M
Michael J. Grey
Researcher at Harvard University
Publications - 25
Citations - 1051
Michael J. Grey is an academic researcher from Harvard University. The author has contributed to research in topics: Biology & Unfolded protein response. The author has an hindex of 11, co-authored 18 publications receiving 953 citations. Previous affiliations of Michael J. Grey include National Institutes of Health & University of Connecticut.
Papers
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Journal ArticleDOI
Structural Evidence for Loose Linkage between Ligand Binding and Kinase Activation in the Epidermal Growth Factor Receptor
Chafen Lu,Li-Zhi Mi,Michael J. Grey,Jieqing Zhu,Elizabeth R. Graef,Shigeyuki Yokoyama,Timothy A. Springer +6 more
TL;DR: Results suggest that linkage between ligand-induced dimerization and tyrosine kinase activation is much looser than was previously envisioned.
Journal ArticleDOI
Disulfide bond isomerization in basic pancreatic trypsin inhibitor: multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling.
TL;DR: Conformational changes occurring on the microsecond-millisecond time scale in basic pancreatic trypsin inhibitor (BPTI) are investigated using nuclear magnetic resonance spectroscopy to characterize the kinetics and mechanism of chemical exchange line broadening of the backbone of Cys 14, Lys 15, Cys 38, and Arg 39 in BPTI.
Journal ArticleDOI
Microsecond timescale backbone conformational dynamics in ubiquitin studied with NMR R1ρ relaxation experiments
TL;DR: NMR spin relaxation experiments are used to characterize the dynamics of the backbone of ubiquitin and chemical exchange processes affecting residues Ile 23, Asn 25, Thr 55, and Val 70 are identified using 1H‐15N multiple quantum relaxation experiments.
Journal ArticleDOI
Functional and Structural Stability of the Epidermal Growth Factor Receptor in Detergent Micelles and Phospholipid Nanodiscs
TL;DR: Rec recombinant EGFR constructs containing the extracellular, transmembrane, juxtamembrane and kinase domains are overexpressed and purified from human embryonic kidney 293 cell cultures and the oligomerization state, overall structure, and functional stability of the purified EGF-bound receptor are characterized in detergent micelles and phospholipid bilayers.
Book ChapterDOI
Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems.
TL;DR: This chapter surveys the theoretical bases for TROSY in spin systems subject to chemical exchange linebroadening, the experimental methods that have been developed to quantitatively characterize chemical exchange in large proteins, and the emerging applications to triose phosphate isomerase, hemoglobin, and malate synthase G.