메뉴 건너뛰기




Volumn 6, Issue 4, 1997, Pages 882-891

An engineered amino-terminal domain of yeast phosphoglycerate kinase with native-like structure

Author keywords

autonomously folding domains; isolated domains; phosphoglycerate kinase; protein engineering; protein folding

Indexed keywords

PHOSPHOGLYCERATE KINASE;

EID: 0030987203     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060415     Document Type: Article
Times cited : (12)

References (67)
  • 1
    • 0022350869 scopus 로고
    • The folding and mutual interaction of the domains of yeast 3-phosphoglycerate kinase
    • Adams B, Burgess RJ, Pain RH. 1985. The folding and mutual interaction of the domains of yeast 3-phosphoglycerate kinase. Eur J Biochem 152:715-720.
    • (1985) Eur J Biochem , vol.152 , pp. 715-720
    • Adams, B.1    Burgess, R.J.2    Pain, R.H.3
  • 2
    • 0029044324 scopus 로고
    • NMR structure of a stable OB-fold sub-domain isolated from staphylococcal nuclease
    • Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D. 1995. NMR structure of a stable OB-fold sub-domain isolated from staphylococcal nuclease. J Mol Biol 250:134-143.
    • (1995) J Mol Biol , vol.250 , pp. 134-143
    • Alexandrescu, A.T.1    Gittis, A.G.2    Abeygunawardana, C.3    Shortle, D.4
  • 3
    • 0028884985 scopus 로고
    • Sequential domain unfolding in phosphoglycerate kinase: Fluorescence intensity and anisotropy stopped-flow kinetics of several tryptophan mutants
    • Beechem JM, Sherman MA, Mas MT. 1995. Sequential domain unfolding in phosphoglycerate kinase: Fluorescence intensity and anisotropy stopped-flow kinetics of several tryptophan mutants. Biochemistry 34:13943-13948.
    • (1995) Biochemistry , vol.34 , pp. 13943-13948
    • Beechem, J.M.1    Sherman, M.A.2    Mas, M.T.3
  • 4
    • 0027958569 scopus 로고
    • The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: Activation is inhibited by NIFL
    • Berger DK, Narberhaus F, Kustu S. 1994. The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: Activation is inhibited by NIFL. Proc Natl Acad Sci USA 91:103-107.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 103-107
    • Berger, D.K.1    Narberhaus, F.2    Kustu, S.3
  • 5
    • 0029614733 scopus 로고
    • Functional analysis of isolated cpn10 domains and conserved amino acid residues in spinach chloroplast co-chaperonin by site-directed mutagenesis
    • Bertsch U, Soll J. 1995. Functional analysis of isolated cpn10 domains and conserved amino acid residues in spinach chloroplast co-chaperonin by site-directed mutagenesis. Plant Mol Biol 29:1039-1055.
    • (1995) Plant Mol Biol , vol.29 , pp. 1039-1055
    • Bertsch, U.1    Soll, J.2
  • 6
    • 0028334515 scopus 로고
    • Refolding of the isolated extracellular domain of the erythropoietin receptor
    • Bessalle R, D'Andrea A, Fasman G. 1994. Refolding of the isolated extracellular domain of the erythropoietin receptor. Biochem Biophys Res Commun 200:482-488.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 482-488
    • Bessalle, R.1    D'Andrea, A.2    Fasman, G.3
  • 7
    • 0024973030 scopus 로고
    • A simple model for proteins with interacting domains. Applications to scanning calorimetry data
    • Brandts JF, Hu CQ, Lin LN, Mas MT. 1989. A simple model for proteins with interacting domains. Applications to scanning calorimetry data. Biochemistry 28:8588-8596.
    • (1989) Biochemistry , vol.28 , pp. 8588-8596
    • Brandts, J.F.1    Hu, C.Q.2    Lin, L.N.3    Mas, M.T.4
  • 8
    • 23444449882 scopus 로고
    • Building protein structure and function from modular units
    • Campbell ID, Downing AK. 1994. Building protein structure and function from modular units. Trends Biotechnol 12:168-172.
