CARLOS PACE

Summary

Affiliation: Texas A and M University
Country: USA

Publications

  1. pmc Forces stabilizing proteins
    C Nick Pace
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, TX 77843, United States Department of Molecular and Cellular Medicine, Texas A and M University Health Science Center, College Station, TX 77843, United States Electronic address
    FEBS Lett 588:2177-84. 2014
  2. pmc Contribution of hydrophobic interactions to protein stability
    C Nick Pace
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, TX 77843, USA
    J Mol Biol 408:514-28. 2011
  3. pmc Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins
    C Nick Pace
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas 77843, USA
    Protein Sci 19:929-43. 2010
  4. pmc Protein ionizable groups: pK values and their contribution to protein stability and solubility
    C Nick Pace
    Department of Molecular and Cellular Medicine, Texas A and M Health Science Center, College Station, Texas 77843, USA
    J Biol Chem 284:13285-9. 2009
  5. pmc Heat capacity change for ribonuclease A folding
    C N Pace
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station 77843 1114, USA
    Protein Sci 8:1500-4. 1999
  6. pmc Protein structure, stability and solubility in water and other solvents
    C Nick Pace
    Department of Medical Biochemistry and Genetics, Center for Advanced Biomolecular Research, Texas A and M University, College Station, TX 77843, USA
    Philos Trans R Soc Lond B Biol Sci 359:1225-34; discussion 1234-5. 2004
  7. ncbi request reprint Polar group burial contributes more to protein stability than nonpolar group burial
    C N Pace
    Department of Medical Biochemistry and Genetics and Biochemistry and Biophysics and Center for Advanced Biomolecular Research, Texas A and M University, College Station, Texas 77843 1114, USA
    Biochemistry 40:310-3. 2001
  8. ncbi request reprint Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1
    C Nick Pace
    Department of Medical Biochemistry and Genetics and Center for Advanced Biomolecular Research, Texas A and M University, College Station, TX 77843 1114, USA
    Biophys Chem 101:211-9. 2002
  9. pmc Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    C N Pace
    Department of Medical Biochemistry and Genetics, Center for Macromolecular Design, Texas A and M University, College Station 77843 1114, USA
    Protein Sci 9:1395-8. 2000
  10. ncbi request reprint Tyrosine hydrogen bonds make a large contribution to protein stability
    C N Pace
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station, 77843 1114, USA
    J Mol Biol 312:393-404. 2001

Research Grants

  1. CONFORMATIONAL STABILITY OF GLOBULAR PROTEINS
    CARLOS PACE; Fiscal Year: 2006

Collaborators

  • JOHN M SCHOLTZ
  • J Sevcik
  • G I Makhatadze
  • J C Sacchettini
  • Jerry Tsai
  • John A McLean
  • Marta Bruix
  • Gerald R Grimsley
  • Saul R Trevino
  • Richard L Thurlkill
  • Hailong Fu
  • C Nick Pace
  • Roy W Alston
  • Beatrice M P Huyghues-Despointes
  • David Schell
  • Mauricio Lasagna
  • Gregory D Reinhart
  • Jared M Trefethen
  • Kevin L Shaw
  • Stephanie Newsom
  • Jan M Antosiewicz
  • Douglas V Laurents
  • James M Briggs
  • Kazufumi Takano
  • Gerald Grimsley
  • Abbas Razvi
  • Stephanie Schaefer
  • Alexander A Makarov
  • Vladimir A Mitkevich
  • David N Brems
  • Kuppan Gokulan
  • Lubica Urbanikova
  • Manuel Rico
  • Michael D Daily
  • Saul Trevino

