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Volumn 102, Issue 8, 2012, Pages 1907-1915

Toward a molecular understanding of protein solubility: Increased negative surface charge correlates with increased solubility

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM SULFATE; MACROGOL DERIVATIVE; PROTEIN;

EID: 84859910800     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.01.060     Document Type: Article
Times cited : (284)

References (54)
  • 1
    • 0034918477 scopus 로고    scopus 로고
    • Optimization of protein solubility and stability for protein nuclear magnetic resonance
    • DOI 10.1016/S0076-6879(01)39307-2
    • S. Bagby, K.I. Tong, M. Ikura, V.D. Thomas, L. James, and S. Uli Optimization of protein solubility and stability for protein nuclear magnetic resonance Methods in Enzymology 2001 Academic Press New York 20 41 (Pubitemid 32666554)
    • (2001) Methods in Enzymology , vol.339 , pp. 20-41
    • Bagby, S.1    Tong, K.I.2    Ikura, M.3
  • 2
    • 0035523085 scopus 로고    scopus 로고
    • The new pre-preclinical paradigm: Compound optimization in early and late phase drug discovery
    • G.W. Caldwell, and D.M. Ritchie Z. Yan The new pre-preclinical paradigm: compound optimization in early and late phase drug discovery Curr. Top. Med. Chem. 1 2001 353 366
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 353-366
    • Caldwell, G.W.1    Ritchie, D.M.2    Yan, Z.3
  • 3
    • 0031052836 scopus 로고    scopus 로고
    • Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state
    • DOI 10.1016/S0076-6879(97)76049-X
    • M. Ris-kautt, and A. Ducruix Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state C.W. Carter Jr. Methods in Enzymology 1997 Academic Press New York 23 59 (Pubitemid 27085594)
    • (1997) Methods in Enzymology , vol.276 , pp. 23-59
    • Ries-Kautt, M.1    Ducruix, A.2
  • 4
    • 0027171114 scopus 로고
    • Solubility and secretability
    • DOI 10.1016/0958-1669(93)90012-L
    • C.H. Schein Solubility and secretability Curr. Opin. Biotechnol. 4 1993 456 461 (Pubitemid 23250386)
    • (1993) Current Opinion in Biotechnology , vol.4 , Issue.4 , pp. 456-461
    • Schein, C.H.1
  • 6
    • 9944264495 scopus 로고    scopus 로고
    • Common structural stability properties of 4-helical bundle cytokines: Possible physiological and pharmaceutical consequences
    • DOI 10.2174/1381612043382611
    • M.S. Ricci, and D.N. Brems Common structural stability properties of 4-helical bundle cytokines: possible physiological and pharmaceutical consequences Curr. Pharm. Des. 10 2004 3901 3911 (Pubitemid 39591907)
    • (2004) Current Pharmaceutical Design , vol.10 , Issue.31 , pp. 3901-3911
    • Ricci, M.S.1    Brems, D.N.2
  • 7
    • 33645473596 scopus 로고    scopus 로고
    • Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface
    • H.C. Ahn, and N. Juranić J.L. Markley Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface J. Am. Chem. Soc. 128 2006 4398 4404
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4398-4404
    • Ahn, H.C.1    Juranić, N.2    Markley, J.L.3
  • 10
    • 14044262967 scopus 로고    scopus 로고
    • Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human γD-crystallin
    • DOI 10.1021/bi0479611
    • A. Pande, and O. Annunziata J. Pande Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human γD-crystallin Biochemistry 44 2005 2491 2500 (Pubitemid 40279552)
    • (2005) Biochemistry , vol.44 , Issue.7 , pp. 2491-2500
    • Pande, A.1    Annunziata, O.2    Asherie, N.3    Ogun, O.4    Benedek, G.B.5    Pande, J.6
  • 12
    • 0033621398 scopus 로고    scopus 로고
    • Aberrant protein deposition and neurological disease
    • DOI 10.1074/jbc.274.53.37507
    • M.D. Kaytor, and S.T. Warren Aberrant protein deposition and neurological disease J. Biol. Chem. 274 1999 37507 37510 (Pubitemid 30026802)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.53 , pp. 37507-37510
