Schweiker, Katrina L., Zarrine-Afsar, Arash, Davidson, Alan R., Makhatadze, George I.
Computational design of surface charge–charge interactions has been demonstrated to be an effective way to increase both the thermostability and the stability of proteins. To test the robustness of...
Zarrine-Afsar, Arash, Mittermaier, Anthony, Kay, Lewis E., Davidson, Alan R.
Guanidinium hydrochloride (GuHCl) at low concentrations significantly stabilizes the Fyn SH3 domain. In this work, we have demonstrated that this stabilizing effect is manifested through a dramatic...
Maxwell, Karen L., Wildes, David, Zarrine-Afsar, Arash, De Los Rios, Miguel A., Brown, Andrew G., Friel, Claire T., ...
Recent years have seen the publication of both empirical and theoretical relationships predicting the rates with which proteins fold. Our ability to test and refine these relationships has been...
Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation
Di Nardo, Ariel A., Korzhnev, Dmitry M., Stogios, Peter J., Zarrine-Afsar, Arash, Kay, Lewis E., Davidson, Alan R.
Through a mutagenic investigation of Gly-48, a highly conserved position in the Src homology 3 domain, we have discovered a series of amino acid substitutions that are highly destabilizing, yet...
Dramatic acceleration of protein folding by stabilization of a nonnative backbone conformation
Di Nardo, Ariel A., Korzhnev, Dmitry M., Stogios, Peter J., Zarrine-Afsar, Arash, Kay, Lewis E., Davidson, Alan R.
Through a mutagenic investigation of Gly-48, a highly conserved position in the Src homology 3 domain, we have discovered a series of amino acid substitutions that are highly destabilizing, yet...
Murphy, James M., Korzhnev, Dmitry M., Ceccarelli, Derek F., Briant, Douglas J., Zarrine-Afsar, Arash, Sicheri, Frank, ...
The Par-1/MARK protein kinases play a pivotal role in establishing cellular polarity. This family of kinases contains a unique domain architecture, in which a ubiquitin-associated (UBA) domain is...
Zarrine-Afsar, Arash, Mittermaier, Anthony, Kay, Lewis E., Davidson, Alan R.
Guanidinium hydrochloride (GuHCl) at low concentrations significantly stabilizes the Fyn SH3 domain. In this work, we have demonstrated that this stabilizing effect is manifested through a dramatic...
Φ-Value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy
Neudecker, Philipp, Zarrine-Afsar, Arash, Davidson, Alan R., Kay, Lewis E.
Experimental studies of protein folding frequently are consistent with two-state folding kinetics. However, recent NMR relaxation dispersion studies of several fast-folding mutants of the Fyn Src...
Maxwell, Karen L., Wildes, David, Zarrine-Afsar, Arash, De Los Rios, Miguel A., Brown, Andrew G., Friel, Claire T., ...
Recent years have seen the publication of both empirical and theoretical relationships predicting the rates with which proteins fold. Our ability to test and refine these relationships has been...
Schweiker, Katrina L., Zarrine-Afsar, Arash, Davidson, Alan R., Makhatadze, George I.
Computational design of surface charge–charge interactions has been demonstrated to be an effective way to increase both the thermostability and the stability of proteins. To test the robustness of...
Zarrine-Afsar, Arash, Wallin, Stefan, Neculai, A. Mirela, Neudecker, Philipp, Howell, P. Lynne, Davidson, Alan R., ...
Many experimental and theoretical studies have suggested a significant role for nonnative interactions in protein folding pathways, but the energetic contributions of these interactions are not well...