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Topic Area: Life Sciences Research
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Displaying records 201 to 210 of 251 records.
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201. Spin-Orbit Configuration Interaction Calculation of the Potential Energy Curves of Iodine Oxide
Topic: Life Sciences Research
Published: 4/6/2000
Authors: S Roszak, Morris Krauss, A B Alekseyev, H P Liebermann, R J Buenker
Abstract: An ab initio cofiguration interaction (CI) study including spin-orbit coupling is carried out for the ground and excited states of the IO radical by employing relativistic effective core potentials. The computed spectroscopic constants are in good a ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830117

202. Standard Reference Material for Her2 Testing: Report of a National Institute of Standards and Technology-Sponsored Consensus Workshop
Topic: Life Sciences Research
Published: 6/1/2003
Authors: M E Hammond, Peter E. Dr. Barker, S Taube, S Gutman
Abstract: A workshop was sponsored by National Institute of Standards and Technology (NIST) Cancer Diagnosis Program of National Cancer Institute (CDP NCI), Food and Drug Administration (FDA), and College of American Pathologists (CAP) to address the need for ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830374

203. Standardization of PCR Amplification for Fragile X Trinucleotide Repeat Measurements
Topic: Life Sciences Research
Published: 1/1/2002
Authors: C D O'Connell, Donald H Atha, J P. Jakupciak, Kristy L. Richie
Abstract: To provide the clinical diagnostics community with accurate protocols and measurements for the detection of genetic disorders, we have established a quantitative a quantitative measurement program for trinucleotide repeats associated with human disea ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830252

204. Stark Spectroscopy of Tryptamine Immobilized on a Gold Electrode
Topic: Life Sciences Research
Published: 7/15/1998
Authors: Adolfas Kastytis Gaigalas, Vytautas Reipa, G. Niaura
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=901603

205. Stressing-Out DNA? The Contribution of Serine-Phosphodiester Interactions in Catalysis by Uracil DNA Glycosylase
Topic: Life Sciences Research
Published: 10/17/2000
Authors: R M. Werner, Y. L. Jiang, R. G. Gordley, J. Jagadeesh, Jane E Ladner, G Xiao, M Tordova, G L. Gilliland, J T. Stivers
Abstract: The DNA repair enzyme uracil DNA glycosylase (UDG) pinches the phosphodiester backbone of damaged DNA using the hydroxyl side chains of a conserved trio of serine residues, resulting in flipping of the deoxyuridine from the DNA helix into the enzyme ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830180

206. Structural analysis of heparin by Raman spectroscopy
Topic: Life Sciences Research
Published: 1/1/1996
Authors: Donald H Atha, Adolfas Kastytis Gaigalas, Vytautas Reipa
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=906420

207. Structure (1.3 Å) and Charge States of a Ribonuclease A-Uridine Vanadate Complex: Implications for the Phosphate Ester Hydrolysis Mechanism
Topic: Life Sciences Research
Published: 6/10/1998
Authors: B Wladkowski, L A Svensson, L Sjolin, Jane E Ladner, G L. Gilliland
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=901659

208. Structure and Function of the Xenobiotic Substrate Binding Site and Location of a Potential Non-Substrate Binding Site in a Class Pi Glutathione S-Transferase
Topic: Life Sciences Research
Published: 8/12/1997
Authors: X Ji, M. Tordova, R O'Donnell, J F Parsons, J B Hayden, G L. Gilliland, P Zimniak
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=100240

209. Structure and Reaction in the Active Site of Mammalian Adenylyl Cyclase
Topic: Life Sciences Research
Published: 4/8/2004
Authors: Y. S. Lee, Morris Krauss
Abstract: The reaction path for the catalytic conversion of adenosine triphosphate (ATP) to cyclic adenosine monophosphate (cAMP) by the enzyme mammalian adenylyl cyclase has been calculated theoretically using the Hartree-Fock method. The crystal structure of ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830386

210. Substrate Specificity and Excision Kinetics of Escherichia Coli Endonuclease VIII (Nei) for Modified Bases in DNA Damaged by Free Radicals
Topic: Life Sciences Research
Published: 10/9/2001
Author: M. Dizdaroglu
Abstract: Endonuclease VIII (Nei) is one of three enzymes in Escherichia coli that are involved in base-excision repair of oxidative damage to DNA. We investigated the substrate specificity and excision kinetics of this DNA glycosylase for bases in DNA that ha ...
http://www.nist.gov/manuscript-publication-search.cfm?pub_id=830248



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