    • Kaytor, M.D.1    Warren, S.T.2
  • 16
    • 33846374339 scopus 로고    scopus 로고
    • Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa
    • DOI 10.1016/j.jmb.2006.10.026, PII S0022283606013647
    • S.R. Trevino, J.M. Scholtz, and C.N. Pace Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorably than the other hydrophilic amino acids in RNase Sa J. Mol. Biol. 366 2007 449 460 (Pubitemid 46136196)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.2 , pp. 449-460
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 17
    • 55749096388 scopus 로고    scopus 로고
    • Measuring and increasing protein solubility
    • S.R. Trevino, J.M. Scholtz, and C.N. Pace Measuring and increasing protein solubility J. Pharm. Sci. 97 2008 4155 4166
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4155-4166
    • Trevino, S.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 18
    • 4344602994 scopus 로고    scopus 로고
    • Introduction to protein crystallization
    • DOI 10.1016/j.ymeth.2004.03.019, PII S1046202304001094
    • A. McPherson Introduction to protein crystallization Methods 34 2004 254 265 (Pubitemid 39119812)
    • (2004) Methods , vol.34 , Issue.3 , pp. 254-265
    • McPherson, A.1
  • 19
    • 0018800167 scopus 로고
    • Determination of the apparent thermodynamic activities of saturated protein solutions
    • C.R. Middaugh, and W.A. Tisel A. Rosenberg Determination of the apparent thermodynamic activities of saturated protein solutions J. Biol. Chem. 254 1979 367 370
    • (1979) J. Biol. Chem. , vol.254 , pp. 367-370
    • Middaugh, C.R.1    Tisel, W.A.2    Rosenberg, A.3
  • 20
    • 0031031150 scopus 로고    scopus 로고
    • Initial protein concentration effects on precipitation by salt
    • K.S. Shiau, and T.L. Chen Initial protein concentration effects on precipitation by salt Biotechnol. Bioeng. 53 1997 202 206
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 202-206
    • Shiau, K.S.1    Chen, T.L.2
  • 21
    • 53549094428 scopus 로고    scopus 로고
    • Solubility of lysozyme in the presence of aqueous chloride salts: Common-ion effect and its role on solubility and crystal thermodynamics
    • O. Annunziata, A. Payne, and Y. Wang Solubility of lysozyme in the presence of aqueous chloride salts: common-ion effect and its role on solubility and crystal thermodynamics J. Am. Chem. Soc. 130 2008 13347 13352
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 13347-13352
    • Annunziata, O.1    Payne, A.2    Wang, Y.3
  • 22
    • 0024767845 scopus 로고
    • Aggregation kinetics in salt-induced protein precipitation
    • T.M. Przybycien, and J.E. Bailey Aggregation kinetics in salt-induced protein precipitation AIChE J. 35 1989 1779 1790
    • (1989) AIChE J. , vol.35 , pp. 1779-1790
    • Przybycien, T.M.1    Bailey, J.E.2
  • 23
    • 57749184562 scopus 로고    scopus 로고
    • Anion binding mediated precipitation of a peptibody
    • A. Saluja, and S. Crampton Y.R. Gokarn Anion binding mediated precipitation of a peptibody Pharm. Res. 26 2009 152 160
    • (2009) Pharm. Res. , vol.26 , pp. 152-160
    • Saluja, A.1    Crampton, S.2    Gokarn, Y.R.3
  • 24
    • 57849148494 scopus 로고    scopus 로고
    • Effect of polyols on polyethylene glycol (PEG)-induced precipitation of proteins: Impact on solubility, stability and conformation
    • V. Kumar, V.K. Sharma, and D.S. Kalonia Effect of polyols on polyethylene glycol (PEG)-induced precipitation of proteins: Impact on solubility, stability and conformation Int. J. Pharm. 366 2009 38 43
    • (2009) Int. J. Pharm. , vol.366 , pp. 38-43
    • Kumar, V.1    Sharma, V.K.2    Kalonia, D.S.3
  • 25
    • 0019877808 scopus 로고
    • Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume
    • D.H. Atha, and K.C. Ingham Mechanism of precipitation of proteins by polyethylene glycols. Analysis in terms of excluded volume J. Biol. Chem. 256 1981 12108 12117
    • (1981) J. Biol. Chem. , vol.256 , pp. 12108-12117
