Publications

A full list of publications can be found on Google Scholar

[15] Feng, R.; Gruebele, M.*; Davis, C.M.*“Quantifying protein dynamics and stability in a living organism,” Nat. Commun. 2019, 10, 1179.

Quantifying protein dynamics and stability in a living organism

[14] Wang, Y.†; Sukenik, S.*†; Davis, C.M.; Gruebele, M.* “Cell volume controls protein stability and compactness of the unfolded state,” J. Phys. Chem. B 2018, 122 (49), 11762-11770.

Cell volume controls protein stability and compactness of the unfolded state

[13] Davis, C.M.†; Polzi, L.Z.†; Gruebele, M.; Amadei, A.; Dyer, R.B.*; Daidone, I.* “A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy,” Chem. Sci. 2018, 9, 9002-9011.

A quantitative connection of experimental and simulated folding landscapes by vibrational spectroscopy

[12] Kisley, L.; Serrano, K.M.; Davis, C.M.; Guin, D.; Murphy, E.; Gruebele, M.*; Leckband, D.E.* “Soluble zwitterionic poly(sulfobetaine) destabilizes proteins,” Biomacromolecules 2018, 19 (9), 3894-3901. 

Soluble zwitterionic poly(sulfobetaine) destabilizes proteins

[11] Davis, C.M.; Gruebele, M. “Non-steric interactions predict the trend and steric interactions the offset of protein stability in cells,” ChemPhysChem 2018, 19 (18), 2290-2294.

Non-steric interactions predict the trend and steric interactions the offset of protein stability in cells

[10] Davis, C.M.*; Gruebele, M.* “Labeling for quantitative comparison of imaging measurements in vitro and in cells,” Biochemistry 2018, 57 (13), 1929-1938.

Labeling for quantitative comparison of imaging measurements in vitro and in cells

[9] Reid, K.; Davis, C.M.; Dyer, R.B.; Kindt, J.T. “Binding, folding, and insertion of a β-hairpin peptide at a lipid bilayer surface: influence of electrostatics and lipid tail packing,” Biochim. Biophys. Acta Biomembr. 2018, 1860 (3), 792-800.

Binding, folding, and insertion of a β-hairpin peptide at a lipid bilayer surface: influence of electrostatics and lipid tail packing

[8] Davis, C.M.; Gruebele, M.; Sukenik, S. “How does solvation in the cell affect protein folding and binding?” Curr. Opin. Struct. Biol. 2018, 48, 23-29.

How does solvation in the cell affect protein folding and binding?

[7] Polzi, L.Z.; Davis, C.M.; Gruebele, M.; Dyer, R.B.; Amadei, A.; Daidone, I. “Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation,” FEBS Lett. 2017, 591 (20), 3265-3275.

Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation

[6] Davis, C.M.; Reddish, M.J.; Dyer, R.B. “Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics,” Spectrochim. Acta A 2017, 178, 185-191.

Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics

[5] Davis, C.M.; Dyer, R.B. “The role of electrostatic interactions in folding of β-proteins,” J. Am. Chem. Soc. 2016, 138 (4), 1456-1464.

The role of electrostatic interactions in folding of β-proteins

[4] Davis, C.M.; Cooper, A.K.; Dyer, R.B. “Fast helix formation in the B domain of protein A revealed by site-specific infrared probes,” Biochemistry 2015, 54 (9), 1758-1766.

Fast helix formation in the B domain of protein A revealed by site-specific infrared probes

[3] Davis, C.M.; Dyer, R. B. “WW Domain folding complexity revealed by infrared spectroscopy,” Biochemistry 2014, 53 (34), 5476-5484.

WW Domain folding complexity revealed by infrared spectroscopy

[2] Davis, C.M.; Dyer, R. B. “Dynamics of an ultrafast folding subdomain in the context of a larger protein fold,” J. Am. Chem. Soc. 2013, 135 (51), 19260-19267.

Dynamics of an ultrafast folding subdomain in the context of a larger protein fold

[1] Davis, C.M.; Xiao, S.; Raleigh, D.P.*; Dyer, R. B.* “Raising the speed limit for β-hairpin formation,” J. Am. Chem. Soc. 2012, 134 (35), 14476-14482.

Raising the speed limit for β-hairpin formation

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Davis Lab, Yale University

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