Open Access. Powered by Scholars. Published by Universities.®
- Institution
- Keyword
- Publication
- Publication Type
Articles 1 - 3 of 3
Full-Text Articles in Inorganic Chemistry
Study Of The Role Of Biologically-Relevant, Labile Nickel Pools In The Maturation Of Nickel-Dependent Enzymes, Priyanka Basak
Study Of The Role Of Biologically-Relevant, Labile Nickel Pools In The Maturation Of Nickel-Dependent Enzymes, Priyanka Basak
Doctoral Dissertations
Cellular nickel pools, comprised of static and labile pools of nickel complexes, play important roles in maintaining nickel homeostasis in various organisms (microbes, fungi, and plants), which utilize it as a cofactor of one or more nickel enzymes that catalyze specific reactions and are essential for their proper growth and survival in various ecological niches. Like other metals, tight regulation of cellular nickel levels is critical to prevent toxic effects of nickel deprivation, nickel overload, and ‘free’ nickel. While more static nickel pools include nickel tightly bound to nickel-dependent enzymes, nickel in the labile pool is exchangeable and weakly bound …
Pointing The Zinc Finger On Protein Folding: Energetic Investigation Into The Role Of The Metal-Ion In The Metal-Induced Protein Folding Of Zinc Finger Motifs, Inna Bakman-Sanchez
Pointing The Zinc Finger On Protein Folding: Energetic Investigation Into The Role Of The Metal-Ion In The Metal-Induced Protein Folding Of Zinc Finger Motifs, Inna Bakman-Sanchez
Dissertations, Theses, and Capstone Projects
Interactions between inorganic metal-ion cofactors and organic protein scaffolds are important for the proper structure and function of metalloproteins. Zinc finger proteins (ZFPs) are an example of proteins with such crucial metal-protein interactions. Incorporation of the Zn(II)-ion into ZFPs allows for their correct folding into structures that can carry out vital biological functions which include gene expression and tumor suppression. In addition, engineered ZFPs have shown to be promising genetic therapeutics in the clinic. And yet, there is still a gap in a quantitative understanding of the energetic contribution of the metal-protein interactions towards the structure and function of these …
295— Biomimicry: Investigating The Active Site Model Of Lactate Racemase, Stephanie Podguski, Maisy Ross
295— Biomimicry: Investigating The Active Site Model Of Lactate Racemase, Stephanie Podguski, Maisy Ross
GREAT Day Posters
Because of humans’ heavy impact on nature with industrialization and resource extraction, biomimetics, also known as biomimicry, is a study that has emerged. Biomimetics utilizes observations from nature to comprehend the principles of underlying mechanisms and apply concepts that may benefit science, medicine, engineering and the like. An area of biochemistry we are applying this to is the lactate racemase enzyme.This metalloenzyme is found in many prokaryotic organisms and catalyzes the interconversion between the two optical isomers of lactic acid. The structure of this enzyme consists of a square-planar nickel (II) ion coordinated by a histidine residue and a pincer …