메뉴 건너뛰기




Volumn 60, Issue 1, 2005, Pages 36-45

Hydration of protein-protein interfaces

Author keywords

Crystal packing; Hydrogen bonds; Interface water; Protein protein recognition; Specific and nonspecific interactions

Indexed keywords

ARGININE; ASPARTIC ACID; CARBONYL DERIVATIVE; GLUTAMIC ACID; HOMODIMERIC PROTEIN; PROTEIN; UNCLASSIFIED DRUG; WATER;

EID: 19544372768     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20478     Document Type: Article
Times cited : (198)

References (65)
  • 1
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution
    • Huber R, Kukla D, Bode W, Schwager P, Bartels K, Deisenhofer J, Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution. J Mol Biol 1974;89:73-101.
    • (1974) J Mol Biol , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Deisenhofer, J.6    Steigemann, W.7
  • 2
    • 0017257628 scopus 로고
    • Stability and specificity of protein-protein interactions: The case of the trypsin-trypsin inhibitor complexes
    • Janin J, Chothia C. Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes. J Mol Biol 1976;100:197-211.
    • (1976) J Mol Biol , vol.100 , pp. 197-211
    • Janin, J.1    Chothia, C.2
  • 3
    • 0024278949 scopus 로고
    • Distributions of water around amino acid residues in proteins
    • Thanki N, Thornton JM, Goodfellow JM. Distributions of water around amino acid residues in proteins. J Mol Biol 1988;202:637-657.
    • (1988) J Mol Biol , vol.202 , pp. 637-657
    • Thanki, N.1    Thornton, J.M.2    Goodfellow, J.M.3
  • 4
    • 0025025407 scopus 로고
    • Influence of secondary structure on the hydration of serine, threonine and tyrosine residues in proteins
    • Thanki N, Thornton JM, Goodfellow JM. Influence of secondary structure on the hydration of serine, threonine and tyrosine residues in proteins. Protein Eng 1990;3:495-508.
    • (1990) Protein Eng , vol.3 , pp. 495-508
    • Thanki, N.1    Thornton, J.M.2    Goodfellow, J.M.3
  • 5
    • 0025834829 scopus 로고
    • Analysis of protein main-chain solvation as a function of secondary structure
    • Thanki N, Umrania Y, Thornton JM, Goodfellow JM. Analysis of protein main-chain solvation as a function of secondary structure. J Mol Biol 1991;221:669-691.
    • (1991) J Mol Biol , vol.221 , pp. 669-691
    • Thanki, N.1    Umrania, Y.2    Thornton, J.M.3    Goodfellow, J.M.4
  • 6
    • 0029089271 scopus 로고
    • Significance of bound water to local chain conformations in protein crystals
    • Robert CH, Ho PS. Significance of bound water to local chain conformations in protein crystals. Proc Natl Acad Sci USA 1995;92: 7600-7604.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7600-7604
    • Ch, R.1    Ho, P.S.2
  • 9
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S, Thornton JM. Principles of protein-protein interactions. Proc Natl Acad Sci USA 1996;93:13-20.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 10
    • 0029109468 scopus 로고
    • Protein-protein interactions: A survey of protein dimer structures
    • Jones S, Thornton JM. Protein-protein interactions: a survey of protein dimer structures. Prog Biophys Mol Biol 1995;63:31-65.
    • (1995) Prog Biophys Mol Biol , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 11
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L, Chothia C, Janin J. The atomic structure of protein-protein recognition sites. J Mol Biol 1999;285:2177-2198.
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 12
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis for molecular recognition
    • Wodak SJ, Janin J. Structural basis for molecular recognition. Adv Prot Chem 2002;61:9-73.
    • (2002) Adv Prot Chem , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 13
    • 0037093645 scopus 로고    scopus 로고
    • Dissecting protein-protein recognition sites
    • Chakrabarti P, Janin J. Dissecting protein-protein recognition sites. Proteins 2002;47:334-343.
    • (2002) Proteins , vol.47 , pp. 334-343
    • Chakrabarti, P.1    Janin, J.2
  • 14
    • 0242299201 scopus 로고    scopus 로고
    • Dissecting subunit interfaces in homodimeric proteins
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J. Dissecting subunit interfaces in homodimeric proteins. Proteins 2003;53:708-719.
    • (2003) Proteins , vol.53 , pp. 708-719
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 15
    • 0029586759 scopus 로고
    • Protein-protein interaction at crystal contacts
    • Janin J, Rodier F. Protein-protein interaction at crystal contacts. Proteins 1995;23:580-587.
    • (1995) Proteins , vol.23 , pp. 580-587
    • Janin, J.1    Rodier, F.2
  • 16
    • 0031297461 scopus 로고    scopus 로고
    • Specific vs non-specific contacts in protein crystals
    • Janin J. Specific vs non-specific contacts in protein crystals. Nature Struct Biol 1997;4:973-974.
    • (1997) Nature Struct Biol , vol.4 , pp. 973-974
    • Janin, J.1
  • 17
    • 0030850230 scopus 로고    scopus 로고
    • Protein-protein crystal-packing contacts
    • Carugo O, Argos P. Protein-protein crystal-packing contacts. Protein Sci 1997;6:2261-2263.
    • (1997) Protein Sci , vol.6 , pp. 2261-2263
    • Carugo, O.1    Argos, P.2
  • 18
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • Dasgupta S, Iyer GH, Bryant SH, Lawrence CE, Bell JA. Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers. Proteins 1997;28:494-514.
    • (1997) Proteins , vol.28 , pp. 494-514
    • Dasgupta, S.1    Iyer, G.H.2    Bryant, S.H.3    Lawrence, C.E.4    Bell, J.A.5
  • 19
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl H, Henrick K, Thornton JM. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins 2000;41:47-57.
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 20
