메뉴 건너뛰기




Volumn 6, Issue 8, 1997, Pages 1727-1733

The effect of denaturants on protein structure

Author keywords

Denaturants; Dihydrofolate reductase; Protein mobility; Ribonuclease A

Indexed keywords

DIHYDROFOLATE REDUCTASE; RIBONUCLEASE A;

EID: 0030841382     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060813     Document Type: Article
Times cited : (95)

References (46)
  • 1
    • 0024412497 scopus 로고
    • Mutational effects on protein stability
    • Alber T. 1989. Mutational effects on protein stability. Annu Rev Biochem 58:765-98.
    • (1989) Annu Rev Biochem , vol.58 , pp. 765-798
    • Alber, T.1
  • 4
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate
    • Bolin JT, Filman DJ, Matthews DA, Hamlin RC, Kraut J. 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J Biol Chem 257:13650-13662.
    • (1982) J Biol Chem , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 5
    • 0000103283 scopus 로고
    • Monte Carlo simulations on the like-charged guanidinium-guanidinium ion pair in water
    • Boudon S, Wipff G, Maigret B. 1990. Monte Carlo simulations on the like-charged guanidinium-guanidinium ion pair in water. J Phys Chem 94:6056-6061.
    • (1990) J Phys Chem , vol.94 , pp. 6056-6061
    • Boudon, S.1    Wipff, G.2    Maigret, B.3
  • 6
    • 0025141786 scopus 로고
    • Surface tension measurements show that chaotropic salting-in denaturants are not just water-structure breakers
    • Breslow R, Guo T. 1990. Surface tension measurements show that chaotropic salting-in denaturants are not just water-structure breakers. Proc Natl Acad Sci USA 87:167-169.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 167-169
    • Breslow, R.1    Guo, T.2
  • 7
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger AT, Kuriyan J, Karplus M. 1987. Crystallographic R factor refinement by molecular dynamics. Science 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 8
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding
    • Bystroff C, Kraut J. 1991. Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding. Biochemistry 30:2227-2239.
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 9
    • 0025270551 scopus 로고
    • Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate-NADP+ ternary complex. Substrate binding and a model for the transition state
    • Bystroff C, Oatley SJ, Kraut J. 1990. Crystal structures of Escherichia coli dihydrofolate reductase: The NADP+ holoenzyme and the folate-NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 29:3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 10
    • 0028103275 scopus 로고
    • Collaborative Computational Project, Number 4 1994. Acta Cryst D50:760-763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 11
    • 0020442184 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis
    • Filman DJ, Bolin JT, Matthews DA, Kraut J. 1982. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis. J Biol Chem 257:13663-13672.
    • (1982) J Biol Chem , vol.257 , pp. 13663-13672
    • Filman, D.J.1    Bolin, J.T.2    Matthews, D.A.3    Kraut, J.4
  • 12
    • 0017226279 scopus 로고
    • Low resolution structure of the glycogen phosphorylase A monomer and comparison with phosphorylase B
    • Fletterick RJ, Sygusch J, Murray N, Madsen NB, Johnson LN. 1976. Low resolution structure of the glycogen phosphorylase A monomer and comparison with phosphorylase B. J Mol Biol 103:1-13.
    • (1976) J Mol Biol , vol.103 , pp. 1-13
    • Fletterick, R.J.1    Sygusch, J.2    Murray, N.3    Madsen, N.B.4    Johnson, L.N.5
  • 13
    • 0002365131 scopus 로고
    • The relationship of structure to the effectiveness of denaturing agents for proteins
    • Gordon JA, Jencks WP. 1963. The relationship of structure to the effectiveness of denaturing agents for proteins. Biochemistry 2:47-57.
    • (1963) Biochemistry , vol.2 , pp. 47-57
    • Gordon, J.A.1    Jencks, W.P.2
  • 16
    • 0018266792 scopus 로고
    • Expression of functionality of α-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation
    • Hibbard LS, Tulinski A. 1978. Expression of functionality of α-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation. Biochemistry 17:5460-5468.
    • (1978) Biochemistry , vol.17 , pp. 5460-5468
    • Hibbard, L.S.1    Tulinski, A.2
  • 17
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystal structures
    • Hodel A, Kim SH, Brünger AT. 1992. Model bias in macromolecular crystal structures. Acta Cryst A48:851-858.
