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Titlebook: Biomolecules‘ Conformational Changes Studied by Simulations and Enhanced Sampling; Yui Tik (Andrew) Pang Book 2024 The Editor(s) (if appli

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發(fā)表于 2025-3-23 10:37:27 | 只看該作者
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發(fā)表于 2025-3-23 14:33:01 | 只看該作者
https://doi.org/10.1007/978-3-642-99340-4s vary widely, both in size and function. At the macro level, we have macromolecules: proteins that catalyze various biochemical reactions and provide structural integrity to tissues, carbohydrates that serve as primary energy sources and offer structural support, lipids that form cellular membranes
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發(fā)表于 2025-3-23 19:19:06 | 只看該作者
Die Unvermeidbarkeit der Metaphysikding” between the molecule and the binding site, which is a directional interaction between a halogen atom and a nucleophilic atom. Such an interaction is induced by an electron cloud shift of the halogen atom toward its covalently bonded neighbor to form the .-bond, leaving a small electrostatic po
14#
發(fā)表于 2025-3-24 01:10:17 | 只看該作者
https://doi.org/10.1007/978-3-658-31593-1r domain of autotransporters is almost always composed of a large β-helix, with only a small portion of it being relevant to its virulence function. This has led to the hypothesis that the folding of the β-helical structure aids the secretion of the passenger domain across the Gram-negative outer me
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發(fā)表于 2025-3-24 04:35:56 | 只看該作者
Metaphysik: Denken im Modus des Leidenseptor binding domain (RBD) switching from a “down” (closed) to an “up” (open) state. Here, we used large-scale molecular dynamics simulations and two-dimensional replica exchange umbrella sampling calculations with more than a thousand windows and an aggregate total of 160 μs of simulation to invest
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發(fā)表于 2025-3-24 10:19:14 | 只看該作者
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發(fā)表于 2025-3-24 16:47:33 | 只看該作者
Springer Theseshttp://image.papertrans.cn/b/image/192711.jpg
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發(fā)表于 2025-3-24 22:30:28 | 只看該作者
Biomolecules‘ Conformational Changes Studied by Simulations and Enhanced Sampling978-3-031-70602-8Series ISSN 2190-5053 Series E-ISSN 2190-5061
20#
發(fā)表于 2025-3-25 00:24:57 | 只看該作者
https://doi.org/10.1007/978-3-031-70602-8biomolecular dynamics; conformational flexibility; conformational dynamics of proteins; capsid assembly
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