    • (1994) Trends Biotechnol , vol.12 , pp. 168-172
    • Campbell, I.D.1    Downing, A.K.2
  • 9
    • 0027298784 scopus 로고
    • Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities
    • Chakrabartty A, Kortemme T, Padmanabhan S, Baldwin RL. 1993. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry 32:5560-5565.
    • (1993) Biochemistry , vol.32 , pp. 5560-5565
    • Chakrabartty, A.1    Kortemme, T.2    Padmanabhan, S.3    Baldwin, R.L.4
  • 10
    • 0021760764 scopus 로고
    • Homologous versus heterologous gene expression in the yeast, Saccharomyces cerevisiae
    • Chen CY, Opperman H, Hitzeman RA. 1984. Homologous versus heterologous gene expression in the yeast, Saccharomyces cerevisiae. Nucleic Acids Res 12:8951-8970.
    • (1984) Nucleic Acids Res , vol.12 , pp. 8951-8970
    • Chen, C.Y.1    Opperman, H.2    Hitzeman, R.A.3
  • 11
    • 0021943866 scopus 로고
    • Supercoil sequencing: A fast and simple method for sequencing plasmid DNA
    • Chen EY, Seeburg PH. 1985. Supercoil sequencing: A fast and simple method for sequencing plasmid DNA. DNA 4:165-170.
    • (1985) DNA , vol.4 , pp. 165-170
    • Chen, E.Y.1    Seeburg, P.H.2
  • 14
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink MR. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J 66:482-501.
    • (1994) Biophys J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 15
    • 0025336465 scopus 로고
    • An NMR study of anion binding to yeast phosphoglycerate kinase
    • Fairbrother WJ, Graham HC, Williams RJP. 1990. An NMR study of anion binding to yeast phosphoglycerate kinase. Eur J Biochem 190:161-169.
    • (1990) Eur J Biochem , vol.190 , pp. 161-169
    • Fairbrother, W.J.1    Graham, H.C.2    Williams, R.J.P.3
  • 18
    • 0024405187 scopus 로고
    • NMR analysis of site-specific mutants of yeast phosphoglycerate kinase: An investigation of the triose-binding site
    • Fairbrother WJ, Walker PA, Minard P, Littlechild JA, Watson HC, Williams RJP. 1989c. NMR analysis of site-specific mutants of yeast phosphoglycerate kinase: An investigation of the triose-binding site. Eur J Biochem 183: 57-67.
    • (1989) Eur J Biochem , vol.183 , pp. 57-67
    • Fairbrother, W.J.1    Walker, P.A.2    Minard, P.3    Littlechild, J.A.4    Watson, H.C.5    Williams, R.J.P.6
  • 19
    • 0026567099 scopus 로고
    • The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase
    • Freire E, Murphy KP, Sanchez-Ruiz JM, Galisteo ML, Privalov PL. 1992. The molecular basis of cooperativity in protein folding. Thermodynamic dissection of interdomain interactions in phosphoglycerate kinase. Biochemistry 31:250-256.
    • (1992) Biochemistry , vol.31 , pp. 250-256
    • Freire, E.1    Murphy, K.P.2    Sanchez-Ruiz, J.M.3    Galisteo, M.L.4    Privalov, P.L.5
  • 20
    • 0029037099 scopus 로고
    • Isolated RNA binding domain of a class I tRNa synthetase
    • Gale AJ, Schimmel P. 1995. Isolated RNA binding domain of a class I tRNA synthetase. Biochemistry 54:8896-8903.
    • (1995) Biochemistry , vol.54 , pp. 8896-8903
    • Gale, A.J.1    Schimmel, P.2
  • 21
    • 0029160655 scopus 로고
    • Reconstitution of the second step in NO synthesis using the isolated oxygenase and reductase domains of macrophage NO synthase
    • Ghosh DK, Abu-Soud HM, Stuehr DJ. 1995. Reconstitution of the second step in NO synthesis using the isolated oxygenase and reductase domains of macrophage NO synthase. Biochemistry 34:11316-11320.
