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| 2. |
- Aravind, P. V., et al.
(författare)
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Negative emissions at negative cost-an opportunity for a scalable niche
- 2022
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Ingår i: Frontiers in Energy Research. - : Frontiers Media SA. - 2296-598X. ; 10
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Tidskriftsartikel (refereegranskat)abstract
- In the face of the rapidly dwindling carbon budgets, negative emission technologies are widely suggested as required to stabilize the Earth's climate. However, finding cost-effective, socially acceptable, and politically achievable means to enable such technologies remains a challenge. We propose solutions based on negative emission technologies to facilitate wealth creation for the stakeholders while helping to mitigate climate change. This paper comes up with suggestions and guidelines on significantly increasing carbon sequestration in coffee farms. A coffee and jackfruit agroforestry-based case study is presented along with an array of technical interventions, having a special focus on bioenergy and biochar, potentially leading to "negative emissions at negative cost. " The strategies for integrating food production with soil and water management, fuel production, adoption of renewable energy systems and timber management are outlined. The emphasis is on combining biological and engineering sciences to devise a practically viable niche that is easy to adopt, adapt and scale up for the communities and regions to achieve net negative emissions. The concerns expressed in the recent literature on the implementation of emission reduction and negative emission technologies are briefly presented. The novel opportunities to alleviate these concerns arising from our proposed interventions are then pointed out. Our analysis indicates that 1 ha coffee jackfruit-based agroforestry can additionally sequester around 10 tonnes of CO2-eq and lead to an income enhancement of up to 3,000-4,000 Euros in comparison to unshaded coffee. Finally, the global outlook for an easily adoptable nature-based approach is presented, suggesting an opportunity to implement revenue-generating negative emission technologies on a gigatonne scale. We anticipate that our approach presented in the paper results in increased attention to the development of practically viable science and technology-based interventions in order to support the speeding up of climate change mitigation efforts.
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| 3. |
- Kasson, Peter M., et al.
(författare)
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Atomic-Resolution Simulations Predict a Transition State for Vesicle Fusion Defined by Contact of a Few Lipid Tails
- 2010
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Ingår i: PloS Computational Biology. - : Public Library of Science (PLoS). - 1553-734X .- 1553-7358. ; 6:6, s. e1000829-
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Tidskriftsartikel (refereegranskat)abstract
- Membrane fusion is essential to both cellular vesicle trafficking and infection by enveloped viruses. While the fusion protein assemblies that catalyze fusion are readily identifiable, the specific activities of the proteins involved and nature of the membrane changes they induce remain unknown. Here, we use many atomic-resolution simulations of vesicle fusion to examine the molecular mechanisms for fusion in detail. We employ committor analysis for these million-atom vesicle fusion simulations to identify a transition state for fusion stalk formation. In our simulations, this transition state occurs when the bulk properties of each lipid bilayer remain in a lamellar state but a few hydrophobic tails bulge into the hydrophilic interface layer and make contact to nucleate a stalk. Additional simulations of influenza fusion peptides in lipid bilayers show that the peptides promote similar local protrusion of lipid tails. Comparing these two sets of simulations, we obtain a common set of structural changes between the transition state for stalk formation and the local environment of peptides known to catalyze fusion. Our results thus suggest that the specific molecular properties of individual lipids are highly important to vesicle fusion and yield an explicit structural model that could help explain the mechanism of catalysis by fusion proteins.
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| 4. |
- Kasson, Peter M., et al.
(författare)
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Water Ordering at Membrane Interfaces Controls Fusion Dynamics
- 2011
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Ingår i: Journal of the American Chemical Society. - : American Chemical Society. - 0002-7863 .- 1520-5126. ; 133:11, s. 3812-3815
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Tidskriftsartikel (refereegranskat)abstract
- Membrane interfaces are critical to many cellular functions, yet the vast array of molecular components involved make the fundamental physics of interaction difficult to define. Water has been shown to play an important role in the dynamics of small biological systems, for example when trapped in hydrophobic regions, but the molecular details of water have generally been thought dispensable when considering large membrane interfaces. Nevertheless, spectroscopic data indicate that water has distinct, ordered behavior near membrane surfaces. While coarse-grained simulations have achieved success recently in aiding understanding the dynamics of membrane assemblies, it is natural to ask, does the missing chemical nature of water play an important role? We have therefore performed atomic-resolution simulations of vesicle fusion to understand the role of chemical detail, particularly the molecular structure of water, in membrane fusion and at membrane interfaces more generally. These membrane interfaces present a form of hydrophilic confinement, yielding surprising, non-bulk-like water behavior.
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| 5. |
- Rhee, Young Min, et al.
(författare)
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Simulations of the role of water in the protein-folding mechanism
- 2004
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 101:17, s. 6456-6461
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Tidskriftsartikel (refereegranskat)abstract
- There are many unresolved questions regarding the role of water in protein folding. Does water merely induce hydrophobic forces, or does the discrete nature of water play a structural role in folding? Are the nonadditive aspects of water important in determining the folding mechanism? To help to address these questions, we have performed simulations of the folding of a model protein (BBA5) in explicit solvent. Starting 10,000 independent trajectories from a fully unfolded conformation, we have observed numerous folding events, making this work a comprehensive study of the kinetics of protein folding starting from the unfolded state and reaching the folded state and with an explicit solvation model and experimentally validated rates. Indeed, both the raw TIP3P folding rate (4.5 +/- 2.5 micros) and the diffusion-constant corrected rate (7.5 +/- 4.2 micros) are in strong agreement with the experimentally observed rate of 7.5 +/- 3.5 micros. To address the role of water in folding, the mechanism is compared with that predicted from implicit solvation simulations. An examination of solvent density near hydrophobic groups during folding suggests that in the case of BBA5, there are water-induced effects not captured by implicit solvation models, including signs of a "concurrent mechanism" of core collapse and desolvation.
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