P. B. Lawrence

Criteria for Selecting PEGylation Sites on Proteins for Higher Thermodynamic Stability

P. B. Lawrence, 2016 .

PEG-based Changes to β -sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location

J. Price, Brown, P. Nathaniel, 2019 .

Polyethylene Glycol Based Changes to β-Sheet Protein Conformational and Proteolytic Stability Depend on Conjugation Strategy and Location.

Q. Xiao, J. Price, P. B. Lawrence, 2017, Bioconjugate chemistry.

Conjugation Strategy Strongly Impacts the Conformational Stability of a PEG-Protein Conjugate.

Minnie I Langlois, J. Price, B. K. Pandey, 2016, ACS Chemical Biology.

How PEGylation influences protein conformational stability.

J. Price, P. B. Lawrence, J. L. Price, 2016, Current opinion in chemical biology.

Impact of site-specific PEGylation on the conformational stability and folding rate of the Pin WW domain depends strongly on PEG oligomer length.

Maxim B. Prigozhin, S. S. Matthews, J. Price, 2013, Bioconjugate chemistry.

Criteria for selecting PEGylation sites on proteins for higher thermodynamic and proteolytic stability.

Maxim B. Prigozhin, Minnie I Langlois, Y. Levy, 2014, Journal of the American Chemical Society.