    • (1995) Biochemistry , vol.34 , pp. 11316-11320
    • Ghosh, D.K.1    Abu-Soud, H.M.2    Stuehr, D.J.3
  • 22
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 23
    • 0027433120 scopus 로고
    • Visualization of the adsorption of a bacterial endo-beta-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose
    • Gilkes NR, Kilburn DG, Miller RC Jr, Warren RA, Sugiyama J, Chanzy H, Henrissat B. 1993. Visualization of the adsorption of a bacterial endo-beta-1,4-glucanase and its isolated cellulose-binding domain to crystalline cellulose. Int J Biol Macromol 15:347-351.
    • (1993) Int J Biol Macromol , vol.15 , pp. 347-351
    • Gilkes, N.R.1    Kilburn, D.G.2    Miller Jr., R.C.3    Warren, R.A.4    Sugiyama, J.5    Chanzy, H.6    Henrissat, B.7
  • 24
    • 0026536746 scopus 로고
    • Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate
    • Harlos K, Vas M, Blake CF. 1992. Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-D-glycerate. Proteins Struct Funct Genet 12:133-144.
    • (1992) Proteins Struct Funct Genet , vol.12 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.F.3
  • 25
    • 0025787374 scopus 로고
    • Autonomous folding and coenzyme binding of the excised pyridoxal 5′-phosphate binding domain of aspartate aminotransferase from Escherichia coli
    • Herold M, Leistler B, Hage A, Luger K, Kirschner K. 1991. Autonomous folding and coenzyme binding of the excised pyridoxal 5′-phosphate binding domain of aspartate aminotransferase from Escherichia coli Biochemistry 30:3612-3620
    • (1991) Biochemistry , vol.30 , pp. 3612-3620
    • Herold, M.1    Leistler, B.2    Hage, A.3    Luger, K.4    Kirschner, K.5
  • 26
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, Saiki RK. 1988. A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions. Nucleic Acid Res 16:7351-7367.
    • (1988) Nucleic Acid Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 27
    • 0023146181 scopus 로고
    • Thermodynamic study of yeast phosphoglycerate kinase
    • Hu CQ, Sturtevant JM. 1987. Thermodynamic study of yeast phosphoglycerate kinase. Biochemistry 26:178-182.
    • (1987) Biochemistry , vol.26 , pp. 178-182
    • Hu, C.Q.1    Sturtevant, J.M.2
  • 28
    • 0027384577 scopus 로고
    • Effect of cavity-creating mutations in the hydrophobic core of chymostrypsin inhibitor 2
    • Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR. 1993. Effect of cavity-creating mutations in the hydrophobic core of chymostrypsin inhibitor 2. Biochemistry 32:11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    ElMasry, N.3    Johnson, C.M.4    Fersht, A.R.5
  • 29
    • 0028295627 scopus 로고
    • Autonomous folding of the excised coenzyme-binding domain of D-glyceraldehyde 3-phosphate dehydrogenase from Thermotoga maritima
    • Jecht M, Tomschy A, Kirschner K, Jaenicke R. 1994. Autonomous folding of the excised coenzyme-binding domain of D-glyceraldehyde 3-phosphate dehydrogenase from Thermotoga maritima. Protein Sci 3:411-418.
    • (1994) Protein Sci , vol.3 , pp. 411-418
    • Jecht, M.1    Tomschy, A.2    Kirschner, K.3    Jaenicke, R.4
  • 30
    • 0030025170 scopus 로고    scopus 로고
    • Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage
    • Klemm JD, Pabo CO. 1996. Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage Genes & Dev 10:27-36.
    • (1996) Genes & Dev , vol.10 , pp. 27-36
    • Klemm, J.D.1    Pabo, C.O.2
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0017380039 scopus 로고
    • Isolation and characterization of Saccharomyces cerevisiae glycolytic pathway mutants
    • Lam KB, Marmur J. 1977. Isolation and characterization of Saccharomyces cerevisiae glycolytic pathway mutants. J Bacterial 130:746-749.
    • (1977) J Bacterial , vol.130 , pp. 746-749
    • Lam, K.B.1    Marmur, J.2
  • 33
    • 0029003308 scopus 로고
    • Electron transfer between cytochrome c and the isolated CuA domain: Identification of substrate-binding residues in cytochrome c oxidase
    • Lappalainen P, Watmough NJ, Greenwood C, Saraste M. 1995. Electron transfer between cytochrome c and the isolated CuA domain: Identification of substrate-binding residues in cytochrome c oxidase. Biochemistry 54:5824-5830.