Detail Information

Publications28

  1. pmc Forces stabilizing proteins
    C Nick Pace
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, TX 77843, United States Department of Molecular and Cellular Medicine, Texas A and M University Health Science Center, College Station, TX 77843, United States Electronic address
    FEBS Lett 588:2177-84. 2014
    ..6) Polar group burial can make a favorable contribution to protein stability even if the polar group is not hydrogen bonded. (7) Hydrophobic interactions and hydrogen bonds both make large contributions to protein stability...
  2. pmc Contribution of hydrophobic interactions to protein stability
    C Nick Pace
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, TX 77843, USA
    J Mol Biol 408:514-28. 2011
    ..6) Conformational entropy contributes about 2.4 kcal/mol per residue to protein instability. The globular conformation of proteins is stabilized predominantly by hydrophobic interactions...
  3. pmc Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins
    C Nick Pace
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas 77843, USA
    Protein Sci 19:929-43. 2010
    ..In all cases considered, including staph nuclease, the extent of unfolding by urea can be accounted for using the data and approach developed in the laboratory of Wayne Bolen (Auton et al., Proc Natl Acad Sci 2007; 104:15317-15323)...
  4. pmc Protein ionizable groups: pK values and their contribution to protein stability and solubility
    C Nick Pace
    Department of Molecular and Cellular Medicine, Texas A and M Health Science Center, College Station, Texas 77843, USA
    J Biol Chem 284:13285-9. 2009
    ..We review what has been learned about pK values of ionizable groups in proteins from experimental studies and discuss the important contributions they make to protein stability and solubility...
  5. pmc Heat capacity change for ribonuclease A folding
    C N Pace
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station 77843 1114, USA
    Protein Sci 8:1500-4. 1999
    ..08 kcal mol(-1) K(-1). Estimates of the conformational stability of ribonuclease A based on these results from thermal unfolding are in good agreement with estimates from urea unfolding analyzed using the linear extrapolation method...
  6. pmc Protein structure, stability and solubility in water and other solvents
    C Nick Pace
    Department of Medical Biochemistry and Genetics, Center for Advanced Biomolecular Research, Texas A and M University, College Station, TX 77843, USA
    Philos Trans R Soc Lond B Biol Sci 359:1225-34; discussion 1234-5. 2004
    ..For these and other reasons it seems unlikely that the life we know could exist in any solvent system other than water...
  7. ncbi request reprint Polar group burial contributes more to protein stability than nonpolar group burial
    C N Pace
    Department of Medical Biochemistry and Genetics and Biochemistry and Biophysics and Center for Advanced Biomolecular Research, Texas A and M University, College Station, Texas 77843 1114, USA
    Biochemistry 40:310-3. 2001
    ..This suggests that the hydrogen bonding and van der Waals interactions of peptide groups in the tightly packed interior of folded protein are more favorable than similar interactions with water in the unfolded protein...
  8. ncbi request reprint Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1
    C Nick Pace
    Department of Medical Biochemistry and Genetics and Center for Advanced Biomolecular Research, Texas A and M University, College Station, TX 77843 1114, USA
    Biophys Chem 101:211-9. 2002
    ..However, pK values can be shifted by several pK units by the Born self energy associated with burying ionizable groups and by favorable intramolecular hydrogen bonding...
  9. pmc Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    C N Pace
    Department of Medical Biochemistry and Genetics, Center for Macromolecular Design, Texas A and M University, College Station 77843 1114, USA
    Protein Sci 9:1395-8. 2000
    ..Further support is provided by studies of the ionic strength dependence of the stability of charge-reversal mutants of ribonuclease Sa. These results may have important implications for the mechanism of protein folding...
  10. ncbi request reprint Tyrosine hydrogen bonds make a large contribution to protein stability
    C N Pace
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station, 77843 1114, USA
    J Mol Biol 312:393-404. 2001
    ....
  11. ncbi request reprint Linear extrapolation method of analyzing solvent denaturation curves
    C N Pace
    Departments of Medical Biochemistry and Genetics, Biochemistry and Biophysics, and Center for Macromolecular Design, Texas A and M University, College Station, Texas 77843 1114, USA
    Proteins . 2000
    ..In this article, we trace the history of the linear extrapolation method, review how the method is used to measure protein stability, and then discuss some of the other important uses...
  12. ncbi request reprint Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins
    Richard L Thurlkill
    Department of Molecular and Cellular Medicine, Texas A and M University System Health Science Center, College Station, TX 77843, USA
    J Mol Biol 362:594-604. 2006
    ....
  13. pmc Increasing protein stability by improving beta-turns
    Hailong Fu
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas, USA
    Proteins 77:491-8. 2009
    ..Improving beta-turns by substituting Pro residues is a generally useful way of increasing protein stability...
  14. pmc Increasing protein stability: importance of DeltaC(p) and the denatured state
    Hailong Fu
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas 77843, USA
    Protein Sci 19:1044-52. 2010