    • Atha, D.H.1    Ingham, K.C.2
  • 26
    • 0031029477 scopus 로고    scopus 로고
    • Charge density-dependent strength of hydration and biological structure
    • K.D. Collins Charge density-dependent strength of hydration and biological structure Biophys. J. 72 1997 65 76 (Pubitemid 27043418)
    • (1997) Biophysical Journal , vol.72 , Issue.1 , pp. 65-76
    • Collins, K.D.1
  • 27
    • 0027484016 scopus 로고
    • Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation
    • P.D. Thomas, and K.A. Dill Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation Protein Sci. 2 1993 2050 2065 (Pubitemid 23354709)
    • (1993) Protein Science , vol.2 , Issue.12 , pp. 2050-2065
    • Thomas, P.D.1    Dill, K.A.2
  • 28
    • 0022381773 scopus 로고
    • Mechanism of poly(ethylene glycol) interaction with proteins
    • DOI 10.1021/bi00345a005
    • T. Arakawa, and S.N. Timasheff Mechanism of poly(ethylene glycol) interaction with proteins Biochemistry 24 1985 6756 6762 (Pubitemid 16170203)
    • (1985) Biochemistry , vol.24 , Issue.24 , pp. 6756-6762
    • Arakawa, T.1    Timasheff, S.N.2
  • 29
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton, IRL Press Oxford
    • C.N. Pace, and J.M. Sholtz Measuring the conformational stability of a protein T.E. Creighton, Protein Structure: A Practical Approach 1997 IRL Press Oxford 229 321
    • (1997) Protein Structure: A Practical Approach , pp. 229-321
    • Pace, C.N.1    Sholtz, J.M.2
  • 31
    • 0032542062 scopus 로고    scopus 로고
    • Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1
    • DOI 10.1021/bi9815243
    • E.J. Hebert, and A. Giletto C.N. Pace Contribution of a conserved asparagine to the conformational stability of ribonucleases Sa, Ba, and T1 Biochemistry 37 1998 16192 16200 (Pubitemid 28536255)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16192-16200
    • Hebert, E.J.1    Giletto, A.2    Sevcik, J.3    Urbanikova, L.4    Wilson, K.S.5    Dauter, Z.6    Pace, C.N.7
  • 33
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 35
    • 0034624021 scopus 로고    scopus 로고
    • Binding of the general anesthetics propofol and halothane to human serum albumin: High resolution crystal structures
    • DOI 10.1074/jbc.M005460200
    • A.A. Bhattacharya, S. Curry, and N.P. Franks Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures J. Biol. Chem. 275 2000 38731 38738 (Pubitemid 32009208)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.49 , pp. 38731-38738
    • Bhattacharya, A.A.1    Curry, S.2    Franks, N.P.3
  • 36
    • 65249109808 scopus 로고    scopus 로고
    • Prostate-specific antigen is a "chymotrypsin-like" serine protease with unique P1 substrate specificity
    • A.M. LeBeau, and P. Singh S.R. Denmeade Prostate-specific antigen is a "chymotrypsin-like" serine protease with unique P1 substrate specificity Biochemistry 48 2009 3490 3496
    • (2009) Biochemistry , vol.48 , pp. 3490-3496
    • Lebeau, A.M.1    Singh, P.2    Denmeade, S.R.3
  • 37
    • 0034711229 scopus 로고    scopus 로고
    • Crystal structures of Apo- and holo-bovine α-lactalbumin at 2.2-A resolution reveal an effect of calcium on inter-lobe interactions
    • DOI 10.1074/jbc.M004752200
    • E.D. Chrysina, K. Brew, and K.R. Acharya Crystal structures of apo- and holo-bovine α-lactalbumin at 2. 2- resolution reveal an effect of calcium on inter-lobe interactions J. Biol. Chem. 275 2000 37021 37029 (Pubitemid 32002118)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 37021-37029
    • Chrysina, E.D.1    Brew, K.2    Acharya, K.R.3
  • 41
    • 0034446453 scopus 로고    scopus 로고
    • Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry
    • DOI 10.1002/1097-0290(2000)71:3<194::AID-BIT1009>3.0.CO;2-Q
    • S.A. Tobler, N.E. Sherman, and E.J. Fernandez Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry Biotechnol. Bioeng. 71 2000-2001 194 207 (Pubitemid 32381139)
