Open Access Theses and Dissertations

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You searched for +publisher:"University of Missouri – Columbia" +contributor:("Van Doren, Steven R."). Showing records 1 – 2 of 2 total matches.

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1. Marcink, Tara. Membrane interactions with membrane type 1 matrix metalloproteinase.

Degree: 2018, University of Missouri – Columbia

URL: http://hdl.handle.net/10355/68915 

Membrane type 1 matrix metalloproteinase (MT1-MMP) is essential to a myriad of extracellular activities including tumor cell migration and angiogenesis. At the cell surface, MT1-MMP is a major factor in the proteolysis of receptors, growth factors, and collagen. MT1-MMP extracellular domains bind the cell surface which can be influential in bringing these complexes together. This study uses new techniques to uncover the interactions between MT1-MMP and the cell surface. Described here is the development of techniques in protein and lipid preparations, NMR data acquisition, and structure determination by molecular dynamics simulations. Through these methods, the HPX domain was shown to bind nanodiscs by opposing tips of blade II and blade IV. The protruding part of these tips contain an EPGYPK sequence that are seen dipping into the membrane surface making contact with the lipid head groups. Blade IV membrane binding allows collagen to bind unhindered. Both blade II and blade IV membrane binding structures are shown to be favorable for homodimerization without disruption of the collagen binding site. The catalytic domain is shown to at least transiently bind membranes. This study then hypothesizes and discusses how these interactions impact both future peripheral protein membrane interaction studies and uncover similarities between the MMP family. Advisors/Committee Members: Van Doren, Steven R. (advisor).
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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Marcink, T. (2018). Membrane interactions with membrane type 1 matrix metalloproteinase. (Thesis). University of Missouri – Columbia. Retrieved from http://hdl.handle.net/10355/68915

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):

Marcink, Tara. “Membrane interactions with membrane type 1 matrix metalloproteinase.” 2018. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. http://hdl.handle.net/10355/68915.

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

MLA Handbook (7th Edition):

Marcink, Tara. “Membrane interactions with membrane type 1 matrix metalloproteinase.” 2018. Web. 15 Apr 2021.

Vancouver:

Marcink T. Membrane interactions with membrane type 1 matrix metalloproteinase. [Internet] [Thesis]. University of Missouri – Columbia; 2018. [cited 2021 Apr 15]. Available from: http://hdl.handle.net/10355/68915.

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

Council of Science Editors:

Marcink T. Membrane interactions with membrane type 1 matrix metalloproteinase. [Thesis]. University of Missouri – Columbia; 2018. Available from: http://hdl.handle.net/10355/68915

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


University of Missouri – Columbia

2. Xu, Jia (Research scientist). Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis.

Degree: 2016, University of Missouri – Columbia

URL: https://doi.org/10.32469/10355/59793 

Phosphomannomutase/phosphoglucomutase (PMM/PGM) contributes to the infectivity of an opportunistic human pathogen Pseudomonas aeruginosa by participating in carbohydrate biosynthesis. As a phospho-transfer enzyme, PMM/PGM catalyzes reversible conversion between 1- and 6- phosphosugars via a bisphosphorylated hexose intermediate rotating 180[degree symbol] in the catalytic cleft. Although PMM/PGM is well studied both structurally and kinetically, the mechanisms of its intramolecular and intermolecular communication are less well understood, especially in solution. Multiple solution NMR techniques are used in this dissertation's work to reveal information on PMM/PGM interactions at the atomic level. NMR-detected hydrogen exchange in combination with molecular dynamics and electrostatic calculations found phosphorylation of active Ser108 residue stabilizes PMM/PGM by attracting domains together. Responses of PMM/PGM to various phosphosugars were characterized by NMR-detected titrations. The large set of assigned peaks were analyzed by various types of principal component analysis (PCA) to derive binding isotherms, over-arching relationships among phosphosugar ligand binding reactions, and equilibrium shifts of PMM/PGM during its catalytic cycle. PCA was also found to be able to extract binding isotherms directly from non-interpreted 2D NMR spectra of complexes forming in solution. Procedures were identified that are reliable for obtaining the binding isotherms, regardless of the spectral peaks being in the fast, slow, or intermediate exchange regimes, or mixtures thereof. Applying PCA to time-domain NMR data also yields binding isotherms from titrations in fast or slow exchange. The algorithm readily extracts from an MRI movie its time courses, such as breathing and heart rate in chest imaging. To enable the community to exploit these new capabilities, we have developed the multi-platform software named TREND to track equilibrium and non-equilibrium population shifts among 2D data frames. The principal components obtained represent the main changes among the data frames. Besides binding isotherms and time courses, the main changes extracted by TREND can be any variety of population shifts. TREND can reconstruct the series of measurements from selected principal components. TREND supports multiple data formats, including raw NMR data, images, movies, lists, and spreadsheet files. The software can also be used for data clustering or noise filtering. Advisors/Committee Members: Van Doren, Steven R., 1963- (advisor), Beamer, Lesa J. (Lesa Jean) (advisor).

Subjects/Keywords: Pseudomonas aeruginosa infections; Nuclear magnetic resonance spectroscopy

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

APA (6th Edition):

Xu, J. (. s. (2016). Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis. (Thesis). University of Missouri – Columbia. Retrieved from https://doi.org/10.32469/10355/59793

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):

Xu, Jia (Research scientist). “Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis.” 2016. Thesis, University of Missouri – Columbia. Accessed April 15, 2021. https://doi.org/10.32469/10355/59793.

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

MLA Handbook (7th Edition):

Xu, Jia (Research scientist). “Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis.” 2016. Web. 15 Apr 2021.

Vancouver:

Xu J(s. Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis. [Internet] [Thesis]. University of Missouri – Columbia; 2016. [cited 2021 Apr 15]. Available from: https://doi.org/10.32469/10355/59793.

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

Council of Science Editors:

Xu J(s. Stability, states, and interactions of the enzyme PMM/PGM by NMR and multivariate analysis: Stability, states, and interactions of the enzyme phosphomannomutase/phosphoglucomutase by nuclear magnetic resonance and multivariate analysis. [Thesis]. University of Missouri – Columbia; 2016. Available from: https://doi.org/10.32469/10355/59793

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

.