메뉴 건너뛰기




Volumn 37, Issue 3, 1999, Pages 441-453

The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures

Author keywords

Hydrophobicity; Hyperthermophile; Psychrophile; Salt bridges; Thermophile

Indexed keywords

AMINO ACID; PHOSPHOGLYCERATE KINASE; TRIOSEPHOSPHATE ISOMERASE;

EID: 0032709104     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991115)37:3<441::AID-PROT11>3.0.CO;2-7     Document Type: Article
Times cited : (135)

References (65)
  • 1
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R, Böhm G. The stability of proteins in extreme environments. Curr Opin Struct Biol 1998;8:738-748.
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 2
    • 0032521220 scopus 로고    scopus 로고
    • Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium
    • Russell RJM, Gerike U, Danson MJ, Hough DW, Taylor GL. Structural adaptations of the cold-active citrate synthase from an Antarctic bacterium. Structure 1998;6:351-361.
    • (1998) Structure , vol.6 , pp. 351-361
    • Russell, R.J.M.1    Gerike, U.2    Danson, M.J.3    Hough, D.W.4    Taylor, G.L.5
  • 3
    • 0031941134 scopus 로고    scopus 로고
    • Triose-phophate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus
    • Alvarez M, Zeelen JP, Mainfroid V, et al. Triose-phophate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. J Biol Chem 1998;273:2199-2206.
    • (1998) J Biol Chem , vol.273 , pp. 2199-2206
    • Alvarez, M.1    Zeelen, J.P.2    Mainfroid, V.3
  • 4
    • 0032534759 scopus 로고    scopus 로고
    • Structure of the psychrophilic Alteromonas haloplanctisα-amylase give insight into cold adaptation at a molecular level
    • Aghajari N, Feller G, Gerday C, Haser R. Structure of the psychrophilic Alteromonas haloplanctisα-amylase give insight into cold adaptation at a molecular level. Structure 1998;6:1503-1516.
    • (1998) Structure , vol.6 , pp. 1503-1516
    • Aghajari, N.1    Feller, G.2    Gerday, C.3    Haser, R.4
  • 5
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational characteristics related to thermostability
    • Querol E, Perez-Pons JA, Mozo-Villarias A. Analysis of protein conformational characteristics related to thermostability. Protein Eng. 1996;9:265-271.
    • (1996) Protein Eng. , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 6
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins:Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke R, Schurig H, Beaucamp N, Ostendorp R. Structure and stability of hyperstable proteins:glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Adv Protein Chem 1996;48:181-269.
    • (1996) Adv Protein Chem , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 7
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing
    • Voght G, Argos P. Protein thermal stability: hydrogen bonds or internal packing. Folding Design 1997;2:S40-S46.
    • (1997) Folding Design , vol.2
    • Voght, G.1    Argos, P.2
  • 9
    • 0027242141 scopus 로고
    • Structure of the open and closed state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
    • Noble MEM, Zeelen JP, Wierenga RK. Structure of the open and closed state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism. Proteins 1993;16:311-326.
    • (1993) Proteins , vol.16 , pp. 311-326
    • Noble, M.E.M.1    Zeelen, J.P.2    Wierenga, R.K.3
  • 10
    • 0025015392 scopus 로고
    • Anatomy of a conformational change: Hinged "lid" motion of the triose phosphate isomerase loop
    • Joseph D, Petsko GA, Karplus M. Anatomy of a conformational change: Hinged "lid" motion of the triose phosphate isomerase loop. Science 1990;249:1425-1428.
    • (1990) Science , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 11
    • 0030055827 scopus 로고    scopus 로고
    • Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies
    • Schliebs W, Thanki, N, Eritja R, Wierenga R. Active site properties of monomeric triosephosphate isomerase (monoTIM) as deduced from mutational and structural studies. Protein Sci 1996;5:229-239.
