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Base specific binding of copper (II) to Z-DNA : 1.3 A single crystal structure of d(m⁵CGUAm⁵CG) soaked with CuCl₂Geierstanger, Bernhard H. 06 July 1990 (has links)
Graduation date: 1991
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Factors affecting circulating growth hormone binding protein in chickensTobar-Dupres, Eric T. 13 August 1992 (has links)
Growth hormone binding protein (GHBP) may be an important
factor in the regulation of growth as well as an indirect,
less invasive way of predicting the status of growth hormone
receptors. Several factors (age, nutritional status, sex,
and glucocorticoid administration) have been reported to
influence circulating growth hormone (GH) levels, growth
hormone receptor (GHR) activity and/or GHBP in mammalian
species. Therefore, the studies conducted in this research
were designed to determine if these factors have any affect
on serum GHBP in the young broiler chicken. Serum GHBP
activity was expressed as a percent specifically bound ¹²⁵IhGH
(%SB), as measured by a dextran-coated charcoal assay.
Serum GHBP activity was highest (mean %SB= 14.6 ± 1.2) at
hatch aniedecreased linearly (r= -.9516) to 4 wk of age
(mean %SB= 4.1 ± 0.6). Sex had no significant affect on
serum GHBP activity from hatch to 4 wk of age. Short term
nutrient deprivation (24 h fast) of 4 wk old birds had no
significant affect on serum GHBP activity, nor did
refeeding. Feeding birds nutrient poor diets (low energy,
low protein or low energy and low protein) did not
significantly affect serum GHBP activity when compared to
birds fed a commercial broiler diet. Pulsatile delivery of
cortisone acetate (1, 5 and 10 mg/d/b) had no affect on
serum GHBP activity at any dose. These results suggest that
serum GHBP activity in the chicken is not affected by many
factors which do influence GHBP in mammalian species. The
lack of response to nutrient deprivation and cortisone
acetate may be a factor related to the age of the birds used
in these studies. / Graduation date: 1993
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Crystallographic studies of <i>Escherichia coli</i> phosphoenolpyruvate carboxykinaseMatte, Alan Michael 01 January 1996 (has links)
The crystal structure of ATP-dependent phosphoenolpyruvate carboxykinase (ATP-oxaloacetate carboxy-lyase, (transphosphorylating), E.C. 4.1.1.49; PCK) from Escherichia coli K12 has been determined using a combination of multiple isomorphous replacement and density modification, and refined to a R-index of 0.202 (R-free = 0.244) at 1.9 A resolution. PCK catalyses the decarboxylation and ATP-dependent phosphorylation of oxaloacetate to form phosphoenolpyruvate, the first committed step of gluconeogenesis in E. coli. Each PCK molecule consists of a 275 residue N-terminal and 265 residue C-terminal ar mononucleotide-binding domain, with the active site located within a cleft between the two domains. PCK is an open-faced, mixed $\alpha/\beta$ protein with a unique overall tertiary structure. The putative phosphate-binding region of the ATP-binding site adopts the P-loop motif common to many ATP- and GTP-binding proteins. However, the â-sheet topology of the mononucleotide-binding fold of PCK differs from all other families within the P-loop containing nucleoside triphosphate hydrolase superfamily, suggesting PCK represents the first member of a new family of such proteins. The mononucleotide-binding domain also differs in structure from the classical mononucelotide-binding fold (CMBF), common to adenylate kinase, RecA, p21$\sp{{Ha}-ras}$, and elongation factor-Tu. Several highly-conserved amino acid residues among the ATP-dependent PCK family, including R65, Y207, K212, K213, H232, K254, T255, D269, K288 and R333 appear to make up the active site of the enzyme. A cysteine residue, C233, is located near the active site, and in the E. coli enzyme this residue is buried and is probably not involved in substrate binding or catalysis. Previous chemical modification studies, on several ATP- and GTP-dependent PCKs, have been assessed in view of these structural results. A mechanism of catalysis based on these and additional results is proposed. The structure of E. coli PCK complexed with the calcium-analogue Tb$\sp{3+}$ has been refined to an R-index of 0.205 (R-free = 0.259) at 2.5 A. Two binding sites for Tb$\sp{3+}$ have been determined, one within the active site coordinating to the side chains of K213, H232, and D269, and the other within the C-terminal domain, coordinating to the side chains of E508 and E511. No large structural movements are observed in PCK as a result of Tb$\sp{3+}$ binding, even though Ca$\sp{2+}$ is a known activator.
