Lessons in stability from thermophilic proteins

Por Razvi, Abbas, Scholtz, J. Martin
Publicado em 2006

The role of protein stability, solubility, and net charge in amyloid fibril formation

Por Schmittschmitt, Jason P., Scholtz, J. Martin
Publicado em 2003

Osmolyte effects on helix formation in peptides and the stability of coiled-coils

Por Celinski, Scott A., Scholtz, J. Martin
Publicado em 2002

A direct comparison of helix propensity in proteins and peptides

Por Myers, Jeffrey K., Pace, C. Nick, Scholtz, J. Martin
Publicado em 1997

Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility

Por Pace, C. Nick, Grimsley, Gerald R., Scholtz, J. Martin
Publicado em 2009

A summary of the measured pK values of the ionizable groups in folded proteins

Por Grimsley, Gerald R, Scholtz, J Martin, Pace, C Nick
Publicado em 2009

Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa

Por Trevino, Saul R., Scholtz, J. Martin, Pace, C. Nick
Publicado em 2006

Forces Stabilizing Proteins

Por Pace, C. Nick, Scholtz, J. Martin, Grimsley, Gerald R.
Publicado em 2014

Interactions of Peptides with a Protein Pore

Por Movileanu, Liviu, Schmittschmitt, Jason P., Scholtz, J. Martin, Bayley, Hagan
Publicado em 2005

Protein structure, stability and solubility in water and other solvents.

Por Pace, C Nick, Treviño, Saul, Prabhakaran, Erode, Scholtz, J Martin
Publicado em 2004

Increasing protein stability: Importance of ΔC(p) and the denatured state

Por Fu, Hailong, Grimsley, Gerald, Scholtz, J Martin, Pace, C Nick
Publicado em 2010

Purification and Biochemical Characterization of the Lambda Holin

Por Smith, David L., Struck, Douglas K., Scholtz, J. Martin, Young, Ry
Publicado em 1998

Increasing Protein Conformational Stability by Optimizing β-turn Sequence

Por Trevino, Saul R., Schaefer, Stephanie, Scholtz, J. Martin, Pace, C. Nick
Publicado em 2007

An engineered leucine zipper a position mutant with an unusual three-state unfolding pathway

Por Zhu, Hai, Celinski, Scott A., Scholtz, J. Martin, Hu, James C.
Publicado em 2001

pK values of the ionizable groups of proteins

Por Thurlkill, Richard L., Grimsley, Gerald R., Scholtz, J. Martin, Pace, C. Nick
Publicado em 2006

Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa

Por Trefethen, Jared M., Pace, C. Nick, Scholtz, J. Martin, Brems, David N.
Publicado em 2005

INCREASING PROTEIN STABILITY BY IMPROVING BETA-TURNS

Por Fu, Hailong, Grimsley, Gerald R., Razvi, Abbas, Scholtz, J. Martin, Pace, C. Nick
Publicado em 2009

Toward a Molecular Understanding of Protein Solubility: Increased Negative Surface Charge Correlates with Increased Solubility

Por Kramer, Ryan M., Shende, Varad R., Motl, Nicole, Pace, C. Nick, Scholtz, J. Martin
Publicado em 2012

Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence

Por Alston, Roy W., Lasagna, Mauricio, Grimsley, Gerald R., Scholtz, J. Martin, Reinhart, Gregory D., Pace, C. Nick
Publicado em 2008

Tryptophan Fluorescence Reveals the Presence of Long-Range Interactions in the Denatured State of Ribonuclease Sa

Por Alston, Roy W., Lasagna, Mauricio, Grimsley, Gerald R., Scholtz, J. Martin, Reinhart, Gregory D., Pace, C. Nick
Publicado em 2008