J Martin Scholtz
J Martin Scholtz
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Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
JK Myers, C Nick Pace, J Martin Scholtz
Protein Science 4 (10), 2138-2148, 1995
A helix propensity scale based on experimental studies of peptides and proteins
CN Pace, JM Scholtz
Biophysical journal 75 (1), 422-427, 1998
Measuring the conformational stability of a protein
CN Pace, JM Scholtz
Protein structure: A practical approach 2, 299-321, 1997
The mechanism of alpha-helix formation by peptides
JM Scholtz, RL Baldwin
Annual review of biophysics and biomolecular structure 21 (1), 95-118, 1992
Parameters of helix–coil transition theory for alanine‐based peptides of varying chain lengths in water
JM Scholtz, H Qian, EJ York, JM Stewart, RL Baldwin
Biopolymers: Original Research on Biomolecules 31 (13), 1463-1470, 1991
A summary of the measured pK values of the ionizable groups in folded proteins
GR Grimsley, JM Scholtz, CN Pace
Protein Science 18 (1), 247-251, 2009
Protein ionizable groups: pK values and their contribution to protein stability and solubility
CN Pace, GR Grimsley, JM Scholtz
Journal of Biological Chemistry 284 (20), 13285-13289, 2009
Protein structure, stability and solubility in water and other solvents
C Nick Pace, S Trevino, E Prabhakaran, J Martin Scholtz
Philosophical Transactions of the Royal Society of London. Series B …, 2004
Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water.
JM Scholtz, S Marqusee, RL Baldwin, EJ York, JM Stewart, M Santoro, ...
Proceedings of the National Academy of Sciences 88 (7), 2854-2858, 1991
Lessons in stability from thermophilic proteins
A Razvi, JM Scholtz
Protein Science 15 (7), 1569-1578, 2006
The energetics of ion-pair and hydrogen-bonding interactions in a helical peptide
JM Scholtz, H Qian, VH Robbins, RL Baldwin
Biochemistry 32 (37), 9668-9676, 1993
Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility
RM Kramer, VR Shende, N Motl, CN Pace, JM Scholtz
Biophysical journal 102 (8), 1907-1915, 2012
pK values of the ionizable groups of proteins
RL Thurlkill, GR Grimsley, JM Scholtz, CN Pace
Protein science 15 (5), 1214-1218, 2006
Contribution of hydrogen bonds to protein stability
CN Pace, H Fu, K Lee Fryar, J Landua, SR Trevino, D Schell, RL Thurlkill, ...
Protein Science 23 (5), 652-661, 2014
Contribution of hydrophobic interactions to protein stability
CN Pace, H Fu, KL Fryar, J Landua, SR Trevino, BA Shirley, ...
Journal of molecular biology 408 (3), 514-528, 2011
Forces stabilizing proteins
CN Pace, JM Scholtz, GR Grimsley
FEBS letters 588 (14), 2177-2184, 2014
Protein structure: a practical approach
CN Pace, JM Scholtz
Measuring the conformational stability of a protein 1, 383, 1997
Osteopontin is a ligand for the α4β1 integrin
KJ Bayless, GA Meininger, JM Scholtz, GE Davis
Journal of cell science 111 (9), 1165-1174, 1998
Interactions of peptides with a protein pore
L Movileanu, JP Schmittschmitt, JM Scholtz, H Bayley
Biophysical journal 89 (2), 1030-1045, 2005
Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa
SR Trevino, JM Scholtz, CN Pace
Journal of molecular biology 366 (2), 449-460, 2007
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