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You searched for +publisher:"University of New Hampshire" +contributor:("Rick Cote"). Showing records 1 – 3 of 3 total matches.

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1. Haynie, Benjamin. CHIRAL BIOMOLECULE-INDUCED CHIROPTICAL ACTIVITY IN QUANTUM DOTS.

Degree: MS, 2017, University of New Hampshire

Chiroptical activity in cadmium selenide (CdSe) and cadmium sulfide (CdS) quantum dots (QDs) has been induced by interactions with chiral capping ligands, either with thiol functional group containing biomolecules (e.g. cysteine) or ‘thiol-free’ biomolecules (e.g. malic acid). This induced chirality is theorized to be the result of electronic orbital hybridization between the QD and ligand, not from physical distortion of crystal structure. The polarity of the resulting circular dichroism (CD) spectra shows a ‘mirror-image’ between enantiomers of the same ligand. However, it is possible for two ligands of the same absolute configuration to induce mirror-image CD spectra, as is the case for L-homocysteine and N-acetyl-L-cysteine. This is theorized to be a result of the geometric arrangement of the ligands on the surface of the QD, as predicted by non-empirical ab initio simulations. Further, the functional groups present in the ligand play a role in the induction of chiroptical activity, possibly by affecting the binding geometry or orbital hybridization of the ligand. With this and continuing work, it may be possible to predict the ligand-induced chiroptical activity of these QDs, leading to the opportunity for rational design of chiral QDs and other nanomaterial systems. Advisors/Committee Members: Krisztina Varga, Rick Cote, Christine Caputo.

Subjects/Keywords: chiral; nanoparticles; Nanoscience

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Haynie, B. (2017). CHIRAL BIOMOLECULE-INDUCED CHIROPTICAL ACTIVITY IN QUANTUM DOTS. (Thesis). University of New Hampshire. Retrieved from https://scholars.unh.edu/thesis/1157

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Haynie, Benjamin. “CHIRAL BIOMOLECULE-INDUCED CHIROPTICAL ACTIVITY IN QUANTUM DOTS.” 2017. Thesis, University of New Hampshire. Accessed August 24, 2019. https://scholars.unh.edu/thesis/1157.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Haynie, Benjamin. “CHIRAL BIOMOLECULE-INDUCED CHIROPTICAL ACTIVITY IN QUANTUM DOTS.” 2017. Web. 24 Aug 2019.

Vancouver:

Haynie B. CHIRAL BIOMOLECULE-INDUCED CHIROPTICAL ACTIVITY IN QUANTUM DOTS. [Internet] [Thesis]. University of New Hampshire; 2017. [cited 2019 Aug 24]. Available from: https://scholars.unh.edu/thesis/1157.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Haynie B. CHIRAL BIOMOLECULE-INDUCED CHIROPTICAL ACTIVITY IN QUANTUM DOTS. [Thesis]. University of New Hampshire; 2017. Available from: https://scholars.unh.edu/thesis/1157

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

2. Hogan, Donna. Technique for normalization of cross-linked peptide ion intensity to elucidate enzymatic conformational changes.

Degree: MS, 2017, University of New Hampshire

Cross-linking coupled to Liquid Chromatography/Mass Spectrometry (CXMS) has become an invaluable technique for examining protein-protein interactions and monitoring enzymatic conformational changes. Thus far, comparative quantitation of cross-linked peptides measured by their mass spectrometry (MS) ion intensity is employed to deduce residue cross-linking propensity and spatial proximity. Using two distinct conformations of a structurally well-characterized model protein, we examined the correlation of cross-linked peptide MS signals and distances, but were not able to observe any obvious correlation. Conceivably, several physiochemical factors can affect residue reactivities thus MS signal intensity of the corresponding cross-linked peptides. For NHS ester chemical cross-linkers, the NHS ester functionality often undergo hydrolysis simultaneously to produce dead-end cross-links. Importantly, these dead-end cross-links have proved to be a reliable measurement of the cross-linked lysine residues. Therefore, we propose a novel analytical method by which these dead-end cross-links provide important contextual information about the amino acid side chains involved in cross-linking reactions. Normalization of cross-linked peptide ion intensity against the cognate dead-end cross-links yields a value (proportional cross-link intensity) which can provide a basis for comparison across different biochemical conditions or enzyme interaction states. In this work, we use this method in conjunction with isotopically labeled cross-linking reagents to examine the conformational changes on the part of HtpG (the E. coli homolog of Hsp90) and a truncation mutant of one of its client proteins, Staphylococcal Nuclease. Dramatic conformational changes are observed in the client protein as HtpG transitions through its ATPase cycle. Next, we apply label-free quantitation and the proportional cross-link intensity model to the vertebrate retina enzyme Phosphodiesterase 6 (PDE6). Through pair-wise combinations of the catalytic subunits, cyclic GMP, and the inhibitory subunits, we observe conformational changes in response to allosteric binding of regulatory subunits and molecules. Advisors/Committee Members: Feixia Chu, Rick Cote, Estelle Hrabak.

