LEADER 00000nam  2200349   4500 
001    AAI3128870 
005    20051108095751.5 
008    051108s2004                        eng d 
020    0496761315 
035    (UnM)AAI3128870 
040    UnM|cUnM 
100 1  Kostic, Milka 
245 10 Structural and dynamical studies of metal containing 
       proteins by NMR 
300    235 p 
500    Source: Dissertation Abstracts International, Volume: 65-
       04, Section: B, page: 1883 
500    Adviser:  Thomas C. Pochapsky 
502    Thesis (Ph.D.)--Brandeis University, 2004 
520    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 
590    School code: 0021 
590    DDC 
650  4 Chemistry, Physical 
650  4 Chemistry, Biochemistry 
650  4 Biophysics, General 
690    0494 
690    0487 
690    0786 
710 20 Brandeis University 
773 0  |tDissertation Abstracts International|g65-04B 
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