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Sequential injection analysis for the investigation of biomolecular interactions /Connors, Wendy Lee. January 2000 (has links)
Thesis (Ph. D.)--University of Washington, 2000. / Vita. Includes bibliographical references (leaves 129-140).
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Isolation and characterization of hermes, an RNA-binding protein gene expressed in the developing heart /Gerber, Wendy Veronica, January 1999 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 1999. / Vita. Includes bibliographical references (leaves 114-129). Available also in a digital version from Dissertation Abstracts.
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Dissecting the cooperative energetics of the binding interactions between peptides and MHC class II proteins /McFarland, Benjamin James, January 2001 (has links)
Thesis (Ph. D.)--University of Washington, 2001. / Vita. Includes bibliographical references (leaves 172-200).
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Protein interactions with the catechol estrogens 4-hydroxyestrone and 4-hydroxyestradiol in mouse tissue lysate : binding and metabolism studies /Philips, Brian John, January 2001 (has links)
Thesis (Ph. D.)--University of Missouri--Columbia, 2001. / "December 2001. Typescript. Vita. Includes bibliographical references (leaves 326-347). Also available on the Internet.
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Functional polymers and proteins at interfaces /Schilke, Karl F. January 1900 (has links)
Thesis (Ph. D.)--Oregon State University, 2010. / Printout. Includes bibliographical references (leaves 173-189). Also available on the World Wide Web.
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Polyunsaturated fatty acids suppress hepatic lipogenic gene transcription by accelerating sterol regulatory element binding protein-1 transcript decay /Xu, Jing, January 2001 (has links)
Thesis (Ph. D.)--University of Texas at Austin, 2001. / Vita. Includes bibliographical references (leaves 148-173). Available also in a digital version from Dissertation Abstracts.
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Structural and functional aspects of the multifaceted SlyD in Helicobacter pyloriCheng, Tianfan., 程天凡. January 2012 (has links)
As a ubiquitous protein-folding helper in bacterial cytosol, SlyD is a peptidylprolyl
isomerase (PPIase) of the FK506-binding protein (FKBP) family. It has two
important functional domains, the IF (insert-in-flap) domain with chaperone
activity and the FKBP domain with PPIase activity. It also possesses a histidine- and
cysteine-rich C-terminal metal-binding domain, which binds to selected
divalent metal ions (e.g. Ni2+, Zn2+) and is critical for participation in metal
trafficking for metalloenzymes.
SlyD from Helicobacter pylori was investigated both structurally and functionally
by a variety of biophysical, biochemical and molecular biology techniques.
HpSlyD was cloned, expressed and purified. It binds to Ni2+ and Zn2+ with
dissociation constants (Kd) of 2.74 and 3.79 μM, respectively. Both Ni2+ and Zn2+
can competitively bind to HpSlyD. The C-terminus was demonstrated to convey
nickel resistance in vivo. It also binds to Bi3+ with Kd of 4.4 × 10-24 M.
Furthermore, Zn2+, Cu2+ and Bi3+ can induce the dimerization or oligomerization
of HpSlyD.
The solution structure of the C-terminus-truncated SlyD from Helicobacter pylori
(HpSlyDΔC) was determined by NMR, which demonstrates that HpSlyDΔC folds
into two well-separated, orientation-independent domains. Both the FKBP and IF
domains fold into a structure consisting of a four-stranded antiparallel β-sheet and
an α-helix.
Binding of Ni2+ instead of Zn2+ induced the conformational changes in FKBP
domain, where the active sites are positioned, suggesting a regulatory role of
nickel on the function of HpSlyD. It was also confirmed that HpSlyD can
associate with the Tat (twin-arginine translocation) signal peptide from small
subunit of [NiFe] hydrogenase (HydA), an accessory protein HpHypB for [NiFe]
hydrogenase mainly by the IF domain. Surprisingly HpSlyD was found to form a
complex with HpUreE, a urease chaperone, indicative of the “cross-talk” between
[NiFe] hydrogenase and urease.
The possible mechanism of HpSlyD for the cooperation with HpHypB was also
explored. In the presence of different metal ions, HpSlyD was shown to regulate
the GTPase activity of HpHypB, implicating the possible metal transfer induced
by HpSlyD. It was suggested that HpSlyD modulates the nickel insertion of [NiFe]
hydrogenase by controlling the GTPase activity of HpHypB. In this thesis, the
SlyD protein from H. pylori was shown as an important regulator for the
activation of both [NiFe] hydrogenase and urease. / published_or_final_version / Chemistry / Doctoral / Doctor of Philosophy
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