Basic Atomic Physics

Contains reports on five research projects.National Science Foundation Grant PHY 89-19381U.S. Navy - Office of Naval Research Grant N00014-90-J-1322Joint Services Electronics Program Contract DAAL03-89-C-0001National Science Foundation Grant PHY 86-05893U.S. Army Research Office Contract DAAL03-89-K-0082U.S. Navy - Office of Naval Research Grant N00014-89-J-1207U.S. Navy - Office of Naval Research Grant N00014-90-J-164

Atomic Resonance and Scattering

Contains reports on six research projects.National Science Foundation (Grant PHY 83-06273)U.S. Navy - Office of Naval Research (Contract N00014-79-C-0183)Joint Services Electronics Program (Contract DAALO03-86-K-0002)National Science Foundation (Grant PHY 84-11483)National Science Foundation (Grant PHY 86-05893)National Science Foundation (Grant ECS 84-21392)U.S. Navy - Office of Naval Research (Contract N00014-83-K-0695)National Science Foundation (Grant CHE 84-21392

Atomic Resonance and Scattering

Contains reports on six research projects.National Science Foundation (PHY83-06273)Joint Services Electronics Program (DAAL03-86-K-0002)National Science Foundation (PHY84-11483)U.S. Navy-Office of Naval Research (Grant N00014-79-C-0183)Joint Services Electronics Program (Contract DAAG29-83-K-0003)National Science Foundation (Grant PHY83-07172-A01)U.S. Navy - Office of Naval Research (Grant N00014-83-K-0695)National Science Foundation (Grant CHE84-21392

Basic Atomic Physics

Contains reports on five research projects.Joint Services Electronics Program Contract DAAL03-89-C-0001National Science Foundation Grant PHY 87-06560National Science Foundation Contract PHY 86-05893U.S. Army Research Office Contract DAAL03-89-K-0082U.S. Navy - Office of Naval Research Contract N00014-89-J-1207U.S. Navy - Office of Naval Research Contract N00014-83-K-069

Atomic Resonance and Scattering

Contains reports on two research projects.National Science Foundation (Grant PHY 87-06560)Joint Services Electronics Program (Contract DAAL03-86-K-O002)U.S. Navy - Office of Naval Research (Contract N00014-83-K-0695)National Science Foundation (Grant PHY 86-05893

Basic Atomic Physics

Contains reports on seven research projects.National Science Foundation (Grant PHY 87-06560)Joint Services Electronics Program (Contract DAAL03-86-K-0001)Joint Services Electronics Program (Contract DAAL03-89-C-0002)National Science Foundation (Grant PHY 86-05893)U.S. Navy - Office of Naval Research (Contract N00014-83-K-0695)U.S. Navy - Office of Naval Research (Contract N00014-89-J-1207

Basic Atomic Physics

Contains reports on five research projects.National Science Foundation Grant PHY 89-19381U.S. Navy - Office of Naval Research Contract N00014-90-J-1322Joint Services Electronics Program Contract DAAL03-89-C-0001Joint Services Electronics Program Contract DAAL03-92-C-0001U.S. Army Research Office Contract DAAL03-89-K-0082U.S. Navy - Office of Naval Research Grant N00014-89-J-1207U.S. Navy - Office of Naval Research Grant N00014-90-J-1642National Science Foundation Grant PHY 86-05893National Science Foundation Grant PHY 89-2176

Energy level structure of atoms in magnetic fields

Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Physics, 1991.Includes bibliographical references (leaves 155-162).byu Chun-Ho Iu.Ph.D

One amino acid makes a difference-Characterization of a new TPMT allele and the influence of SAM on TPMT stability

Thiopurine induced toxicity is associated with defects in the thiopurine methyltransferase (TPMT) gene. TPMT is a polymorphic enzyme, with most of the single nucleotide polymorphisms (SNPs) causing an amino acid change, altering the enzymatic activity of the TPMT protein. In this study, we characterize a novel patient allele c.719A amp;gt; C, named TPMT*41, together with the more common variant *3C c.719A amp;gt; G, resulting in an amino acid shift at tyrosine 240 to serine, p.Y240S and cysteine, p.Y240C respectively. We show that the patient heterozygote for c.719A amp;gt; C has intermediate enzymatic activity in red blood cells. Furthermore, in vitro studies, using recombinant protein, show that TPMT p.Y240S is less stable than both TPMTwt and TPMT p.Y240C. The addition of SAM increases the stability and, in agreement with Isothermal Titration Calorimetry (ITC) data, higher molar excess of SAM is needed in order to stabilize TPMT p.Y240C and TPMT p.Y240S compared to TPMTwt. Molecular dynamics simulations show that the loss of interactions is most severe for Y240S, which agrees with the thermal stability of the mutations. In conclusion, our study shows that SAM increases the stability of TPMT and that changing only one amino acid can have a dramatic effect on TPMT stability and activity.Funding Agencies|LiU Cancer Network; Medical Research Council of Southeast Sweden; Lars Hiertas Memory Foundation; Samariten Foundation; Swedish Society of Medicine Linkoping; Ostgotaregionens Cancerfond; Swedish e-Science Research Center</p