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Author Kostic, Milka
Title Structural and dynamical studies of metal containing proteins by NMR
book jacket
Descript 235 p
Note Source: Dissertation Abstracts International, Volume: 65-04, Section: B, page: 1883
Adviser: Thomas C. Pochapsky
Thesis (Ph.D.)--Brandeis University, 2004
Metal containing proteins represent an extremely diverse group of proteins that are involved in large variety of processes in all three kingdoms of life. From the NMR viewpoint, metal containing proteins can be roughly divided into proteins containing paramagnetic and diamagnetic metals. Presence of the paramagnetic metals possess certain challenges to NMR characterization of such proteins. Part I of this thesis describes two different approaches for sequence specific resonance assignments in paramagnetic regions of metal containing proteins. First approach is based on using the combination of selective labeling and longitudinal relaxation time, T1 measurements for residue specific assignments. Second approach is based on the application of the newly developed 13C-detected 2D NMR methods based on rapid recycle HMQC pulse sequence. Part II of this Thesis describes approaches to characterize paramagnetic protein structure and dynamics using NMR. Detailed NMR studies of a class of Cys4Fe2S2 ferredoxins, that transfer electrons to different members of cytochrome P450 family of enzymes, with the special focus on redox-dependent behavior of these proteins, are described. In order to establish specific features responsible for observed redox-dependent behavior of different members of Cys4Fe2S 2 vertebrate-type ferredoxins family, detailed comparative studies were done on three Cys4Fe2S2 ferredoxins and results are presented here. In addition, critical role of a strictly conserved basic residue found in Cys4Fe2S2 ferredoxins in transmitting redox-dependent structural and dynamical perturbations is established and discussed. Finally, Part III introduces several points of interest regarding methionine metabolism and reports on work done in order to obtain complete resonance assignments and structure of enolase-phosphatase, E1, from methionine salvage pathway of Klebsiella oxytoca are reported, and some interesting features of this bi-functional enzyme are discussed
School code: 0021
Host Item Dissertation Abstracts International 65-04B
Subject Chemistry, Physical
Chemistry, Biochemistry
Biophysics, General
Alt Author Brandeis University
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