    • (1995) Biochemistry , vol.54 , pp. 5824-5830
    • Lappalainen, P.1    Watmough, N.J.2    Greenwood, C.3    Saraste, M.4
  • 34
    • 0028874438 scopus 로고
    • Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain
    • Lemmon MA, Ferguson KM, O'Brien R, Sigler PB, Schlessinger J. 1995. Specific and high-affinity binding of inositol phosphates to an isolated pleckstrin homology domain. Proc Natl Acad Sci USA 92:10472-10476.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10472-10476
    • Lemmon, M.A.1    Ferguson, K.M.2    O'Brien, R.3    Sigler, P.B.4    Schlessinger, J.5
  • 36
    • 33847797485 scopus 로고
    • Nuclear magnetic resonance study of the solution structures of some crown ethers and their cation complexes
    • Live D, Chan SI. 1976. Nuclear magnetic resonance study of the solution structures of some crown ethers and their cation complexes. J Am Chem Soc 98:3769-3778.
    • (1976) J Am Chem Soc , vol.98 , pp. 3769-3778
    • Live, D.1    Chan, S.I.2
  • 37
    • 0024464461 scopus 로고
    • Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor
    • Manning MC, Woody RW. 1989. Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor. Biochemistry 28:8609-8613.
    • (1989) Biochemistry , vol.28 , pp. 8609-8613
    • Manning, M.C.1    Woody, R.W.2
  • 38
    • 0022449011 scopus 로고
    • Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange
    • Mas MT, Chen CY, Hitzeman RA, Riggs AD. 1986. Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange. Science 255:788-790.
    • (1986) Science , vol.255 , pp. 788-790
    • Mas, M.T.1    Chen, C.Y.2    Hitzeman, R.A.3    Riggs, A.D.4
  • 39
    • 0024295022 scopus 로고
    • Site-directed mutagenesis of histidine-388 in the hinge region of yeast 3-phosphoglycerate kinase: Effects of catalytic activity and activation by sulfate
    • Mas MT, Bailey JM, Resplandor ZE. 1988a. Site-directed mutagenesis of histidine-388 in the hinge region of yeast 3-phosphoglycerate kinase: Effects of catalytic activity and activation by sulfate. Biochemistry 27:1168-1172.
    • (1988) Biochemistry , vol.27 , pp. 1168-1172
    • Mas, M.T.1    Bailey, J.M.2    Resplandor, Z.E.3
  • 40
    • 0023808530 scopus 로고
    • Structure-function relationships in 3-phospho-glycerate kinase: Role of the carboxy-terminal peptide
    • Mas MT, Resplandor ZE. 1988b. Structure-function relationships in 3-phospho-glycerate kinase: Role of the carboxy-terminal peptide. Proteins Struct Funct Genet 4:56-62.
    • (1988) Proteins Struct Funct Genet , vol.4 , pp. 56-62
    • Mas, M.T.1    Resplandor, Z.E.2
  • 41
    • 0029045962 scopus 로고
    • Effects of C-terminal deletions on the conformational state and denaturation of phosphoglycerate kinase
    • Mas MT, Chen HH, Aisaka K, Lin LN, Brandts JF. 1995. Effects of C-terminal deletions on the conformational state and denaturation of phosphoglycerate kinase. Biochemistry 54:7391-7940.
    • (1995) Biochemistry , vol.54 , pp. 7391-7940
    • Mas, M.T.1    Chen, H.H.2    Aisaka, K.3    Lin, L.N.4    Brandts, J.F.5
  • 42
    • 0030095921 scopus 로고    scopus 로고
    • 2.0 Å resolution structure of a ternary complex of pig muscle phosphoglycerate kinase containing 3-phospho-D-glycerate and the nucleotide Mn adenylylimidodiphosphate
    • May A, Vas M, Harlos K, Blake C. 1996. 2.0 Å resolution structure of a ternary complex of pig muscle phosphoglycerate kinase containing 3-phospho-D-glycerate and the nucleotide Mn adenylylimidodiphosphate. Proteins Struct Funct Genet 24:292-303.
