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oai:figshare.com:article/32995298 2026-05-01T00:00:00Z portal_693 item_type_8 month_year_05_2026

NMR-Based Characterization of Proteins: Structure, Dynamics and Binding Interfaces of Influenza A's M1 Leonel Bustamante Carballo (24400253) Chemistry, Physical Chemistry, Biochemistry Biophysics, General Biomolecular structure, dynamics and interactions are fundamental for understanding how living systems operate at atomic scale. Proteins and nucleic acids carry out most processes essential to life, and they are equally central to the molecular mechanisms underlying disease. Addressing major contemporary health challenges, such as cancer, viral infections, neurodegeneration, and congenital disorders, requires scientific advances that provide a strong basis for developing therapeutic strategies. In this context, solution-state Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful analytical tool: it can be used to characterize molecular structure under conditions that resemble physiological environments, it allows the observation of dynamic processes across a wide range of NMR-accessible timescales and facilitates residue-level mapping of molecular surfaces involved in intermolecular recognition. The first two chapters of this dissertation focus on the theoretical background required for interpreting NMR experiments. Chapter 1 introduces the fundamentals of nuclear magnetism and describes how NMR exploits the quantum-mechanical properties of nuclear spin to extract biophysical information. Chapter 2 describes multidimensional NMR techniques used to probe biomolecular structure and dynamics, alongside the biochemical and experimental workflow necessary for their application. Chapter 3 applies these methods to the semi-large N-terminal domain of Influenza A Matrix Protein 1 (M1), detailing its structure, dynamic behavior, and potential interfaces involved in molecular recognition and binding. Chapter 4 investigates these interfaces further, in the context of mechanistic self-assembly, nucleic acid association, and membrane interaction. The goal of this work is to demonstrate how solution-state NMR is a versatile tool for elucidating molecular structure, dynamics, and residue-specific interactions. By examining M1’s sensitivity to environmental changes, characterizing its mechanisms of self-assembly and nucleic-acid and membrane association, and integrating these findings into a hypothesis-based model of intermolecular interactions, this dissertation provides new insight into the molecular behavior of a key influenza protein. 2026-05-01T00:00:00Z Text Thesis 10.25417/uic.32995298.v1 https://figshare.com/articles/thesis/NMR-Based_Characterization_of_Proteins_Structure_Dynamics_and_Binding_Interfaces_of_Influenza_A_s_M1/32995298 In Copyright Open Access after 2028-05-01