메뉴 건너뛰기




Volumn 5, Issue 2, 1996, Pages 204-211

Are turns required for the folding of ribonuclease T1?

Author keywords

circular permuted proteins; protein folding; ribonuclease T1

Indexed keywords

RIBONUCLEASE T1;

EID: 0030020571     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050203     Document Type: Article
Times cited : (34)

References (35)
  • 1
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick T, Mayne L, Englander SW. 1995. Protein folding intermediates: Native-state hydrogen exchange. Science 269:192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.2    Mayne, L.3    Englander, S.W.4
  • 2
    • 0026516388 scopus 로고
    • A fully active variant of dihydrofolate reductase with a circularly permuted sequence
    • Buchwalder A, Szadkowski H, Kirschner K. 1992. A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry 31:1621-1630.
    • (1992) Biochemistry , vol.31 , pp. 1621-1630
    • Buchwalder, A.1    Szadkowski, H.2    Kirschner, K.3
  • 3
    • 0014163158 scopus 로고
    • The statistical analysis of enzyme kinetic data
    • Cleland WW. 1967. The statistical analysis of enzyme kinetic data. Adv Enzymol Related Areas Mol Biol 29:1-32.
    • (1967) Adv Enzymol Related Areas Mol Biol , vol.29 , pp. 1-32
    • Cleland, W.W.1
  • 4
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg DP, Creighton TE. 1983. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor J Mol Biol 165:407-413.
    • (1983) J Mol Biol , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 5
    • 0001798502 scopus 로고
    • Immunoblotting
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory
    • Harlow E, Lane D. 1988. Immunoblotting. In: Antibodies: A laboratory manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory, pp 471-510.
    • (1988) Antibodies: A Laboratory Manual , pp. 471-510
    • Harlow, E.1    Lane, D.2
  • 6
    • 0020473605 scopus 로고
    • Specific protein-nucleic acid recognition in ribonuclease Tl-2′-guanylic acid complex: An X-ray study
    • Heinemann U, Saenger W. 1982. Specific protein-nucleic acid recognition in ribonuclease Tl-2′-guanylic acid complex: An X-ray study. Nature 299:27-31.
    • (1982) Nature , vol.299 , pp. 27-31
    • Heinemann, U.1    Saenger, W.2
  • 7
    • 0024520745 scopus 로고
    • Site directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR. 1989. Site directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 10
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings PA, Wright PE. 1993. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262: 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 11
    • 0028178981 scopus 로고
    • A circularly permuted recombinant interleukin-4 toxin with increased activity
    • Kreitman R, Puri RK, Pastan I. 1994. A circularly permuted recombinant interleukin-4 toxin with increased activity. Proc Natl Acad Sci USA 91:6889-6893.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6889-6893
    • Kreitman, R.1    Puri, R.K.2    Pastan, I.3
  • 12
    • 0018093765 scopus 로고
    • Conformational preferences of amino acids in globular proteins
    • Levitt M. 1978. Conformational preferences of amino acids in globular proteins. Biochemistry 17:4277-4285.
    • (1978) Biochemistry , vol.17 , pp. 4277-4285
    • Levitt, M.1
  • 13
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a βα barrel enzyme in vivo
    • Luger K, Hommel U, Herold M, Hofsteenge J, Kirschner K. 1989. Correct folding of circularly permuted variants of a βα barrel enzyme in vivo. Science 243:206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 14
    • 0025727187 scopus 로고
    • Structurally conserved water molecules in ribonuclease T1
    • Malin R, Zielenkiewicz P, Saenger W. 1991. Structurally conserved water molecules in ribonuclease T1. J Biol Chem 266:4848-4852.
    • (1991) J Biol Chem , vol.266 , pp. 4848-4852
    • Malin, R.1    Zielenkiewicz, P.2    Saenger, W.3
  • 15
    • 0026357217 scopus 로고
    • Ribonuclease T1 with free recognition and catalytic site: Crystal structure analysis at 1.5 Å resolution
    • Martinez-Oyanedel J, Choe HW, Heinemann U, Saenger W. 1991. Ribonuclease T1 with free recognition and catalytic site: Crystal structure analysis at 1.5 Å resolution. J Mol Biol 222:335-352.
    • (1991) J Mol Biol , vol.222 , pp. 335-352
    • Martinez-Oyanedel, J.1    Choe, H.W.2    Heinemann, U.3    Saenger, W.4
  • 16
    • 0027550008 scopus 로고
    • A purification method for labile variants of ribonuclease T1
    • Mayr LM, Schmid FX. 1993. A purification method for labile variants of ribonuclease T1. Protein Purif Expr 4:52-58.
    • (1993) Protein Purif Expr , vol.4 , pp. 52-58
    • Mayr, L.M.1    Schmid, F.X.2
  • 17
    • 0027335940 scopus 로고
    • Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange two-dimensional NMR spectroscopy
    • Mullins LS, Pace CN, Raushel FM. 1993. Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange two-dimensional NMR spectroscopy. Biochemistry 32:6152-6156.
    • (1993) Biochemistry , vol.32 , pp. 6152-6156
    • Mullins, L.S.1    Pace, C.N.2    Raushel, F.M.3
  • 19
    • 0017128657 scopus 로고