    • (2000) Biotechnology and Bioengineering , vol.71 , Issue.3 , pp. 194-207
    • Tobler, S.A.1    Sherman, N.E.2    Fernandez, E.J.3
  • 42
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • R.L. Baldwin How Hofmeister ion interactions affect protein stability Biophys. J. 71 1996 2056 2063 (Pubitemid 26325984)
    • (1996) Biophysical Journal , vol.71 , Issue.4 , pp. 2056-2063
    • Baldwin, R.L.1
  • 44
    • 0032768223 scopus 로고    scopus 로고
    • Stability, activity and flexibility in α-lactalbumin
    • L.H. Greene, and J.A. Grobler K. Brew Stability, activity and flexibility in α-lactalbumin Protein Eng. 12 1999 581 587
    • (1999) Protein Eng. , vol.12 , pp. 581-587
    • Greene, L.H.1    Grobler, J.A.2    Brew, K.3
  • 45
    • 0030932504 scopus 로고    scopus 로고
    • Destabilization of human serum albumin by polyethylene glycols studied by thermodynamical equilibrium and kinetic approaches
    • DOI 10.1016/S0141-8130(96)01150-6, PII S0141813096011506
    • B. Farruggia, and G. García G. Picó Destabilization of human serum albumin by polyethylene glycols studied by thermodynamical equilibrium and kinetic approaches Int. J. Biol. Macromol. 20 1997 43 51 (Pubitemid 27168657)
    • (1997) International Journal of Biological Macromolecules , vol.20 , Issue.1 , pp. 43-51
    • Farruggia, B.1    Garcia, G.2    D'Angelo, C.3    Pico, G.4
  • 46
    • 0011374284 scopus 로고
    • Conformation of fibrinogen: Calorimetric evidence for a three-nodular structure
    • J.W. Donovan, and E. Mihalyi Conformation of fibrinogen: calorimetric evidence for a three-nodular structure Proc. Natl. Acad. Sci. USA 71 1974 4125 4128
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4125-4128
    • Donovan, J.W.1    Mihalyi, E.2
  • 47
    • 0022335486 scopus 로고
    • Nucleation and growth of protein crystals: General principles and assays
    • G. Feher, and Z. Kam Nucleation and growth of protein crystals: general principles and assays Methods Enzymol. 114 1985 77 112
    • (1985) Methods Enzymol. , vol.114 , pp. 77-112
    • Feher, G.1    Kam, Z.2
  • 49
    • 77956848213 scopus 로고    scopus 로고
    • Short communication: Relationships between α-lactalbumin and quality traits in bulk milk
    • E. Wickström, and K. Persson Waller A. Sternesjö Short communication: relationships between α-lactalbumin and quality traits in bulk milk J. Dairy Sci. 93 2010 4577 4581
    • (2010) J. Dairy Sci. , vol.93 , pp. 4577-4581
    • Wickström, E.1    Persson Waller, K.2    Sternesjö, A.3
  • 51
    • 0028999046 scopus 로고
    • Sticky ions in biological systems
    • K.D. Collins Sticky ions in biological systems Proc. Natl. Acad. Sci. USA 92 1995 5553 5557
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5553-5557
    • Collins, K.D.1
  • 52
    • 4344565219 scopus 로고    scopus 로고
    • Ions from the Hofmeister series and osmolytes: Effects on proteins in solution and in the crystallization process
    • DOI 10.1016/j.ymeth.2004.03.021, PII S1046202304001124
    • K.D. Collins Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process Methods 34 2004 300 311 (Pubitemid 39119814)
    • (2004) Methods , vol.34 , Issue.3 , pp. 300-311
    • Collins, K.D.1
  • 53
    • 34249706387 scopus 로고    scopus 로고
    • Ions in water: Characterizing the forces that control chemical processes and biological structure
    • DOI 10.1016/j.bpc.2007.03.009, PII S0301462207000786
    • K.D. Collins, G.W. Neilson, and J.E. Enderby Ions in water: characterizing the forces that control chemical processes and biological structure Biophys. Chem. 128 2007 95 104 (Pubitemid 46843439)
    • (2007) Biophysical Chemistry , vol.128 , Issue.2-3 , pp. 95-104
    • Collins, K.D.1    Neilson, G.W.2    Enderby, J.E.3
  • 54
    • 84885608153 scopus 로고    scopus 로고
    • Protein Calculator. http://www.scripps.edu/∼cdputnam/protcalc.html.
    • Protein Calculator


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