    • (1996) Protein Sci , vol.5 , pp. 229-239
    • Schliebs, W.1    Thanki, N.2    Eritja, R.3    Wierenga, R.4
  • 12
    • 0016810498 scopus 로고
    • Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 Å resolution
    • Banner DW, Bloomer AC, Petsko GA, et al. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 Å resolution. Nature 1975;255:609-614.
    • (1975) Nature , vol.255 , pp. 609-614
    • Banner, D.W.1    Bloomer, A.C.2    Petsko, G.A.3
  • 13
    • 0026519169 scopus 로고
    • Comparison of the refined crystal structures of liganded and the unliganded chicken, yeast and trypanosomal triosephosphate isomerase
    • Wierenga RK, Noble MEM, Davenport RC. Comparison of the refined crystal structures of liganded and the unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J Mol Biol 1992;224:1115-1126.
    • (1992) J Mol Biol , vol.224 , pp. 1115-1126
    • Wierenga, R.K.1    Noble, M.E.M.2    Davenport, R.C.3
  • 15
    • 0025785056 scopus 로고
    • Refined 1.83Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4M-ammonium sulphate
    • Wierenga RK, Noble MEM, Vriend G, Nauche S, Hol WGJ. Refined 1.83Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4M-ammonium sulphate. J Mol Biol 1991;220:995-1015.
    • (1991) J Mol Biol , vol.220 , pp. 995-1015
    • Wierenga, R.K.1    Noble, M.E.M.2    Vriend, G.3    Nauche, S.4    Hol, W.G.J.5
  • 16
    • 0000400122 scopus 로고
    • Structure of triosephosphate isomerase from Escherichia coli determined at 2.6Å resolution
    • Noble MEM, Zeelen JP, Wierenga RK. Structure of triosephosphate isomerase from Escherichia coli determined at 2.6Å resolution. Acta Crystallogr 1993;D49:403-417.
    • (1993) Acta Crystallogr , vol.D49 , pp. 403-417
    • Noble, M.E.M.1    Zeelen, J.P.2    Wierenga, R.K.3
  • 17
    • 0028298146 scopus 로고
    • Crystal structure of recombinant human triosphosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme
    • Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WGJ. Crystal structure of recombinant human triosphosphate isomerase at 2.8 Å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci 1994;3:810-821.
    • (1994) Protein Sci , vol.3 , pp. 810-821
    • Mande, S.C.1    Mainfroid, V.2    Kalk, K.H.3    Goraj, K.4    Martial, J.A.5    Hol, W.G.J.6
  • 18
    • 0031570683 scopus 로고    scopus 로고
    • Triosephosphate isomerase from Plasmodium falciparum: The crystal structure provides insights into antimalarial drug design
    • Velanker SS, Ray SS, Gokhale RS, Hemalatha Balaram SS, Murthy MRN. Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. Structure 1997;5:751-761.
    • (1997) Structure , vol.5 , pp. 751-761
    • Velanker, S.S.1    Ray, S.S.2    Gokhale, R.S.3    Hemalatha Balaram, S.S.4    Murthy, M.R.N.5
  • 19
    • 0032929094 scopus 로고    scopus 로고
    • Structural and mutational studies of leishmania triosephosphate isomerase: A point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power
    • Williams JC, Zeelen JP, Neubauer G, Vriend G, Backmann J, Michels PA, Lambeir AM, Wierenga RK. Structural and mutational studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Prot Eng 1999;12:243.
    • (1999) Prot Eng , vol.12 , pp. 243
    • Williams, J.C.1    Zeelen, J.P.2    Neubauer, G.3    Vriend, G.4    Backmann, J.5    Michels, P.A.6    Lambeir, A.M.7    Wierenga, R.K.8
  • 20
    • 0032538281 scopus 로고    scopus 로고
    • Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes
    • Maldonado E, Soriano-Garcia M, Moreno A, et al. Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes. J Mol Biol 1998;283:193-203.
