing data. Additionally, we thank two anonymous reviewers for their constructive comments.Peer reviewedPublisher PD