    • Simple assay methods for ribonuclease T1, T2 and nuclease P1
    • Oshima T, Uenishi N, Imahori K. 1976. Simple assay methods for ribonuclease T1, T2 and nuclease P1. Anal Biochem 71:632-634.
    • (1976) Anal Biochem , vol.71 , pp. 632-634
    • Oshima, T.1    Uenishi, N.2    Imahori, K.3
  • 20
    • 0023042010 scopus 로고
    • The disulphide folding pathway of ribonuclease T1
    • Pace CN, Creighton TE. 1986. The disulphide folding pathway of ribonuclease T1. J Mol Biol 188:11820-11825.
    • (1986) J Mol Biol , vol.188 , pp. 11820-11825
    • Pace, C.N.1    Creighton, T.E.2
  • 21
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds
    • Pace CN, Grimsley GR, Thompson JA, Barnet BJ. 1988. Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J Biol Chem 263:11820-11825.
    • (1988) J Biol Chem , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thompson, J.A.3    Barnet, B.J.4
  • 23
    • 0028331910 scopus 로고
    • Crystallographic study of Glu 58 Ala-RNase T1 2′-guanosine monophosphate at 1.9-Å resolution
    • Pletinckx J, Steyaert J, Zegers I, Choe HW, Heinemann U, Wyns L. 1994. Crystallographic study of Glu 58 Ala-RNase T1 2′-guanosine monophosphate at 1.9-Å resolution. Biochemistry 33:1654-1662.
    • (1994) Biochemistry , vol.33 , pp. 1654-1662
    • Pletinckx, J.1    Steyaert, J.2    Zegers, I.3    Choe, H.W.4    Heinemann, U.5    Wyns, L.6
  • 24
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 25
    • 0025327131 scopus 로고
    • Purification of recombinant ribonuclease T1 expressed in Escherichia coli
    • Shirley BA, Laurents DV. 1990. Purification of recombinant ribonuclease T1 expressed in Escherichia coli. J Biochem Biophys Methods 20:181-188.
    • (1990) J Biochem Biophys Methods , vol.20 , pp. 181-188
    • Shirley, B.A.1    Laurents, D.V.2
  • 26
    • 0025947177 scopus 로고
    • Subsite interactions of ribonuclease T1 : Asn 36 and Asn 98 accelerate GpN transesterification through interactions with the leaving nucleoside N
    • Steyaert J, Haikal AF, Wyns L, Stanssens P. 1991a. Subsite interactions of ribonuclease T1 : Asn 36 and Asn 98 accelerate GpN transesterification through interactions with the leaving nucleoside N. Biochemistry 30: 8666-8670.
    • (1991) Biochemistry , vol.30 , pp. 8666-8670
    • Steyaert, J.1    Haikal, A.F.2    Wyns, L.3    Stanssens, P.4
  • 27
    • 0025045326 scopus 로고
    • Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine
    • Steyaert J, Hallenga K, Wyns L, Stanssens P. 1990. Histidine-40 of ribonuclease T1 acts as base catalyst when the true catalytic base, glutamic acid-58, is replaced by alanine. Biochemistry 29:9064-9072.
    • (1990) Biochemistry , vol.29 , pp. 9064-9072
    • Steyaert, J.1    Hallenga, K.2    Wyns, L.3    Stanssens, P.4
  • 28
    • 0026064138 scopus 로고
    • Quantitative analysis of the contribution of Glu 46 and Asn 98 to the guanosine specificity of ribonuclease T1
    • Steyaert J, Opsomer C, Wyns L, Stanssens P. 1991b. Quantitative analysis of the contribution of Glu 46 and Asn 98 to the guanosine specificity of ribonuclease T1. Biochemistry 30:494-499.
    • (1991) Biochemistry , vol.30 , pp. 494-499
    • Steyaert, J.1    Opsomer, C.2    Wyns, L.3    Stanssens, P.4
  • 29
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 30
    • 0028943593 scopus 로고
    • Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Vignais ML, Corbier C, Mulliert G, Branlant C, Branlant G. 1995. Circular permutation within the coenzyme binding domain of the tetrameric glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Protein Sci 4:994-1000.
    • (1995) Protein Sci , vol.4 , pp. 994-1000
    • Vignais, M.L.1    Corbier, C.2    Mulliert, G.3    Branlant, C.4    Branlant, G.5
  • 31
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera AR, Blanco FJ, Serrano L. 1995. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J Mol Biol 247:610-681.
    • (1995) J Mol Biol , vol.247 , pp. 610-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 32
    • 0027143219 scopus 로고
    • Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains
    • Yang YR, Schachman HK. 1993. Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains. Proc Natl Acad Sci USA 90:11980-11984.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11980-11984
    • Yang, Y.R.1    Schachman, H.K.2
  • 33
    • 0017075643 scopus 로고
    • Subsites and catalytic mechanism of ribonuclease T1: Kinetic studies using GpC and GpU as substrates
    • Zabinski M, Walz FG. 1976. Subsites and catalytic mechanism of ribonuclease T1: Kinetic studies using GpC and GpU as substrates. Arch Biochem Biophys 175:558-561.
    • (1976) Arch Biochem Biophys , vol.175 , pp. 558-561
    • Zabinski, M.1    Walz, F.G.2
  • 34
    • 0023359283 scopus 로고
    • DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residues
    • Zell R, Fritz HJ. 1987. DNA mismatch-repair in Escherichia coli counteracting the hydrolytic deamination of 5-methyl-cytosine residues. EMBO J 6:1809-1815.
    • (1987) EMBO J , vol.6 , pp. 1809-1815
    • Zell, R.1    Fritz, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.