Publications

A full list of publications can be found on Google Scholar

Cellular sticking can strongly reduce complex binding by speeding dissociation

PMID:

[18] Davis, C.M.*; Gruebele, M.* “Cellular sticking can strongly reduce complex binding by speeding dissociation,” J. Phys. Chem. B 2021, accepted. DOI: 10.1021/acs.jpcb.1c00950

Cytoskeletal drugs modulate off-target protein folding landscapes inside cells

DOI: 10.1021/acs.biochem.0c00299

PMID: 32567840

[17] Davis, C.M.*; Gruebele, M.* “Cytoskeletal drugs modulate off-target protein folding landscapes inside cells,” Biochemistry 2020, 59 (28), 2650-2659. DOI: 10.1021/acs.biochem.0c00299

An in vitro mimic of in-cell solvation for protein folding studies

DOI: 10.1002/pro.3833

PMID: 31994240

[16] Davis, C.M.*; Deutsch, J.C.; Gruebele, M.* “An in vitro mimic of in-cell solvation for protein folding studies,” Protein Sci. 2020, 29 (4), 1046-1054.

Quantifying protein dynamics and stability in a living organism

DOI: 10.1038/s41467-019-09088-y

PMID: 30862837

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

Cell volume controls protein stability and compactness of the unfolded state

DOI: 10.1021/acs.jpcb.8b08216

PMID: 30289261

[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.

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

DOI: 10.1039/C8SC03786H

PMID: 30647892

[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.

Soluble zwitterionic poly(sulfobetaine) destabilizes proteins

DOI: 10.1021/acs.biomac.8b01120

PMID: 30064224

[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.

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

DOI: 10.1002/cphc.201800534

PMID: 29877016

[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.

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

DOI: 10.1021/acs.biochem.8b00141

PMID: 29546761

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

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

DOI: 10.1016/j.bbamem.2017.12.019

PMID: 29291379

[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.

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

DOI: 10.1016/j.sbi.2017.09.003

PMID: 29035742

[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.

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

DOI: 10.1002/1873-3468.12836

PMID: 28881468

[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.

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

DOI: 10.1016/j.saa.2017.01.069

PMID: 28189834

[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.

The role of electrostatic interactions in folding of β-proteins

DOI: 10.1021/jacs.5b13201

PMID: 26750867

[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.

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

DOI: 10.1021/acs.biochem.5b00037

PMID: 25706439

[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.

WW Domain folding complexity revealed by infrared spectroscopy

DOI: 10.1021/bi500556h

PMID: 25121968

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

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

DOI: 10.1021/ja409608r

PMID: 24320936

[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.

Raising the speed limit for β-hairpin formation

DOI: 10.1021/ja3046734

PMID: 22873643

[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.