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You searched for +publisher:"University of North Carolina" +contributor:("Wang, Yaqiang"). One record found.

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University of North Carolina

1. Wang, Yaqiang. Macromolecular crowding and protein chemistry: views from inside and outside cells.

Degree: Chemistry, 2012, University of North Carolina

The cytoplasm is crowded, and the concentration of macromolecules can reach ~ 300 g/L, an environment vastly different from the dilute, idealized conditions usually used in biophysical studies. Macromolecular crowding arise from two phenomena, excluded volume and nonspecific chemical interactions, until recently, only excluded volume effect has been considered. Theory predicts that this macromolecular crowding can have large effects. Most proteins, however, are studied outside cells in dilute solution with macromolecule concentrations of 10 g/L or less. In-cell NMR provides a means to assess protein biophysics at atomic resolution in living cells, but it remains in its infancy, and several potential challenges need to be addressed. One challenge is the inability to observe 15N-1H NMR spectra from many small globular proteins. 19F NMR was used to expand the application of in-cell NMR. This work suggests that high viscosity and weak interactions in the cytoplasm can make routine 15N enrichment a poor choice for in-cell NMR studies of globular proteins in Escherichia coli. To gain insight into this problem, I turned to in vitro experiments where conditions can be controlled with precision. Using both synthetic polymers and globular proteins, I studied the effects of crowding on the diffusion of the test protein, chymotrypsin inhibitor 2. The results not only pinpoint the source of the problem - nonspecific chemical interactions - but also suggest that proteins are more suitable mimics of the intracellular environment. I also measured the stability of ubiquitin in solutions crowded with synthetic polymers or globular proteins to further elucidate the role of nonspecific chemical interactions under crowded conditions. The increased stability observed in synthetic crowders was consistent with a dominant entropic role for excluded volume, but the effect of protein crowders depended on charge. Protein-induced crowding increased stability when the sign of the net charge of the crowder was the same as that of ubiquitin, but decreased stability when the proteins were oppositely charged. The results indicate that synthetic polymers do not provide physiologically relevant insights and that the overall effect of macromolecular crowding depends on the winner of the near stalemate between excluded volume and nonspecific interactions. Advisors/Committee Members: Wang, Yaqiang, Pielak, Gary J..

Subjects/Keywords: College of Arts and Sciences; Department of Chemistry

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

APA (6th Edition):

Wang, Y. (2012). Macromolecular crowding and protein chemistry: views from inside and outside cells. (Thesis). University of North Carolina. Retrieved from https://cdr.lib.unc.edu/record/uuid:d9c6b6bc-4e68-4734-986c-9900013622e5

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):

Wang, Yaqiang. “Macromolecular crowding and protein chemistry: views from inside and outside cells.” 2012. Thesis, University of North Carolina. Accessed January 24, 2021. https://cdr.lib.unc.edu/record/uuid:d9c6b6bc-4e68-4734-986c-9900013622e5.

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

MLA Handbook (7th Edition):

Wang, Yaqiang. “Macromolecular crowding and protein chemistry: views from inside and outside cells.” 2012. Web. 24 Jan 2021.

Vancouver:

Wang Y. Macromolecular crowding and protein chemistry: views from inside and outside cells. [Internet] [Thesis]. University of North Carolina; 2012. [cited 2021 Jan 24]. Available from: https://cdr.lib.unc.edu/record/uuid:d9c6b6bc-4e68-4734-986c-9900013622e5.

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

Council of Science Editors:

Wang Y. Macromolecular crowding and protein chemistry: views from inside and outside cells. [Thesis]. University of North Carolina; 2012. Available from: https://cdr.lib.unc.edu/record/uuid:d9c6b6bc-4e68-4734-986c-9900013622e5

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

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