    • (1998) J Mol Biol , vol.283 , pp. 193-203
    • Maldonado, E.1    Soriano-Garcia, M.2    Moreno, A.3
  • 21
    • 0028846686 scopus 로고
    • Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions
    • Delboni LF, Mande SC, Rentier-Delrue F, et al. Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions. Protein Sci 1995;4: 2594-2604.
    • (1995) Protein Sci , vol.4 , pp. 2594-2604
    • Delboni, L.F.1    Mande, S.C.2    Rentier-Delrue, F.3
  • 22
    • 0028819196 scopus 로고
    • PGK and TIM from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex
    • Schurig H, Beaucamp N, Ostendorp R, Jaenicke R, Adler E, Knowles JR. PGK and TIM from the hyperthermophilic bacterium Thermotoga maritima form a covalent bifunctional enzyme complex. EMBO J 1995;14:442-452.
    • (1995) EMBO J , vol.14 , pp. 442-452
    • Schurig, H.1    Beaucamp, N.2    Ostendorp, R.3    Jaenicke, R.4    Adler, E.5    Knowles, J.R.6
  • 23
    • 0030850229 scopus 로고    scopus 로고
    • Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: Design and characterization of the separate triosephosphate isomerase
    • Beaucamp N, Hofmann A, Kellerer B, Jaenicke R. Dissection of the gene of the bifunctional PGK-TIM fusion protein from the hyperthermophilic bacterium Thermotoga maritima: design and characterization of the separate triosephosphate isomerase Protein Sci 1997;6:2159-2165.
    • (1997) Protein Sci , vol.6 , pp. 2159-2165
    • Beaucamp, N.1    Hofmann, A.2    Kellerer, B.3    Jaenicke, R.4
  • 24
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis DA. Equilibrium ultracentrifugation of dilute solutions. Biochemistry 1994;3:297-317.
    • (1994) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 1994;D50: 760-763.
    • (1994) Acta Crystallogr D , vol.D50 , pp. 760-763
  • 27
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navazza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr 1994;A50:157-163.
    • (1994) Acta Crystallogr , vol.A50 , pp. 157-163
    • Navazza, J.1
  • 28
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density amps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjelgaard M. Improved methods for building protein models in electron density amps and the location of errors in these models. Acta Crystallogr 1991;A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 30
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brünger AT, Adams PD, Clore MG, et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D 1998;D54:905-921.
    • (1998) Acta Crystallogr D , vol.D54 , pp. 905-921
    • Brünger, A.T.1    Adams, P.D.2    Clore, M.G.3
  • 32
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990;8:52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 33
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 1984;12:387-395.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 34
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 35
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • Richardson JS, Richardson DC. Amino acid preferences for specific locations at the ends of a helices. Science 1988;240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 36
    • 33845377446 scopus 로고
    • Computation of molecular volume
    • Connolly ML. Computation of molecular volume. J Am Chem Soc 1985;107:1118-1124.
    • (1985) J Am Chem Soc , vol.107 , pp. 1118-1124
    • Connolly, M.L.1
  • 37
    • 0003742069 scopus 로고
    • Department of Biochemistry and Molecular Biology, University College, London
    • Hubbard SJ, Thornton JM. NACCESS [computer program]. Department of Biochemistry and Molecular Biology, University College, London; 1993.
    • (1993) NACCESS [Computer Program]
    • Hubbard, S.J.1    Thornton, J.M.2
  • 38
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I, Thornton J. Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994;238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.1    Thornton, J.2
  • 41
    • 0020484055 scopus 로고
    • Partial specific volume changes of proteins: Densimetric studies
    • Durchschlag H, Jaenicke R. Partial specific volume changes of proteins: densimetric studies. Biochem Biophys Res Commun 1982;108:1074-1079.