    • (1992) Acta Cryst , vol.A48 , pp. 851-858
    • Hodel, A.1    Kim, S.H.2    Brünger, A.T.3
  • 18
    • 0027050469 scopus 로고
    • Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains
    • Iwakura M, Matthews CR. 1992. Construction and characterization of a single polypeptide chain containing two enzymatically active dihydrofolate reductase domains. Protein Eng 5:791-796.
    • (1992) Protein Eng , vol.5 , pp. 791-796
    • Iwakura, M.1    Matthews, C.R.2
  • 19
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A47:110-119.
    • (1991) Acta Cryst , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0029001090 scopus 로고
    • Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
    • Kiefhaber T, Labhardt AM, Baldwin RL. 1995. Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375:513-515.
    • (1995) Nature , vol.375 , pp. 513-515
    • Kiefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 21
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim KS, Woodward C. 1993. Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 32:9609-9613.
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.S.1    Woodward, C.2
  • 22
    • 0012433036 scopus 로고
    • Crystalline forms of bovine pancreatic ribonuclease: Techniques of preparation, unit cells, and space groups
    • King MV, Magdoff BS, Adelman MB, Harker D. 1956. Crystalline forms of bovine pancreatic ribonuclease: Techniques of preparation, unit cells, and space groups. Acta Crystallogr 9:460-465.
    • (1956) Acta Crystallogr , vol.9 , pp. 460-465
    • King, M.V.1    Magdoff, B.S.2    Adelman, M.B.3    Harker, D.4
  • 23
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 24
    • 0022349985 scopus 로고
    • Study of ethanol-lysozyme interactions using neutron diffraction
    • Lehmann MS, Mason SA, McIntyre GJ. 1985. Study of ethanol-lysozyme interactions using neutron diffraction. Biochemistry 24:5862-5869.
    • (1985) Biochemistry , vol.24 , pp. 5862-5869
    • Lehmann, M.S.1    Mason, S.A.2    McIntyre, G.J.3
  • 25
    • 0024976535 scopus 로고
    • Binding of dimethyl sulfoxide to lysozyme in crystals, studied with neutron diffraction
    • Lehmann MS, Stansfield RFD. 1989. Binding of dimethyl sulfoxide to lysozyme in crystals, studied with neutron diffraction. Biochemistry 28:7028-7033.
    • (1989) Biochemistry , vol.28 , pp. 7028-7033
    • Lehmann, M.S.1    Stansfield, R.F.D.2
  • 26
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride: A calorimetric study
    • Makhatadze G, Privalov PL. 1992. Protein interactions with urea and guanidinium chloride: A calorimetric study. J Mol Biol 226:491-505.
    • (1992) J Mol Biol , vol.226 , pp. 491-505
    • Makhatadze, G.1    Privalov, P.L.2
  • 27
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. 1968. Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 29
    • 0026672305 scopus 로고
    • NMR determination of residual structure in a urea-denatured protein, the 434-repressor
    • Neri D, Billeter M, Wider G, Wütrich K. 1992. NMR determination of residual structure in a urea-denatured protein, the 434-repressor. Science 257:1559-1563.
    • (1992) Science , vol.257 , pp. 1559-1563
    • Neri, D.1    Billeter, M.2    Wider, G.3    Wütrich, K.4
  • 30
    • 0021191208 scopus 로고
    • Fluctuations in protein structure from X-ray diffraction
    • Petsko GA, Ringe, DR. 1984. Fluctuations in protein structure from X-ray diffraction. Annu Rev Biophys Bioeng 13:331-371.
    • (1984) Annu Rev Biophys Bioeng , vol.13 , pp. 331-371
    • Petsko, G.A.1    Ringe, D.R.2
  • 31
    • 0028220369 scopus 로고
    • A structural basis for the interaction of urea with lysozyme
    • Pike ACW, Acharya KR. 1994. A structural basis for the interaction of urea with lysozyme. Protein Sci 3:706-710.
    • (1994) Protein Sci , vol.3 , pp. 706-710
    • Pike, A.C.W.1    Acharya, K.R.2
  • 32
    • 33847800736 scopus 로고
    • Interactions of urea and other polar compounds in water
    • Roseman M, Jencks WP. 1975. Interactions of urea and other polar compounds in water. J Am Chem Soc 97:631-640.
    • (1975) J Am Chem Soc , vol.97 , pp. 631-640
    • Roseman, M.1    Jencks, W.P.2
  • 33
    • 0023068366 scopus 로고
    • The thermodynamic stability of proteins
    • Schellman JA. 1987. The thermodynamic stability of proteins. Ann Rev Biophys Biophys Chem 16:115-137.
