The introduction of eleven single-point stabilizing mutations based on force field calculations and evolutionary analysis yielded soluble domain-swapped intermediates trapped in local energy minima. Here, we reveal a unique example where the computational stabilization of a monomeric α/β-hydrolase enzyme ( T m = 73.5 ☌ Δ T m > 23 ☌) affected the protein folding energy landscape. Computer-encoded algorithms are increasingly employed to stabilize native proteins for use in research and biotechnology applications. This book addresses questions concerning mitigation measures in major sectors with original analyses of aspects including energy subsidies, sectoral energy efficiencies in manufacturing sectors, forest concessions, energy-saving labeling schemes, policy mixes for the urban transportation sector, and the introduction of waste-to-energy technologies.The functionality of an enzyme depends on its unique three-dimensional structure, which is a result of the folding process when the nascent polypeptide follows a funnel-like energy landscape to reach a global energy minimum. Another unique feature is that it was jointly written by Indonesian and international authors, as well as by academics and development practitioners. The most important feature of the book is its examination of multiple facets of climate change issues in Indonesia, which allows readers to understand the complexity of climate change in developing countries: the synergies and trade-offs between different climate change actions as well as between climate and development priorities.
This book demonstrates the challenges and opportunities of climate change actions in developing countries and primarily focuses on case studies in Indonesia, the world’s fourth most populous country.
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