    • (1996) Proteins Struct Funct Genet , vol.24 , pp. 292-303
    • May, A.1    Vas, M.2    Harlos, K.3    Blake, C.4
  • 43
    • 0029946037 scopus 로고    scopus 로고
    • Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate
    • McPhillips TM, Hsu BT, Sherman MA, Mas MT, Rees DC. 1996. Structure of the R65Q mutant of yeast 3-phosphoglycerate kinase complexed with Mg-AMP-PNP and 3-phospho-D-glycerate. Biochemistry 35:4118-4127.
    • (1996) Biochemistry , vol.35 , pp. 4118-4127
    • McPhillips, T.M.1    Hsu, B.T.2    Sherman, M.A.3    Mas, M.T.4    Rees, D.C.5
  • 44
    • 0024743903 scopus 로고
    • Efficient expression and characterization of isolated structural domains of yeast phosphoglycerate kinase generated by site-directed mutagenesis
    • Minard P, Hall L, Betton JM, Missiakas D, Yon JM. 1989. Efficient expression and characterization of isolated structural domains of yeast phosphoglycerate kinase generated by site-directed mutagenesis. Protein Eng 3:55-60.
    • (1989) Protein Eng , vol.3 , pp. 55-60
    • Minard, P.1    Hall, L.2    Betton, J.M.3    Missiakas, D.4    Yon, J.M.5
  • 45
    • 0025079267 scopus 로고
    • Unfolding-refolding of the domains in yeast phosphoglycerate kinase: Comparison with the isolated engineered domains
    • Missiakas D, Betton JM, Minard P, Yon JM. 1990. Unfolding-refolding of the domains in yeast phosphoglycerate kinase: Comparison with the isolated engineered domains. Biochemistry 29:8683-8689.
    • (1990) Biochemistry , vol.29 , pp. 8683-8689
    • Missiakas, D.1    Betton, J.M.2    Minard, P.3    Yon, J.M.4
  • 46
    • 0028205462 scopus 로고
    • Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3
    • Munro AW, Lindsay JG, Coggin JR, Kelly SM, Price NC. 1994. Structural and enzymological analysis of the interaction of isolated domains of cytochrome P-450 BM3. FEBS Lett 343:70-14.
    • (1994) FEBS Lett , vol.343 , pp. 70-114
    • Munro, A.W.1    Lindsay, J.G.2    Coggin, J.R.3    Kelly, S.M.4    Price, N.C.5
  • 48
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T. 1995. How to measure and predict the molar absorption coefficient of a protein Protein Sci 4:2411-2423.
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 49
    • 0028925982 scopus 로고
    • The expression in E. coli and purification of isolated non-thioredoxin-like domains of human
    • Parry JW, Clark JR, Tuite MF, Freedman RB. 1995. The expression in E. coli and purification of isolated non-thioredoxin-like domains of human PDL. Biochem Soc Trans 23:71S.
    • (1995) PDL. Biochem Soc Trans , vol.23
    • Parry, J.W.1    Clark, J.R.2    Tuite, M.F.3    Freedman, R.B.4
  • 51
    • 0029365465 scopus 로고
    • Backbone assignment, secondary structure and protein a binding of an isolated, human antibody VH domain
    • Riechmann L, Davies J. 1995. Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain. J Biomol NMR 6:141-52.
    • (1995) J Biomol NMR , vol.6 , pp. 141-152
    • Riechmann, L.1    Davies, J.2
  • 53
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method: Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method: Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27:8063-8063.
    • (1988) Biochemistry , vol.27 , pp. 8063-8063
    • Santoro, M.M.1    Bolen, D.W.2
  • 54
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman JA. 1978. Solvent denaturation. Biopolymers 17:1305-1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 55
    • 0001428018 scopus 로고
    • L conformation at the ends of helices
    • Jaenicke R, ed. Amsterdam: Elsevier
    • L conformation at the ends of helices. In: Jaenicke R, ed. Protein folding. Amsterdam: Elsevier. pp 53-61.
