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Full-Text Articles in Molecular Biology
Supertertiary Structural Dynamics Modulate Function In Postsynaptic Density Protein 95, George L. Hamilton Iii
Supertertiary Structural Dynamics Modulate Function In Postsynaptic Density Protein 95, George L. Hamilton Iii
All Dissertations
Proteins, RNA, and DNA serve as the primary sub-cellular machinery that give rise to the necessary functions of life. The long-standing paradigm has been that the structures of biomolecules, or the arrangement of the subunits that make up a biomolecule, determine biological function. However, biomolecules are not static objects. Instead, they often undergo structural rearrangements that are crucial to enabling and regulating their functions. In my thesis I present several studies of the interplay between the structures, dynamics, and functions of biomolecules that combine experimental fluorescence spectroscopy and computational methods to probe these systems at the single-molecule level. In particular, …
Thermal Conductivity Of Bovine Serum Albumin: A Tool To Probe Denaturation Of Protein, Byoung Kyoo Park, Namwoo Yi, Jaesung Park, Tae Y. Choi, Jin Young Lee, Ahmed Busnaina, Dongsik Kim
Thermal Conductivity Of Bovine Serum Albumin: A Tool To Probe Denaturation Of Protein, Byoung Kyoo Park, Namwoo Yi, Jaesung Park, Tae Y. Choi, Jin Young Lee, Ahmed Busnaina, Dongsik Kim
Ahmed A. Busnaina
We demonstrate a strong correlation between denaturation of bovine serum albumin (BSA) and the thermal conductivity k of aqueous solutions of BSA. When denaturation of BSA began, k dropped significantly. These results suggest that k, i.e., the ability of a protein to transport passively applied thermal energy, can be exploited to probe the conformational dynamics of BSA and potentially of other proteins. The technique of protein analysis demonstrated in this work is expected to be useful in micro-total-analysis systems because it is easier to miniaturize and to integrate into a device than is conventional differential scanning calorimetry analysis.
Study Of Dynamic Processes In Protein Synthesis Using Heterogeneous Ribosome Specimens, Jie Fu
Study Of Dynamic Processes In Protein Synthesis Using Heterogeneous Ribosome Specimens, Jie Fu
Legacy Theses & Dissertations (2009 - 2024)
Single-particle reconstruction from cryo-electron microscopy (cryo-EM) images is a widely used technique in studying the structure of macromolecular complexes. This technique allows the visualization of molecules in their native hydrated state. The heterogeneity of two-dimensional projection images, resulting from the co-existence of different states of a macromolecular complex, remains a major obstacle, as it impairs the validity of reconstruction and limits the progress toward higher resolution. On the other hand, co-existing structures, if successfully extracted from a single dataset, can provide valuable information about the equilibrium and dynamics of the biological system being studied.