Forces stabilizing proteins von Nick Pace, C., Scholtz, J. Martin, Grimsley, Gerald R.

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Toward a Molecular Understanding of Protein Solubility: Increased Negative Surface Charge Correlates with Increased Solubility von Kramer, Ryan M., Shende, Varad R., Motl, Nicole, Pace, C. Nick, Scholtz, J. Martin

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Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility von Pace, C. Nick, Grimsley, Gerald R., Scholtz, J. Martin

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Lessons in stability from thermophilic proteins von Razvi, Abbas, Scholtz, J. Martin

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A summary of the measured pK values of the ionizable groups in folded proteins von Grimsley, Gerald R., Scholtz, J. Martin, Pace, C. Nick

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Contribution of hydrogen bonds to protein stability von Pace, C. Nick, Fu, Hailong, Fryar, Katrina, Landua, John, Trevino, Saul R., Schell, David, Thurlkill, Richard L., Imura, Satoshi, Scholtz, J. Martin, Gajiwala, Ketan, Sevcik, Jozef, Urbanikova, Lubica, Myers, Jeffery K., Takano, Kazufumi, Hebert, Eric J., Shirley, Bret A., Grimsley, Gerald R.

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Contribution of Hydrophobic Interactions to Protein Stability von Pace, C. Nick, Fu, Hailong, Fryar, Katrina Lee, Landua, John, Trevino, Saul R., Shirley, Bret A., Hendricks, Marsha McNutt, Iimura, Satoshi, Gajiwala, Ketan, Scholtz, J. Martin, Grimsley, Gerald R.

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Interactions of Peptides with a Protein Pore von Movileanu, Liviu, Schmittschmitt, Jason P., Martin Scholtz, J., Bayley, Hagan

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Protein structure, stability and solubility in water and other solvents von Nick Pace, C., Treviño, Saul, Prabhakaran, Erode, Martin Scholtz, J.

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Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa von Trevino, Saul R., Scholtz, J. Martin, Pace, C. Nick

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pK values of the ionizable groups of proteins von Thurlkill, Richard L., Grimsley, Gerald R., Scholtz, J. Martin, Pace, C. Nick

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Increasing protein stability by improving beta-turns von Fu, Hailong, Grimsley, Gerald R., Razvi, Abbas, Scholtz, J. Martin, Pace, C. Nick

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The role of protein stability, solubility, and net charge in amyloid fibril formation von Schmittschmitt, Jason P., Scholtz, J. Martin

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Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence von Alston, Roy W., Lasagna, Mauricio, Grimsley, Gerald R., Scholtz, J. Martin, Reinhart, Gregory D., Pace, C. Nick

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A Thermodynamic Comparison of HPr Proteins from Extremophilic Organisms von Razvi, Abbas, Scholtz, J. Martin

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Measuring and Increasing Protein Solubility von Trevino, Saul R., Scholtz, J.Martin, Pace, C.Nick

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Increasing Protein Conformational Stability by Optimizing β-Turn Sequence von Trevino, Saul R., Schaefer, Stephanie, Scholtz, J. Martin, Pace, C. Nick

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Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa von Trefethen, Jared M., Pace, C. Nick, Scholtz, J. Martin, Brems, David N.

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The Contribution of Polar Group Burial to Protein Stability Is Strongly Context-dependent von Takano, Kazufumi, Scholtz, J.Martin, Sacchettini, James C., Pace, C.Nick

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Tryptophan Fluorescence Reveals the Presence of Long-Range Interactions in the Denatured State of Ribonuclease Sa von Alston, Roy W., Lasagna, Mauricio, Grimsley, Gerald R., Martin Scholtz, J., Reinhart, Gregory D., Nick Pace, C.

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