    ..Finally, the thermodynamics of folding of these stabilized variants of RNase Sa are compared with those observed for proteins from thermophiles...
  15. ncbi request reprint pK values of histidine residues in ribonuclease Sa: effect of salt and net charge
    Beatrice M P Huyghues-Despointes
    Department of Medical Biochemistry and Genetics, Center for Advanced Biomolecular Research, Texas A and M University, College Station, TX 77843 1114, USA
    J Mol Biol 325:1093-105. 2003
    ..Structure-based pK calculations capture the salt-dependence relatively well but are unable to predict absolute histidine pK values...
  16. pmc A summary of the measured pK values of the ionizable groups in folded proteins
    Gerald R Grimsley
    Department of Molecular and Cellular Medicine, Texas A and M University System Health Science Center, College Station, Texas 77843, USA
    Protein Sci 18:247-51. 2009
    ..3 +/- 1.2 (20); Lys 10.5 +/- 1.1 (35); C-terminus 3.3 +/- 0.8 (22) and N-terminus 7.7 +/- 0.5 (16). We compare these results with the measured pK values of these groups in alanine pentapeptides, and comment on our overall findings...
  17. doi request reprint Spectrophotometric determination of protein concentration
    Gerald R Grimsley
    The Texas A and M University System Health Science Center, College Station, Texas, USA
    Curr Protoc Protein Sci . 2004
    ..A sensitive method is provided for measuring the concentration of proteins that contain few if any tryptophan or tyrosine residues, and a simple method is provided for estimating total protein concentration in crude extracts...
  18. doi request reprint Measuring and increasing protein solubility
    Saul R Trevino
    Department of Molecular and Cellular Medicine, Texas A and M University System Health Science Center, College Station, Texas 77843 1114, USA
    J Pharm Sci 97:4155-66. 2008
    ....
  19. ncbi request reprint Charge-charge interactions are key determinants of the pK values of ionizable groups in ribonuclease Sa (pI=3.5) and a basic variant (pI=10.2)
    Douglas V Laurents
    Department of Medical Biochemistry and Genetics, Department of Biochemistry and Biophysics, Center for Advanced Biomolecular Research, Texas A and M University, College Station, TX 77843 1114, USA
    J Mol Biol 325:1077-92. 2003
    ....
  20. pmc Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa
    Saul R Trevino
    Department of Molecular and Cellular Medicine, Texas A and M University, College Station, TX 77843, USA
    J Mol Biol 366:449-60. 2007
    ..Therefore, to increase protein solubility, asparagine, glutamine, or threonine should be replaced with aspartic acid, glutamic acid or serine...
  21. pmc pK values of the ionizable groups of proteins
    Richard L Thurlkill
    Department of Molecular and Cellular Medicine, Texas A and M University, System Health Science Center, College Station, Texas 77843, USA
    Protein Sci 15:1214-8. 2006
    ..Our pK values will be useful to those who study pK perturbations in folded and unfolded proteins, and to those who use theory to gain a better understanding of the factors that determine the pK values of the ionizable groups of proteins...
  22. ncbi request reprint Hydrogen bonding increases packing density in the protein interior
    David Schell
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas 77843 2128, USA
    Proteins 63:278-82. 2006
    ..For example, peptide groups in which both polar groups are hydrogen bonded occupy a volume, on average, 5.2 A3 less than a peptide group that is not hydrogen bonded...
  23. pmc Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa
    Jared M Trefethen
    Department of Biochemistry and Biophysics, Texas A and M University, College Station, TX 77843 1114, USA
    Protein Sci 14:1934-8. 2005
    ....
  24. ncbi request reprint Asp79 makes a large, unfavorable contribution to the stability of RNase Sa
    Saul R Trevino
    Department of Medical Biochemistry and Genetics, Texas A and M University, College Station, TX 77843, USA
    J Mol Biol 354:967-78. 2005
    ..When it is possible, replacing buried, non-hydrogen bonded, ionizable side-chains with non-polar side-chains is an excellent means of increasing protein stability...
  25. pmc Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa
    Roy W Alston
    Department of Medical Biochemistry and Genetics, Department of Biochemistry and Biophysics, Texas A and M University, College Station, Texas, USA
    Biophys J 87:4036-47. 2004
    ..Although all of the Trp side chains in the variants contribute to the unusual positive circular dichroism band observed near 235 nm for RNase Sa, the contribution is greatest for Y81W...
  26. pmc Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites
    Janel R McLean
    Department of Chemistry, Laboratory for Biological Mass Spectrometry, Texas A and M University, College Station, Texas 77843, USA
    J Phys Chem B 114:809-16. 2010
    ....
  27. pmc Increasing protein conformational stability by optimizing beta-turn sequence
    Saul R Trevino
    Department of Molecular and Cellular Medicine, Texas A and M University System Health Science Center, College Station, TX 77843, USA
    J Mol Biol 373:211-8. 2007
    ....
  28. pmc Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa
    Roy W Alston
    Department of Molecular and Cellular Medicine, Texas A and M University Health Science Center, Texas A and M University, College Station, Texas 77843, USA
    Biophys J 94:2288-96. 2008
    ....

Research Grants1

  1. CONFORMATIONAL STABILITY OF GLOBULAR PROTEINS
    CARLOS PACE; Fiscal Year: 2006
    ..To gain a better understanding of protein solubility, we will study the effect of single changes in the amino acid sequence of RNase Sa on the solubility of the folded and unfolded states of the protein. ..