    • (1987) Ann Rev Biophys Biophys Chem , vol.16 , pp. 115-137
    • Schellman, J.A.1
  • 34
    • 0000114334 scopus 로고
    • The kinetics of protein denaturation. I. the behavior of the optical rotation of ovalbumin in urea solutions
    • Simpson RB, Kauzmann W. 1953. The kinetics of protein denaturation. I. The behavior of the optical rotation of ovalbumin in urea solutions. J Am Chem Soc 75:5139-5152.
    • (1953) J Am Chem Soc , vol.75 , pp. 5139-5152
    • Simpson, R.B.1    Kauzmann, W.2
  • 35
    • 0016345765 scopus 로고
    • Crystallographic study of the interaction of urea with lysozyme
    • Snape KW, Tijan R, Blake CCF, Koshland DE. 1974. Crystallographic study of the interaction of urea with lysozyme. Nature 250:295-298.
    • (1974) Nature , vol.250 , pp. 295-298
    • Snape, K.W.1    Tijan, R.2    Blake, C.C.F.3    Koshland, D.E.4
  • 37
    • 0026606219 scopus 로고
    • Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320 K
    • Tilton RF Jr, Dewan JC, Petsko GA. 1992. Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease A at nine different temperatures from 98 to 320 K. Biochemistry 31:2469-2481.
    • (1992) Biochemistry , vol.31 , pp. 2469-2481
    • Tilton Jr., R.F.1    Dewan, J.C.2    Petsko, G.A.3
  • 38
    • 0026788012 scopus 로고
    • Water as ligand: Preferential hydration and exclusion of denaturants in protein unfolding
    • Timasheff SN. 1992. Water as ligand: Preferential hydration and exclusion of denaturants in protein unfolding. Biochemistry 31:9857-9864.
    • (1992) Biochemistry , vol.31 , pp. 9857-9864
    • Timasheff, S.N.1
  • 39
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff SN. 1993. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu Rev Biophys Biomol Struct 22:67-97.
    • (1993) Annu Rev Biophys Biomol Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 40
    • 33947485233 scopus 로고
    • Nonpolar group participation in the denaturation of proteins by urea and guanidinium salts. Model compound studies
    • Wetlaufer DB, Malik SK, Stoller L, Coffin RL. 1964. Nonpolar group participation in the denaturation of proteins by urea and guanidinium salts. Model compound studies. J Am Chem Soc 86:508-514.
    • (1964) J Am Chem Soc , vol.86 , pp. 508-514
    • Wetlaufer, D.B.1    Malik, S.K.2    Stoller, L.3    Coffin, R.L.4
  • 41
    • 0001210234 scopus 로고
    • The probability distribution of X-ray intensities
    • Wilson AJC. 1949. The probability distribution of X-ray intensities. Acta Crystallogr 2:318-321.
    • (1949) Acta Crystallogr , vol.2 , pp. 318-321
    • Wilson, A.J.C.1
  • 42
    • 0021111042 scopus 로고
    • Structure of ribonuclease A: Results of joint neutron and X-ray refinement at 2.0 Å resolution
    • Wlodower A, Sjölin, L. 1983. Structure of ribonuclease A: Results of joint neutron and X-ray refinement at 2.0 Å resolution. Biochemistry 22:2720-2728.
    • (1983) Biochemistry , vol.22 , pp. 2720-2728
    • Wlodower, A.1    Sjölin, L.2
  • 43
    • 0029103572 scopus 로고
    • A structural explanation for enzyme memory in nonaqueous solvents
    • Yennawar HP, Yennawar NH, Farber GK. 1995. A structural explanation for enzyme memory in nonaqueous solvents. J Am Chem Soc 117:577-585.
    • (1995) J Am Chem Soc , vol.117 , pp. 577-585
    • Yennawar, H.P.1    Yennawar, N.H.2    Farber, G.K.3
  • 45
    • 0017335799 scopus 로고
    • Crystallographic studies of protein denaturation and renaturations. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme
    • Yonath A, Podjarny A, Honig B, Sielecki A, Traub W. 1977. Crystallographic studies of protein denaturation and renaturations. 2. Sodium dodecyl sulfate induced structural changes in triclinic lysozyme. Biochemistry 16:1418-1424.
    • (1977) Biochemistry , vol.16 , pp. 1418-1424
    • Yonath, A.1    Podjarny, A.2    Honig, B.3    Sielecki, A.4    Traub, W.5
  • 46
    • 0017913146 scopus 로고
    • Structural analysis of denaturant-protein interactions: Comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme
    • Yonath A, Podjamy A, Honig B, Traub W, Sielecki A, Herzberg O, Moult J. 1978. Structural analysis of denaturant-protein interactions: Comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme. Biophys Struct Mech 4:27-36.
    • (1978) Biophys Struct Mech , vol.4 , pp. 27-36
    • Yonath, A.1    Podjamy, A.2    Honig, B.3    Traub, W.4    Sielecki, A.5    Herzberg, O.6    Moult, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.