C. Nick Pace
#145,882
Most Influential Person Now
C. Nick Pace's AcademicInfluence.com Rankings
C. Nick Pacechemistry Degrees
Chemistry
#3857
World Rank
#4901
Historical Rank
Physical Chemistry
#560
World Rank
#612
Historical Rank
C. Nick Pacebiology Degrees
Biology
#10591
World Rank
#13931
Historical Rank
Biochemistry
#1685
World Rank
#1820
Historical Rank
Download Badge
Chemistry Biology
C. Nick Pace's Degrees
- PhD Biochemistry University of California, Berkeley
- Masters Chemistry Stanford University
- Bachelors Chemistry Stanford University
Why Is C. Nick Pace Influential?
(Suggest an Edit or Addition)C. Nick Pace's Published Works
Number of citations in a given year to any of this author's works
Total number of citations to an author for the works they published in a given year. This highlights publication of the most important work(s) by the author
Published Works
- How to measure and predict the molar absorption coefficient of a protein (1995) (3614)
- Determination and analysis of urea and guanidine hydrochloride denaturation curves. (1986) (2113)
- A helix propensity scale based on experimental studies of peptides and proteins. (1998) (859)
- Forces contributing to the conformational stability of proteins (1996) (651)
- The Stability of Globular Protein (1975) (541)
- Urea and Guanidine Hydrochloride Denaturation of Ribonuclease , Lysozyme , & Zhymotrypsin , and @ Lactoglobulin * (2003) (474)
- Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. (1988) (396)
- A summary of the measured pK values of the ionizable groups in folded proteins (2008) (389)
- Conformational stability of globular proteins. (1990) (381)
- Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility* (2009) (370)
- Protein structure, stability and solubility in water and other solvents. (2004) (323)
- pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. (1990) (311)
- pK values of the ionizable groups of proteins (2006) (302)
- Linear extrapolation method of analyzing solvent denaturation curves (2000) (276)
- Contribution of hydrogen bonds to protein stability (2014) (271)
- Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility. (2012) (263)
- Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. (1992) (253)
- Hydrogen bonding stabilizes globular proteins. (1996) (245)
- Contribution of hydrophobic interactions to protein stability. (2011) (239)
- The effect of net charge on the solubility, activity, and stability of ribonuclease Sa (2001) (229)
- Contribution of the hydrophobic effect to globular protein stability. (1992) (219)
- Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa. (2007) (203)
- Increasing protein stability by altering long‐range coulombic interactions (1999) (203)
- Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. (1974) (188)
- A new method for determining the heat capacity change for protein folding. (1989) (170)
- Protein conformational stabilities can be determined from hydrogen exchange rates (1999) (153)
- Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3. (1998) (153)
- Helix propensities are identical in proteins and peptides. (1997) (145)
- Measuring and increasing protein stability. (1990) (144)
- Polar group burial contributes more to protein stability than nonpolar group burial. (2001) (143)
- The stability of globular proteins. (1975) (141)
- Determining globular protein stability: guanidine hydrochloride denaturation of myoglobin. (1979) (138)
- Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation. (1980) (138)
- Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. (1997) (136)
- Measuring and increasing protein solubility. (2008) (131)
- Ribonuclease T1: Structure, Function, and Stability (1991) (130)
- Guanidine hydrochloride and acid denaturation of horse, cow, and Candida krusei cytochromes c. (1974) (122)
- Tyrosine hydrogen bonds make a large contribution to protein stability. (2001) (122)
- Increasing protein conformational stability by optimizing β-turn sequence (2007) (115)
- Urea denaturation of barnase: pH dependence and characterization of the unfolded state. (1992) (111)
- A direct comparison of helix propensity in proteins and peptides. (1997) (110)
- 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). (2003) (99)
- Increasing protein stability by improving beta‐turns (2009) (94)
- Spectrophotometric Determination of Protein Concentration (2003) (84)
- Measuring the conformational stability of a protein by NMR. (2006) (83)
- Measuring the conformational stability of a protein by hydrogen exchange. (2001) (82)
- Thermodynamics of ribonuclease T1 denaturation. (1992) (81)
- Buried, charged, non-ion-paired aspartic acid 76 contributes favorably to the conformational stability of ribonuclease T1. (1999) (81)
- Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding. (1995) (76)
- Solvent denaturation of proteins and interpretations of the m value. (2009) (73)
- Conformational stability and mechanism of folding of ribonuclease T1. (1989) (67)
- Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic (2002) (67)
- Heat capacity change for ribonuclease A folding (1999) (65)
- Purification of ribonucleases Sa, Sa2, and Sa3 after expression in Escherichia coli. (1997) (62)
- Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins. (2006) (61)
- Energetics of ribonuclease T1 structure. (1994) (61)
- Conformational stability and activity of ribonuclease T1 and mutants. Gln25----Lys, Glu58----Ala, and the double mutant. (1989) (60)
