Search Results - "Pace, N C"

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  1. 1

    Polar Group Burial Contributes More to Protein Stability than Nonpolar Group Burial by Pace, C. Nick

    Published in Biochemistry (Easton) (16-01-2001)
    “…On the basis of studies of Asn to Ala mutants, the gain in stability from burying amide groups that are hydrogen bonded to peptide groups is 80 cal/(mol Å3)…”
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  2. 2

    How to measure and predict the molar absorption coefficient of a protein by Pace, C. Nick, Vajdos, Felix, Fee, Lanette, Grimsley, Gerald, Gray, Theronica

    Published in Protein science (01-11-1995)
    “…The molar absorption coefficient, ε, of a protein is usually based on concentrations measured by dry weight, nitrogen, or amino acid analysis. The studies…”
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  3. 3

    Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding by Myers, Jeffrey K., Nick Pace, C., Martin Scholtz, J.

    Published in Protein science (01-10-1995)
    “…Denaturant m values, the dependence of the free energy of unfolding on denaturant concentration, have been collected for a large set of proteins. The m value…”
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  4. 4

    Charge–charge interactions influence the denatured state ensemble and contribute to protein stability by PACE, C. NICK, ALSTON, ROY W., SHAW, KEVIN L.

    Published in Protein science (01-07-2000)
    “…Several recent studies have shown that it is possible to increase protein stability by improving electrostatic interactions among charged groups on the surface…”
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  5. 5

    Conformational stability of globular proteins by Pace, C N

    “…The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt…”
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  6. 6

    Measuring and increasing protein stability by Pace, C N

    Published in Trends in biotechnology (Regular ed.) (01-04-1990)
    “…Recently, it has become possible to construct proteins to order and this has promoted interest in learning how to increase their stability. This article…”
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  7. 7

    Increasing protein stability by altering long-range coulombic interactions by GRIMSLEY, GERALD R., SHAW, KEVIN L., FEE, LANETTE R., ALSTON, ROY W., HUYGHUES-DESPOINTES, BEATRICE M.P., THURLKILL, RICHARD L., SCHOLTZ, J. MARTIN, PACE, C. NICK

    Published in Protein science (01-09-1999)
    “…It is difficult to increase protein stability by adding hydrogen bonds or burying nonpolar surface. The results described here show that reversing the charge…”
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  8. 8

    Contribution of the hydrophobic effect to globular protein stability by Pace, C N

    Published in Journal of molecular biology (05-07-1992)
    “…The decrease in conformational stability, delta(delta G), has been measured for 72 aliphatic side-chain mutants from four proteins in which a larger side-chain…”
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  9. 9

    Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds by Pace, C N, Grimsley, G R, Thomson, J A, Barnett, B J

    Published in The Journal of biological chemistry (25-08-1988)
    “…Ribonuclease T1 has two disulfide bonds linking cysteine residues 2-10 and 6-103. We have prepared a derivative of ribonuclease T1 in which one disulfide bond…”
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  11. 11

    Contribution of hydrogen bonding to the conformational stability of ribonuclease T1 by Shirley, Bret A, Stanssens, Patrick, Hahn, Ulrich, Pace, C. Nick

    Published in Biochemistry (Easton) (28-01-1992)
    “…For 30 years, the prevailing view has been that the hydrophobic effect contributes considerably more than hydrogen bonding to the conformational stability of…”
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  12. 12

    Heat capacity change for ribonuclease A folding by PACE, C. NICK, GRIMSLEY, GERALD R., THOMAS, SUSAN T., MAKHATADZE, GEORGE I.

    Published in Protein science (01-07-1999)
    “…The change in heat capacity ΔCp for the folding of ribonuclease A was determined using differential scanning calorimetry and thermal denaturation curves. The…”
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  13. 13

    Protein conformational stabilities can be determined from hydrogen exchange rates by Scholtz, J. Martin, Pace, C. Nick, Huyghues-Despointes, Beatrice M.P

    Published in Nature structural biology (01-10-1999)
    “…Measuring protein conformational stability is one key to solving the protein folding problem. The conformational stability is the free energy change of the…”
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  14. 14

    A Helix Propensity Scale Based on Experimental Studies of Peptides and Proteins by Nick Pace, C., Martin Scholtz, J.

    Published in Biophysical journal (01-07-1998)
    “…The average globular protein contains 30% α-helix, the most common type of secondary structure. Some amino acids occur more frequently in α-helices than…”
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  15. 15

    Linear extrapolation method of analyzing solvent denaturation curves by Pace, C. Nick, Shaw, Kevin L.

    “…The two most common methods of measuring the conformational stability of a protein are differential scanning calorimetry and an analysis of solvent…”
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  16. 16

    Cytotoxicity mechanism of the RNase Sa cationic mutants involves inhibition of potassium current through Ca2+-activated channels by Mitkevich, V A, Pace, C N, Koschinski, A, Makarov, A A, Ilinskaya, O N

    Published in Molekuliarnaia biologiia (01-11-2015)
    “…Bacterial ribonucleases (RNases) are considered to be potential anticancer agents. One of most important determinants of RNase cytotoxicity is the net charge…”
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  17. 17

    Conformational stability and mechanism of folding of ribonuclease T1 by Thomson, J A, Shirley, B A, Grimsley, G R, Pace, C N

    Published in The Journal of biological chemistry (15-07-1989)
    “…Urea and thermal unfolding curves for ribonuclease T1 (RNase T1) were determined by measuring several different physical properties. In all cases, steep,…”
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  18. 18

    Urea denaturation of barnase: pH dependence and characterization of the unfolded state by Pace, C. Nick, Laurents, Douglas V, Erickson, Rick E

    Published in Biochemistry (Easton) (17-03-1992)
    “…To investigate the pH dependence of the conformational stability of barnase, urea denaturation curves were determined over the pH range 2-10. The maximum…”
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  19. 19

    Conformational stability and activity of ribonuclease T1 and mutants. Gln25----Lys, Glu58----Ala, and the double mutant by SHIRLEY, B. A, STANSSENS, P, STEYAERT, J, PACE, C. N

    Published in The Journal of biological chemistry (15-07-1989)
    “…Ribonuclease T1 (RNase T1) and mutants Gln25---Lys, Glu58---Ala, and the double mutant were prepared from a chemically synthesized gene, cloned and expressed…”
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