Subjects/Keywords: chemical cross-linking; enzymes; LCMS; proteins; Biophysics; Molecular biology; Biochemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Hogan, D. (2017). Technique for normalization of cross-linked peptide ion intensity to elucidate enzymatic conformational changes. (Thesis). University of New Hampshire. Retrieved from https://scholars.unh.edu/thesis/1106

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Hogan, Donna. “Technique for normalization of cross-linked peptide ion intensity to elucidate enzymatic conformational changes.” 2017. Thesis, University of New Hampshire. Accessed August 24, 2019. https://scholars.unh.edu/thesis/1106.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Hogan, Donna. “Technique for normalization of cross-linked peptide ion intensity to elucidate enzymatic conformational changes.” 2017. Web. 24 Aug 2019.

Vancouver:

Hogan D. Technique for normalization of cross-linked peptide ion intensity to elucidate enzymatic conformational changes. [Internet] [Thesis]. University of New Hampshire; 2017. [cited 2019 Aug 24]. Available from: https://scholars.unh.edu/thesis/1106.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Hogan D. Technique for normalization of cross-linked peptide ion intensity to elucidate enzymatic conformational changes. [Thesis]. University of New Hampshire; 2017. Available from: https://scholars.unh.edu/thesis/1106

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

3. Chan, Jonathan. The Role of Adenylate Cyclase in Hydra Magnipapillata Phototransduction.

Degree: MS, 2017, University of New Hampshire

Cnidarians are members of an early branching phylum of animals with unexpectedly complex sensory capable of detecting light, chemical, and mechanical stimuli despite lacking the specialized sensory organs that bilaterian animals commonly possess. Although there are many obvious differences when comparing bilaterian sensory systems with that of Cnidarians, there is also a surprising degree of similarity. Recent studies reveal that in one species of Cnidaria, the freshwater polyp Hydra magnipapillata, there exists a phototransduction cascade mediated by the G-protein coupled receptor (GPCR) opsin and cyclic nucleotide-gated ion channels; features shared with the vertebrate phototransduction cascade. Other research has shown an increase in cytosolic cAMP levels in response to opsin signaling in heterologous gene expression studies of a jellyfish opsin, which in eukaryotic cells is mediated by the enzyme adenylate cyclase (AC). However, this is where our knowledge of cnidarian phototransduction ends. Here we investigate the possibility that AC plays an active role in hydra phototransduction. We show through a phylogenetic analysis of metazoan AC protein sequences that the hydra genome possesses an AC gene (hmAC) that is orthologous to human AC9. Next, we used in situ hybridization with riboprobes against hmAC to show its co-expression with opsin (hmOps2) in hydra sensory neurons. A photo-response experiment is then performed in the presence or absence of pharmacological agents that affect AC activity. To determine the functional relationship between hmAC and hmOps2, dark-adapted hydra animals are presented with various drug conditions, a light stimulus, and assayed for contraction. Our results support the view that AC plays an active role in the hydra photo-response, suggesting that AC may be a regulator of the cnidarian phototransduction cascade. This study advances our understanding of the early origins and diversification of animal phototransduction. Advisors/Committee Members: David C Plachetzki, Rick Cote, Xuanmao Chen.

Subjects/Keywords: adenylate cyclase; cnidaria; hydra magnipapillata; in situ hybridization; phototransduction; sensory biology; Genetics; Biochemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Chan, J. (2017). The Role of Adenylate Cyclase in Hydra Magnipapillata Phototransduction. (Thesis). University of New Hampshire. Retrieved from https://scholars.unh.edu/thesis/1120

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Chan, Jonathan. “The Role of Adenylate Cyclase in Hydra Magnipapillata Phototransduction.” 2017. Thesis, University of New Hampshire. Accessed August 24, 2019. https://scholars.unh.edu/thesis/1120.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Chan, Jonathan. “The Role of Adenylate Cyclase in Hydra Magnipapillata Phototransduction.” 2017. Web. 24 Aug 2019.

Vancouver:

Chan J. The Role of Adenylate Cyclase in Hydra Magnipapillata Phototransduction. [Internet] [Thesis]. University of New Hampshire; 2017. [cited 2019 Aug 24]. Available from: https://scholars.unh.edu/thesis/1120.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Chan J. The Role of Adenylate Cyclase in Hydra Magnipapillata Phototransduction. [Thesis]. University of New Hampshire; 2017. Available from: https://scholars.unh.edu/thesis/1120

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.