    • (1982) Biochem Biophys Res Commun , vol.108 , pp. 1074-1079
    • Durchschlag, H.1    Jaenicke, R.2
  • 42
    • 0029976451 scopus 로고    scopus 로고
    • Tetrameric triosephosphate isomerase from hyperthermophilic Archaea
    • Kohlhoff M, Dahm A, Hensel R. Tetrameric triosephosphate isomerase from hyperthermophilic Archaea. FEBS Lett 1996;383: 245-250.
    • (1996) FEBS Lett , vol.383 , pp. 245-250
    • Kohlhoff, M.1    Dahm, A.2    Hensel, R.3
  • 43
    • 0032213899 scopus 로고    scopus 로고
    • Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei
    • Bell GS, Russell RJM, Kohlhoff M, et al. Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei. Acta Crystallogr 1998;D54:1419-1421.
    • (1998) Acta Crystallogr , vol.D54 , pp. 1419-1421
    • Bell, G.S.1    Russell, R.J.M.2    Kohlhoff, M.3
  • 44
    • 0343170500 scopus 로고
    • Dramatic thermostabilisation of yeast iso-1-cytochrome c by an asparagine => isoleucine replacement at position 57
    • Das G, Hickey DR, McLendon D, McLendon G, Sherman F. Dramatic thermostabilisation of yeast iso-1-cytochrome c by an asparagine => isoleucine replacement at position 57. Proc Nat. Acad Sci USA 1989;86:496-499.
    • (1989) Proc Nat. Acad Sci USA , vol.86 , pp. 496-499
    • Das, G.1    Hickey, D.R.2    McLendon, D.3    McLendon, G.4    Sherman, F.5
  • 46
    • 0031952431 scopus 로고    scopus 로고
    • Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability
    • Usher KC, de la Cruz AFA, Dahlquist FW, Swanson RV, Simon MI, Remington SJ. Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability. Protein Sci 1998;7:403-412.
    • (1998) Protein Sci , vol.7 , pp. 403-412
    • Usher, K.C.1    De La Cruz, A.F.A.2    Dahlquist, F.W.3    Swanson, R.V.4    Simon, M.I.5    Remington, S.J.6
  • 47
    • 0028014604 scopus 로고
    • Relevance of sequence statistics for the properties of extremophilic proteins
    • Böhm G, Jaenicke R. Relevance of sequence statistics for the properties of extremophilic proteins. Int J Pept Protein Res 1994;43:97-106.
    • (1994) Int J Pept Protein Res , vol.43 , pp. 97-106
    • Böhm, G.1    Jaenicke, R.2
  • 48
    • 0023430560 scopus 로고
    • Enhanced thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews BW, Nicholson H, Becktel WJ. Enhanced thermostability from site-directed mutations that decrease the entropy of unfolding. Proc Natl Acad Sci USA 1987;84:6663-6667.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 49
    • 0029099960 scopus 로고
    • Engineering thermostability: Lessons from thermophilic proteins
    • Russell RJM, Taylor GL. Engineering thermostability: lessons from thermophilic proteins. Curr Opin Biotech 1995;9:370-374.
    • (1995) Curr Opin Biotech , vol.9 , pp. 370-374
    • Russell, R.J.M.1    Taylor, G.L.2
  • 50
    • 0030781507 scopus 로고    scopus 로고
    • Insights into thermal resistance of proteins from intrinsic stability of their α-helices
    • Petukhov L, Kil Y, Kuramitsu S, Lanzov V. Insights into thermal resistance of proteins from intrinsic stability of their α-helices. Proteins 1997;29:309-320.
    • (1997) Proteins , vol.29 , pp. 309-320
    • Petukhov, L.1    Kil, Y.2    Kuramitsu, S.3    Lanzov, V.4
  • 51
    • 0031686238 scopus 로고    scopus 로고
    • Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study
    • Facchiano AM, Colonna G, Ragone R. Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study. Protein Eng 1998;11:753-760.
