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Full-Text Articles in Life Sciences
Multimode Analysis Of Nanoscale Biomolecular Interactions, Purushottam Babu Tiwari
Multimode Analysis Of Nanoscale Biomolecular Interactions, Purushottam Babu Tiwari
FIU Electronic Theses and Dissertations
Biomolecular interactions, including protein-protein, protein-DNA, and protein-ligand interactions, are of special importance in all biological systems. These interactions may occer during the loading of biomolecules to interfaces, the translocation of biomolecules through transmembrane protein pores, and the movement of biomolecules in a crowded intracellular environment. The molecular interaction of a protein with its binding partners is crucial in fundamental biological processes such as electron transfer, intracellular signal transmission and regulation, neuroprotective mechanisms, and regulation of DNA topology. In this dissertation, a customized surface plasmon resonance (SPR) has been optimized and new theoretical and label free experimental methods with related analytical …
Conformational Dynamics Associated With Ligand Binding To Vertebrate Hexa-Coordinate Hemoglobins, Luisana Astudillo
Conformational Dynamics Associated With Ligand Binding To Vertebrate Hexa-Coordinate Hemoglobins, Luisana Astudillo
FIU Electronic Theses and Dissertations
Neuroglobin (Ngb) and cytoglobin (Cygb) are two new additions to the globin family, exhibiting heme iron hexa-coordination, a disulfide bond and large internal cavities. These proteins are implicated in cytoprotection under hypoxic-ischemic conditions, but the molecular basis of their cytoprotective function is unclear.
Herein, a photothermal and spectroscopic study of the interactions of diatomic ligands with Ngb, Cygb, myoglobin and hemoglobin is presented. The impact of the disulfide bond in Ngb and Cygb and role of conserved residues in Ngb His64, Val68, Cys55, Cys120 and Tyr44 on conformational dynamics associated with ligand binding/dissociation were investigated. Transient absorption and photoacoustic calorimetry …