Dong Long

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Allosteric signaling in biomolecules is a key mechanism for a myriad of cellular processes. We present a general yet compact model for protein allostery at atomic detail to quantitatively explain and predict structural-dynamics properties of allosteric signal propagation. The master equation-based approach for allostery by population shift (MAPS) is(More)
Elucidation of the mechanism of biomacromolecular recognition events has been a topic of intense interest over the past century. The inherent dynamic nature of both protein and ligand molecules along with the continuous reshaping of the energy landscape during the binding process renders it difficult to characterize this process at atomic detail. Here, we(More)
The mechanisms of how ligands enter and leave the binding cavity of fatty acid binding proteins (FABPs) have been a puzzling question over decades. Liver fatty acid binding protein (LFABP) is a unique family member which accommodates two molecules of fatty acids in its cavity and exhibits the capability of interacting with a variety of ligands with(More)
A pair of triple resonance based CEST pulse schemes are presented for measuring ¹³C(α) and ¹³C(β) chemical shifts of sparsely populated and transiently formed conformers that are invisible to traditional NMR experiments. CEST profiles containing dips at resonance positions of ¹³C(α) or ¹³C(β) spins of major (ground) and minor (excited) conformers are(More)
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