    • (1980) Protein Folding , pp. 53-61
    • Schellman, C.1
  • 58
    • 0027049247 scopus 로고
    • Characterization of the structure and properties of the His 62 → Ala and Arg 38 → Ala mutants of yeast phosphoglycerate kinase: An investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR
    • Sherman MA, Fairbrother WJ, Mas MT. 1992. Characterization of the structure and properties of the His 62 → Ala and Arg 38 → Ala mutants of yeast phosphoglycerate kinase: An investigation of the catalytic and activatory sites by site-directed mutagenesis and NMR. Protein Sci 1:752-760.
    • (1992) Protein Sci , vol.1 , pp. 752-760
    • Sherman, M.A.1    Fairbrother, W.J.2    Mas, M.T.3
  • 59
    • 0028841922 scopus 로고
    • Probing intradomain and interdomain conformational changes during equilibrium unfolding of phosphoglycerate kinase: Fluorescence and circular dichroism study of tryptophan mutants
    • Sherman MA, Beechem JM, Mas MT. 1995. Probing intradomain and interdomain conformational changes during equilibrium unfolding of phosphoglycerate kinase: Fluorescence and circular dichroism study of tryptophan mutants. Biochemistry 34:13934-13942.
    • (1995) Biochemistry , vol.34 , pp. 13934-13942
    • Sherman, M.A.1    Beechem, J.M.2    Mas, M.T.3
  • 60
    • 0025301090 scopus 로고
    • Probing the role of arginines and histidines in the catalytic function and activation of yeast 3-phosphoglycerate kinase by site-directed mutagenesis
    • Sherman MA, Szpikowska BK, Dean SA, Mathiowetz AM, McQueen NL, Mas MT. 1990. Probing the role of arginines and histidines in the catalytic function and activation of yeast 3-phosphoglycerate kinase by site-directed mutagenesis. J Biol Chem 265:10659-10665.
    • (1990) J Biol Chem , vol.265 , pp. 10659-10665
    • Sherman, M.A.1    Szpikowska, B.K.2    Dean, S.A.3    Mathiowetz, A.M.4    McQueen, N.L.5    Mas, M.T.6
  • 61
    • 0028198619 scopus 로고
    • Equilibrium unfolding of yeast phosphoglycerate kinase and its mutants lacking one or both native tryptophans: A circular dichroism and steady-state and time-resolved fluorescence study
    • Szpikowska BK, Beechem JM, Sherman MA, Mas MT. 1994. Equilibrium unfolding of yeast phosphoglycerate kinase and its mutants lacking one or both native tryptophans: A circular dichroism and steady-state and time-resolved fluorescence study. Biochemistry 33:2217-2225.
    • (1994) Biochemistry , vol.33 , pp. 2217-2225
    • Szpikowska, B.K.1    Beechem, J.M.2    Sherman, M.A.3    Mas, M.T.4
  • 62
    • 0020520185 scopus 로고
    • Amino and carboxy-terminal regions in globular proteins
    • Thornton JM, Sibanda BL. 1983. Amino and carboxy-terminal regions in globular proteins. J Mol Biol 167:443-460.
    • (1983) J Mol Biol , vol.167 , pp. 443-460
    • Thornton, J.M.1    Sibanda, B.L.2
  • 63
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky VN. 1993. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32:13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 65
    • 0028913410 scopus 로고
    • Structure of the isolated catalytic domain of diphtheria toxin
    • Weiss MS, Blanke SR, Collier RJ, Eisenberg D. 1995. Structure of the isolated catalytic domain of diphtheria toxin. Biochemistry 34:773-781.
    • (1995) Biochemistry , vol.34 , pp. 773-781
    • Weiss, M.S.1    Blanke, S.R.2    Collier, R.J.3    Eisenberg, D.4
  • 66
    • 0015597839 scopus 로고
    • Nucleation, rapid folding and globular intrachain regions in proteins
    • Wetlaufer DB. 1973. Nucleation, rapid folding and globular intrachain regions in proteins. Proc Natl Acad Sci USA 70:697-701.
    • (1973) Proc Natl Acad Sci USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.