    • (1998) Protein Eng , vol.11 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 52
    • 0024273441 scopus 로고
    • Enhanced protein thermostability from designed mutations that interact with α-helix dipoles
    • Nicholson H, Becktel W, Matthews BW. Enhanced protein thermostability from designed mutations that interact with α-helix dipoles. Nature 1988;336:651-656.
    • (1988) Nature , vol.336 , pp. 651-656
    • Nicholson, H.1    Becktel, W.2    Matthews, B.W.3
  • 53
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • Serrano L, Fersht AR. Capping and α-helix stability. Nature 1989;342:296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 54
    • 0030855080 scopus 로고    scopus 로고
    • Stabilization of protein structures
    • Lee B, Vasmatzis G. Stabilization of protein structures. Curr Opin Struct Biol 1997;8:423-428.
    • (1997) Curr Opin Struct Biol , vol.8 , pp. 423-428
    • Lee, B.1    Vasmatzis, G.2
  • 55
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. Dominant forces in protein folding. Biochemistry 1990;29: 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 56
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg D, McLachlan AD. Solvation energy in protein folding and binding. Nature 1986;319:199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 57
    • 0027980359 scopus 로고
    • Molecular basis of cooperativity in protein folding. Thermodynamic and structural conditions for the stabilization of compact denatured states
    • Xie D, Freire E. Molecular basis of cooperativity in protein folding. Thermodynamic and structural conditions for the stabilization of compact denatured states. Proteins 1994;19:291-301.
    • (1994) Proteins , vol.19 , pp. 291-301
    • Xie, D.1    Freire, E.2
  • 58
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat BI, Mayo SL. Protein design automation. Protein Sci 1996;5:895-903.
    • (1996) Protein Sci , vol.5 , pp. 895-903
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 59
    • 0344073971 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of unfolding of the trimeric adenylate kinase from the archeon Sulfolobus acidocaldarius
    • Backmann J, Schäfer G, Wyns L, Bönisch H. Thermodynamics and kinetics of unfolding of the trimeric adenylate kinase from the archeon Sulfolobus acidocaldarius. J Mol Biol 1998;284:817-833.
    • (1998) J Mol Biol , vol.284 , pp. 817-833
    • Backmann, J.1    Schäfer, G.2    Wyns, L.3    Bönisch, H.4
  • 60
    • 0029936488 scopus 로고    scopus 로고
    • Determinants of enzyme thermostability observed in the molecular structure of Thermus aquatus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5Å resolution
    • Tanner JT, Hecht RM, Krause KL. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquatus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5Å resolution. Biochemistry 1996;35:2597-2609.
    • (1996) Biochemistry , vol.35 , pp. 2597-2609
    • Tanner, J.T.1    Hecht, R.M.2    Krause, K.L.3
  • 61
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz MF, Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature 1975;255: 256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 62
    • 0029176320 scopus 로고
    • How to make my blood boil
    • Goldman A. How to make my blood boil. Structure 1995;3:1277-1279.
    • (1995) Structure , vol.3 , pp. 1277-1279
    • Goldman, A.1
  • 63
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • Yip KSP, Stillman TJ, Britton KL, et al. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 1995;3:1147-1158.
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.P.1    Stillman, T.J.2    Britton, K.L.3
  • 64
    • 0032514678 scopus 로고    scopus 로고
    • Protein thermostability above 100°C: A key role for ionic interactions
    • Vetriani C, Maeder DL, Tolliday N, et al. Protein thermostability above 100°C: a key role for ionic interactions. Proc Natl Acad Sci USA 1998;95:12300-12305.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12300-12305
    • Vetriani, C.1    Maeder, D.L.2    Tolliday, N.3
  • 65
    • 0022631926 scopus 로고
    • The folding type of a protein is relevant to the amino acid composition
    • Nakashima H, Nishikwa K, Ooi T. The folding type of a protein is relevant to the amino acid composition. J Biochem 1986;99:153-162.
    • (1986) J Biochem , vol.99 , pp. 153-162
    • Nakashima, H.1    Nishikwa, K.2    Ooi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.