- The Contribution of Polar Group Burial to Protein Stability Is Strongly Context-dependent* (2003) (57)
- Kinetics of tryptic hydrolysis of the arginine-valine bond in folded and unfolded ribonuclease T1. (1984) (57)
- Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1. (1998) (56)
- Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala. (1990) (54)
- Increasing protein conformational stability by optimizing beta-turn sequence. (2007) (53)
- A comparison of the effectiveness of protein denaturants for beta-lactoglobulin and ribonuclease. (1980) (52)
- Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopy. (1993) (47)
- Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa (2005) (44)
- Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa. (2004) (42)
- Peptide sequence and conformation strongly influence tryptophan fluorescence. (2008) (41)
- pK values of histidine residues in ribonuclease Sa: effect of salt and net charge. (2003) (38)
- Hydrogen bonding increases packing density in the protein interior (2005) (38)
- Temperature and guanidine hydrochloride dependence of the structural stability of ribonuclease T1. (1992) (36)
- Distinct Secondary Structures of the Leucine-rich Repeat Proteoglycans Decorin and Biglycan (1999) (35)
- Asp79 makes a large, unfavorable contribution to the stability of RNase Sa. (2005) (34)
- Denaturation of Proteins by Urea and Guanidine Hydrochloride (2008) (33)
- Inhibition of pepsinogen activation by gossypol. (1970) (33)
- Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites. (2010) (31)
- pKa of fentanyl varies with temperature: implications for acid-base management during extremes of body temperature. (2005) (30)
- Increasing protein stability: Importance of ΔCp and the denatured state (2010) (30)
- Solution structure and dynamics of ribonuclease Sa (2001) (29)
- Conformational stability of ribonuclease T1 determined by hydrogen‐deuterium exchange (1997) (28)
- Cytotoxicity of RNases is increased by cationization and counteracted by K(Ca) channels. (2004) (26)
- Contribution of active site residues to the activity and thermal stability of ribonuclease Sa (2003) (25)
- Proteins: Structure, Function, and Bioinformatics (2009) (25)
- Determining the conformational stability of a protein using urea denaturation curves. (2009) (24)
- Hydrogen-exchange stabilities of RNase T1 and variants with buried and solvent-exposed Ala --> Gly mutations in the helix. (1999) (24)
- Ribonuclease T1 is stabilized by cation and anion binding. (1988) (23)
- Steady-state kinetic studies of arginase with an improved direct spectrophotometric assay. (1980) (22)
- RNase-induced apoptosis: fate of calcium-activated potassium channels. (2008) (21)
- Tryptophan fluorescence reveals the presence of long-range interactions in the denatured state of ribonuclease Sa. (2008) (20)
- Wheat Alcohol Dehydrogenase Isozymes: PURIFICATION, CHARACTERIZATION, AND GENE EXPRESSION. (1980) (19)
- Purification and partial characterization of alcohol dehydrogenase from wheat. (1979) (17)
- A comparison of the denaturation of bovine -lactoglobulins A and B and goat -lactoglobulin. (1971) (17)
- Cytotoxicity of RNase Sa to the acute myeloid leukemia Kasumi-1 cells depends on the net charge (2014) (16)
- The alpha-helix of ribonuclease T1 as an independent stability unit: direct comparison of peptide and protein stability. (1996) (15)
- How to determine the molar absorption coefficient of a protein (1997) (13)
- Conformational stability of mixed disulfide derivatives of beta-lactoglobulin B. (1983) (12)
- Purification of ribonuclease T1. (1987) (12)
- Charge-charge interactions are the primary determinants of the pK values of the ionizable groups in Ribonuclease T1. (2002) (11)
- Arginase inhibition. (1981) (10)
- Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange. (2005) (10)
- Ultrasonic absorption measurements in aqueous solutions of glycine, diglycine, and triglycine. (1968) (10)
- BBA reportArginase inhibition (1981) (10)
- Globular protein stability: aspects of interest in protein turnover. (1981) (8)
- Increased stability of human growth hormone with reduced lactogenic potency (2002) (7)
- Protein conformations and their stability (1983) (6)
- Preparation of urea and guanidinium chloride stock solutions for measuring denaturant-induced unfolding curves. (2006) (6)
- Letter to the Editor: Sequential assignment and solution secondary structure of doubly labelled ribonuclease Sa (1999) (5)
- Determining a urea or guanidinium chloride unfolding curve. (2006) (3)
- Contribution of Hydrogen Bonding and the Hydrophobic Effect to Conformational Stability of Ribonuclease T1 (1993) (2)
- Cytotoxicity mechanism of the RNase Sa cationic mutants involves inhibition of potassium current through Ca2+-activated channels (2015) (1)
- Determining a thermal unfolding curve. (2006) (0)
- RIBONUCLEASE T1 COMPLEXED WITH 2'GMP/G23A MUTANT (1998) (0)
- Increasing Enzyme Stability (1990) (0)
- N39S MUTANT OF RNASE SA FROM STREPTOMYCES AUREOFACIENS (2004) (0)
- Cytotoxicity mechanism of the RNase Sa cationic mutants involves inhibition of potassium current through Ca2+-activated channels (2015) (0)
- SOLUTION STRUCTURE OF RIBONUCLEASE SA (2001) (0)
- Mutants of RNase Sa (2003) (0)
- SOAKED IN LANGUAGE Hermeneutics of an ecological agency (2021) (0)
- Fine-Tuning Protein Stability (2010) (0)
This paper list is powered by the following services:
What Schools Are Affiliated With C. Nick Pace?
C. Nick Pace is affiliated with the following schools:
