Temple University, Department of Chemistry, has no high-field NMR equipment, while the Department of Biochemistry, School of Medicine at Temple has a 300 MHz, wide-bore Bruker NMR instrument which is presently being booked to near capacity and is insufficient for various types of NMR experiments needed to be performed by the applicants. Research projects described by the applicants herein require information which can best be obtained by high-field, high-resolution NMR techniques. The purpose of this application is to make instrumentation available to support the research of the investigators named above as well as to provide occasional use by other investigators at Temple University. Projects to be supported by the application include: a) structure and dynamics of epidermal growth factors b) physical studies of B-lketo-acyl-ACP-synthetase c) reaction mechanisms of glycohydrolases d) catalytic mechanisms of P-enolpyruvate carboxylkinase and pyruvate carboxylase e) structure of the 2',5' - Oligoadenylates and 2',5' -Oligoadenylate Analogs f) characterization of products in the biosynthesis of 2'-Chloro- 2'-Deoxycoformycin g) mechanisms of threonine synthase and cystathionine delta- synthase h) chlorophyll b synthesis and formation of light-harvesting complexes i) 33S - NMR studies of sulfur oxidation and metabolism j) studies of acetylcholinesterase dephosphorylation compounds by 31P - NMR k) 13C - NMR of conducting polymers

Project Start
1988-04-04
Project End
1989-04-03
Budget Start
1988-04-04
Budget End
1989-04-03
Support Year
1
Fiscal Year
1988
Total Cost
Indirect Cost
Name
Temple University
Department
Type
Schools of Arts and Sciences
DUNS #
City
Philadelphia
State
PA
Country
United States
Zip Code
19122
Daragan, V A; Mayo, K H (1993) Tri- and diglycine backbone rotational dynamics investigated by 13C NMR multiplet relaxation and molecular dynamics simulations. Biochemistry 32:11488-99
Daragan, V A; Ilyina, E; Mayo, K H (1993) Effects of molecular association on structure and dynamics of a collagenous peptide. Biopolymers 33:521-33
Yang, Y; Barker, S; Chen, M J et al. (1993) Effect of low molecular weight aliphatic alcohols and related compounds on platelet factor 4 subunit association. J Biol Chem 268:9223-9
Yang, Y; Mayo, K H (1993) Alcohol-induced protein folding transitions in platelet factor 4: the O-state. Biochemistry 32:8661-71
Daragan, V A; Kloczewiak, M A; Mayo, K H (1993) 13C nuclear magnetic resonance relaxation-derived psi, phi bond rotational energy barriers and rotational restrictions for glycine 13C alpha-methylenes in a GXX-repeat hexadecapeptide. Biochemistry 32:10580-90
Mayo, K H; Barker, S; Kuranda, M J et al. (1992) Molten globule monomer to condensed dimer: role of disulfide bonds in platelet factor-4 folding and subunit association. Biochemistry 31:12255-65
Mayo, K H (1991) Low-affinity platelet factor 4 1H NMR derived aggregate equilibria indicate a physiologic preference for monomers over dimers and tetramers. Biochemistry 30:925-34
Chen, M J; Mayo, K H (1991) Human platelet factor 4 subunit association/dissociation thermodynamics and kinetics. Biochemistry 30:6402-11
Mayo, K H; Parra-Diaz, D; McCarthy, J B et al. (1991) Cell adhesion promoting peptide GVKGDKGNPGWPGAP from the collagen type IV triple helix: cis/trans proline-induced multiple 1H NMR conformations and evidence for a KG/PG multiple turn repeat motif in the all-trans proline state. Biochemistry 30:8251-67
Mayo, K H; Mvele, O M; Puri, R N (1990) Proton magnetic resonance spectroscopic analysis of diadenosine 5',5""'-polyphosphates. FEBS Lett 265:97-100

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