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While it is critical for a protein's structure to be unique and stable, changes in this structure are imperative for binding and catalysis. It is now evident that many protein recognition processes incorporate conformational changes as a requisite event for function. In this manner, protein structure and dynamics are intimately linked with biological activity. We utilize a combination of methods including high resolution multinuclear NMR for solution structure determination, and stopped flow optical, hydrogen/deuterium exchange and mass spectrometric techniques to investigate how protein structure and dynamics are linked with biological activity in solution. Specifically, we are asking: (1) The fundamental question of how amino acid sequence directs protein folding and assembly and (2) What protein/protein interactions are responsible for localization and modulation of signal transduction events?
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Mindfulnessno. 2 (2024): 327-344
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APPLIED DEVELOPMENTAL SCIENCE (2023)
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#Papers: 346
#Citation: 17217
H-Index: 65
G-Index: 123
Sociability: 7
Diversity: 3
Activity: 19
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