The epigenetic post-translational modifications (PTMs) of histone proteins are numerous and have an important role in regulating cellular development. Molecular recognition elements that can bind directly to epigenetic PTMs have previously been developed. The most synthetically accessible of these are a family of molecules called monoaryl-trisulfonate calix[4]arenes. The initial goal of this thesis was to develop research tools consisting of these asymmetrically-derivatized calixarenes immobilized onto a solid resin for the purpose of enrichment of PTM-bearing species. Seven novel resin-immobilized calixarene reagents were created and employed in batch-wise pulldown experiments, as well as chromatographic separations. These experiments produced mixed results: poor efficacy was demonstrated in batch-binding experiments but total separation of certain PTM bearing peptides was achieved in a chromatographic approach. During these studies, a subset of these calixarenes were found to undergo self-association in water in a fashion not previously observed for calixarenes. Secondary goals of the thesis were to create new examples of this self-associating motif, and to characterize and develop structure-function relationships for their assemblies. Eight new self-associating calixarenes were developed and characterized extensively by 1H NMR, isothermal titration calorimetry (ITC), and X-ray crystallography. Self-association was shown to be enthalpically driven with Kd values ranging from 1-20 mM. The dimeric assembly behaviours were remarkably consistent across many different family members, and were shown to persist even in highly competitive media like mock blood and urine. This system represents a novel class of ordered calixarenes assemblies that operate in biological media. / Graduate / 2016-12-23

Thesis (M.S.)--Rochester Institute of Technology, 1991. / Spine title: Active site configuration of GDH. Typescript. References: leaves 73-75.

Thesis (doctoral)--Lund University, 1995. / Added t.p. with thesis inserted.

Thesis (doctoral)--Lund University, 1995. / Added t.p. with thesis inserted.

Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.

Thesis (doctoral)--Lund University, 1994. / Added t.p. with thesis statement inserted.

Thesis (Ph.D.)--University of Nebraska-Lincoln, 2006. / Title from title screen (site viewed July 9, 2007). PDF text: 146 p. : ill. UMI publication number: AAT 3245358. Includes bibliographical references. Also available in microfilm and microfiche formats.

Thesis (Ph.D.)--University of Nebraska-Lincoln, 2007. / Title from title screen (site viewed July 9, 2007). PDF text: 318 p. : ill. UMI publication number: AAT 3249672. Includes bibliographical references. Also available in microfilm and microfiche formats.

Thesis (M.S.)--Montana State University--Bozeman, 2004. / Typescript. Chairperson, Graduate Committee: Mary J. Cloninger. Includes bibliographical references (leaves 133-138).

The design of existing beaded adsorbent materials for column-mode protein purification has emphasized the impact of diffusional transport phenomena upon adsorbent capacity. A design model is presented that optimizes molecular accessibility of proteins relative to the mechanical stability of the material by manipulation of size and solids content for uncross-linked cellulose beads. Cellulose beads of various sizes ranging from about 250 to 1000 pm diameter and having different solids contents were evaluated. Cellulose beads (1.2 mm diameter) gave pressure drops of less than 1 psi per cm of bed at superficial fluid velocities of 100 cm/min in a 1 5 cm bed. Solids content of greater than about 9% cellulose greatly reduced the permeability of large proteins such as thyroglobulin and p-Amylase into the beaded matrix at bead contacting times of 5 and 50 seconds. The amount of permeation in 3% cellulose beads by thyroglobulin at bead contacting times of 5 seconds was about tenfold larger than predicted by diffusion models using the diffusivity of the protein in water. The utility of a low solids content, large bead cellulose support was shown with immobilized IgG (Mr 155 kDa) capturing recombinant human Protein C (M, 62 kDa). The amount of immobilized antibody was varied and immunosorptive capacity of 1 mm cellulose beads was found to be equivalent to that of 0.1 mm cross~linked agarose beads. The immobilization of antibodies to these supports was studied by photomicroscopy of cross-sectioned beads containing immobilized fluorescent labeled antibodies. While 75% of the antibody was immobilized within 0.07 mm of the cellulose bead surface at an antibody density of 1 mg antibody per ml of beads, an appreciable amounts of antibody immobilized deeper into the bead may have been utilized in order to yield capacities equivalent to the smaller agarose beads. The beaded cellulose supports derivatized to form either immunoaffinity or anion exchange matrices exhibited very low non-specific binding. Thus, the particle size, solids content, and extent of derivatization of cellulose matrices can be engineered so as to create matrices that provide high flow rates with low pressure drops while also having desirable adsorptive capacity for proteins. / Ph. D.