Search Results - "EIDSNESS, M. K"

Variation of Molecular Alignment as a Means of Resolving Orientational Ambiguities in Protein Structures from Dipolar Couplings by Al-Hashimi, H.M, Valafar, H, Terrell, M, Zartler, E.R, Eidsness, M.K, Prestegard, J.H

“…Residual dipolar couplings for pairs of proximate magnetic nuclei in macromolecules can easily be measured using high-resolution NMR methods when the molecules…”
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Structural Basis for Thermostability in Aporubredoxins from Pyrococcus furiosus and Clostridium pasteurianum by Zartler, Edward R, Jenney, Francis E, Terrell, Mark, Eidsness, Marly K, Adams, Michael W. W, Prestegard, James H

“…The structures of apo- and holorubredoxins from Pyrococcus furiosus (PfRd) and Clostridium pasteurianum (CpRd) have been investigated and compared using…”
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Evidence for Selenocysteine Coordination to the Active Site Nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus by Eidsness, Marly K., Scott, Robert A., Prickril, Benet C., DerVartanian, Daniel V., Legall, Jean, Moura, Isabel, Jose J. G. Moura, Peck, Harry D.

“…Ni and Se x-ray absorption spectroscopic studies of the [NiFeSe]hydrogenases from Desulfovibrio baculatus are described. The Ni site geometry is…”
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EXAFS analysis of xanthine oxidase complexes with alloxanthine, violapterin, and 6-pteridylaldehyde by Hille, R, George, G. N, Eidsness, M. K, Cramer, S. P

“…The structure of the molybdenum site of xanthine oxidase in the complexes with alloxanthine, violapterin, and 6-pteridylaldehyde has been investigated by using…”
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X-ray absorption spectroscopic studies of the high-spin iron(II) active site of isopenicillin N synthase : evidence for Fe-S interaction in the enzyme-substrate complex by SCOTT, R. A, SHENGKE WANG, EIDSNESS, M. K, AIDAS KRIAUCIUNAS, FROLIK, C. A, CHEN, V. J

“…Isopenicillin N synthase from Cephalosporium acremonium (IPNS; M(r) 38.4K) is an Fe(2+)-requiring enzyme which catalyzes the oxidative conversion of…”
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Near-zero background cloning of PCR products by Zeng, Q, Eidsness, M K, Summers, A O

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Expression of a synthetic gene coding for the amino acid sequence of Clostridium pasteurianum rubredoxin by Eidsness, M K, O'Dell, S E, Kurtz, Jr, D M, Robson, R L, Scott, R A

“…A synthetic gene based on the published amino acid sequence for Clostridium pasteurianum rubredoxin was constructed, cloned in Escherichia coli 71/18 and…”
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Reactions of auranofin and Et3PAuCl with bovine serum albumin by COFFER, M. T, SHAW, C. F. III, EIDSNESS, M. K, WATKINS, J. W. II, ELDER, R. C

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Leucine 41 is a gate for water entry in the reduction of Clostridium pasteurianum rubredoxin by Min, Tongpil, Ergenekan, Can E., Eidsness, Marly K., Ichiye, Toshiko, Kang, Chulhee

“…Biological electron transfer is an efficient process even though the distances between the redox moieties are often quite large. It is therefore of great…”
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EXAFS and WAXS structure determination for an antiarthritic drug, sodium gold(I) thiomalate by Elder, R. C, Ludwig, K, Cooper, J. N, Eidsness, M. K

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Modulation of the Redox Potential of the [Fe(SCys)4] Site in Rubredoxin by the Orientation of a Peptide Dipole by Eidsness, Marly K, Burden, Amy E, Richie, Kimberly A, Kurtz, Donald M, Scott, Robert A, Smith, Eugene T, Ichiye, Toshiko, Beard, Brian, Min, TongPil, Kang, ChulHee

“…Rubredoxins (Rds) may be separated into two classes based upon the correlation of their reduction potentials with the identity of residue 44; those with Ala44…”
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Hydrogen Bonds in Rubredoxins from Mesophilic and Hyperthermophilic Organisms by Bougault, Catherine M, Eidsness, Marly K, Prestegard, James H

“…The extent and strength of the hydrogen bond networks in rubredoxins from the hyperthermophile Pyrococcus furiosus (PfRd), and its mesophilic analogue…”
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Dissecting Contributions to the Thermostability of Pyrococcus furiosus Rubredoxin:  β-Sheet Chimeras by Eidsness, Marly K, Richie, Kimberly A, Burden, Amy E, Kurtz, Donald M, Scott, Robert A

“…The contributions to thermostability of interactions within the β-sheet region of rubredoxins (Rds) were investigated by examining proteins in which β-strand…”
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EXAFS of Klebsiella pneumoniae nitrogenase MoFe protein from wild-type and nif V mutant strains by Eidsness, M. K, Flank, A. M, Smith, B. E, Flood, A. C, Garner, C. D, Cramer, S. P

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X-ray absorption spectroscopic evidence for a unique nickel site in Clostridium thermoaceticum carbon monoxide dehydrogenase by Cramer, Stephen P, Eidsness, Marly K, Pan, W. H, Morton, Thomas A, Ragsdale, Steve W, DerVartanian, Daniel V, Ljungdahl, Lars G, Scott, Robert A

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Reactions of auranofin and chloro(triethylphosphine)gold with bovine serum albumin by Coffer, Mary T, Shaw, C. Frank, Eidsness, M. K, Watkins, J. W, Elder, R. C

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Crystal structure of rubredoxin from Pyrococcus furiosus at 0.95 Å resolution, and the structures of N-terminal methionine and formylmethionine variants of Pf Rd. Contributions of N-terminal interactions to thermostability by Bau, Robert, Rees, D. C., Kurtz, Donald M., Scott, Robert A., Huang, Heshu, Adams, Michael W. W., Eidsness, M. K.

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Bovine serum albumin-gold thiomalate complex: gold-197 Moessbauer, EXAFS and XANES, electrophoresis, sulfur-35 radiotracer, and fluorescent probe competition studies by Shaw, C. Frank, Schaeffer, N. A, Elder, R. C, Eidsness, M. K, Trooster, Jan M, Calis, Gijs H. M

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Recombinant Escherichia coli biotin synthase is a [2Fe-2S] super(2+) protein in whole cells by Cosper, M M, Jameson, GNL, Eidsness, M K, Huynh, B H, Johnson, M K

“…EPR and Moessbauer spectroscopies have been used to determine the type and properties of the iron-sulfur clusters present in homologously expressed recombinant…”
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The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine by Cosper, Michele Mader, Jameson, Guy N L, Davydov, Roman, Eidsness, Marly K, Hoffman, Brian M, Huynh, Boi Hanh, Johnson, Michael K

“…The combination of resonance Raman, electron paramagnetic resonance and Mössbauer spectroscopies has been used to investigate the effect of…”
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