Natalie K. Goto, Ph.D.
Affiliations: | 2001 | University of Toronto, Toronto, ON, Canada |
Area:
Development and Application of NMR Methods for The Study of Protein Structure and DynamicsGoogle:
"Natalie Goto"Mean distance: 10.32
Parents
Sign in to add mentor| Lewis E. Kay | grad student | 2001 | University of Toronto | |
| (The development and application of methods for the study of multi-domain protein structure by solution NMR.) | ||||
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Publications
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| Sarkar SK, Foo ACY, Matyas A, et al. (2020) A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles. The Journal of Biological Chemistry |
| Damry AM, Mayer MM, Broom A, et al. (2019) Origin of conformational dynamics in a globular protein. Communications Biology. 2: 433 |
| Damry AM, Mayer MM, Broom A, et al. (2019) Origin of conformational dynamics in a globular protein. Communications Biology. 2: 433 |
| Ayed SH, Cloutier AD, McLeod LJ, et al. (2017) Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity. The Journal of Biological Chemistry |
| Davey JA, Damry AM, Goto NK, et al. (2017) Rational design of proteins that exchange on functional timescales. Nature Chemical Biology |
| Qureshi T, Goto NK. (2016) Impact of Differential Detergent Interactions on Transmembrane Helix Dimerization Affinities. Acs Omega. 1: 277-285 |
| Davey JA, Damry AM, Euler CK, et al. (2015) Prediction of Stable Globular Proteins Using Negative Design with Non-native Backbone Ensembles. Structure (London, England : 1993). 23: 2011-21 |
| Foo AC, Harvey BG, Metz JJ, et al. (2015) Influence of hydrophobic mismatch on the catalytic activity of Escherichia coli GlpG rhomboid protease. Protein Science : a Publication of the Protein Society. 24: 464-73 |
| Ghasriani H, Kwok JK, Sherratt AR, et al. (2014) Micelle-catalyzed domain swapping in the GlpG rhomboid protease cytoplasmic domain. Biochemistry. 53: 5907-15 |
| Goto NK. (2014) The importance of intrinsic order in a disordered protein ligand. Biophysical Journal. 106: 1557-8 |