Alan R. Davidson

Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge charge interactions (2007)

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...

Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain (2006)

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...

Protein folding: Defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins (2005)

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...

Residues participating in the protein folding nucleus do not exhibit preferential evolutionary conservation (2002)

Stefan M. Larson, Ingo Ruczinski, Alan R. Davidson, David Baker, Kevin W. Plaxco, Howard Hughes Medical

*Corresponding authors Abbreviations used: ACBP, acylcarrier binding protein; AcP, acylphosphatase; ADA2h, the activation domain of human carboxypeptidase; CI2, chymotrypsin inhibitor 2; FKBP, FK506...

A simple in vivo assay for increased protein solubility (1999)

Downloaded From, Karen L. Maxwell, Anthony K. Mittermaier, Alan R. Davidson

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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...

The Biologically Relevant Targets and Binding Affinity Requirements for the Function of the Yeast Actin-Binding Protein 1 Src-Homology 3 Domain Vary With Genetic Context

Haynes, Jennifer, Garcia, Bianca, Stollar, Elliott J., Rath, Arianna, Andrews, Brenda J., Davidson, Alan R.

Many protein–protein interaction domains bind to multiple targets. However, little is known about how the interactions of a single domain with many proteins are controlled and modulated under...

Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain

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...

Protein folding: Defining a “standard” set of experimental conditions and a preliminary kinetic data set of two-state proteins

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...

A folding space odyssey

Davidson, Alan R.

Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge–charge interactions

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...

Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding

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...

The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

Pell, Lisa G., Kanelis, Voula, Donaldson, Logan W., Lynne Howell, P., Davidson, Alan R.

Most bacteriophages possess long tails, which serve as the conduit for genome delivery. We report the solution structure of the N-terminal domain of gpV, the protein comprising the major portion of...