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J. A dissection of specific and non-specific protein-protein interfaces. J Mol Biol 2004;336:943-955.
    • (2004) J Mol Biol , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 21
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971;55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 22
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp K, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3
  • 23
    • 0030831990 scopus 로고    scopus 로고
    • Structure-based analysis of catalysis and substrate definition in the HIT protein family
    • Lima CD, Klein MG. Hendrickson WA. Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science 1997;278:286-290.
    • (1997) Science , vol.278 , pp. 286-290
    • Lima, C.D.1    Klein, M.G.2    Hendrickson, W.A.3
  • 24
    • 0037459095 scopus 로고    scopus 로고
    • The oligomeric states of Haloarcida marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies
    • Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccaï G, Vellieux FMD. The oligomeric states of Haloarcida marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. J Mol Biol 2003;326:859-873.
    • (2003) J Mol Biol , vol.326 , pp. 859-873
    • Irimia, A.1    Ebel, C.2    Madern, D.3    Richard, S.B.4    Cosenza, L.W.5    Zaccaï, G.6    Fmd, V.7
  • 25
    • 0022801412 scopus 로고
    • X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor
    • Bode W, Wei AZ, Huber R, Meyer E, Travis J, Neumann S. X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor. EMBO J 1986;5:2453-2458.
    • (1986) EMBO J , vol.5 , pp. 2453-2458
    • Bode, W.1    Wei, A.Z.2    Huber, R.3    Meyer, E.4    Travis, J.5    Neumann, S.6
  • 26
    • 0030589635 scopus 로고    scopus 로고
    • Substrate mimicry in the active center of a mammalian alpha-amylase: Structural analysis of an enzyme-inhibitor complex
    • Bompard-Gilles C, Rousseau P, Rouge P, Payan F. Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex. Structure 1996;4:1441-1452.
    • (1996) Structure , vol.4 , pp. 1441-1452
    • Bompard-Gilles, C.1    Rousseau, P.2    Rouge, P.3    Payan, F.4
  • 28
    • 0035165846 scopus 로고    scopus 로고
    • Cooperative zinc binding in a sea mutant mimics the SEA-MHC class II interaction
    • Hakansson M, Antonsson P, Bjork P, Svensson LA. Cooperative zinc binding in a sea mutant mimics the SEA-MHC class II interaction. J Biol Inorg Chem 2001;6:757-762.
    • (2001) J Biol Inorg Chem , vol.6 , pp. 757-762
    • Hakansson, M.1    Antonsson, P.2    Bjork, P.3    Svensson, L.A.4
  • 29
  • 30
    • 0033572790 scopus 로고    scopus 로고
    • Wet and dry interfaces: The role of solvent in protein-protein and protein-DNA recognition
    • Janin J. Wet and dry interfaces: the role of solvent in protein-protein and protein-DNA recognition. Structure 1999;7:R277-R279.
    • (1999) Structure , vol.7
    • Janin, J.1
  • 31
    • 0028607523 scopus 로고
    • Cavities and packing at protein interfaces
    • Hubbard SJ, Argos P. Cavities and packing at protein interfaces. Protein Sci 1994;3:2194-2206.
    • (1994) Protein Sci , vol.3 , pp. 2194-2206
    • Hubbard, S.J.1    Argos, P.2
  • 32
    • 0031439702 scopus 로고    scopus 로고
    • Analysis of temperature factor distribution in high-resolution protein structures
    • Parthasarathy S, Murthy MRN. Analysis of temperature factor distribution in high-resolution protein structures. Protein Sci 1997;6:2561-2567.
    • (1997) Protein Sci , vol.6 , pp. 2561-2567
    • Parthasarathy, S.1    Murthy, M.R.N.2
  • 33
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald IK, Thornton JM. Satisfying hydrogen bonding potential in proteins. J Mol Biol 1994;238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 34
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D, Tsai CJ, Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 1997;10:999-1012.
    • (1997) Protein Eng , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 35
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D, Lin SL, Nussinov R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J Mol Biol 1997;265:68-84.
    • (1997) J Mol Biol , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 36
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • Chothia C, Janin J. Principles of protein-protein recognition. Nature 1975;256:705-708.
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 37
    • 0025261918 scopus 로고
    • Solvent effects on protein association and protein folding
    • Ben-Naim A. Solvent effects on protein association and protein folding. Biopolymers 1990;29:567-596.
    • (1990) Biopolymers , vol.29 , pp. 567-596
    • Ben-Naim, A.1
  • 38
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L, Jernigan RL, Covell DG. A role for surface hydrophobicity in protein-protein recognition. Protein Sci 1994;3:717-729.
    • (1994) Protein Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 39
    • 1842405464 scopus 로고    scopus 로고
    • Study of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai CJ, Lin SL, Wolfson HJ, Nussinov R. Study of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci 1997;6:53-64.
    • (1997) Protein Sci , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 40
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg EJ, Mariuzza RA. Molecular recognition in antibody-antigen complexes. Adv Prot Chem 2002;61:119-160.
    • (2002) Adv Prot Chem , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 42
    • 0029364787 scopus 로고
    • Conservation of water molecules in an antibody-antigen interaction
    • Braden BC, Fields BA, Poljak RJ. Conservation of water molecules in an antibody-antigen interaction. J Mol Recognit 1995;8: 317-325.
    • (1995) J Mol Recognit , vol.8 , pp. 317-325
    • Braden, B.C.1    Fields, B.A.2    Poljak, R.J.3
  • 44
    • 0029856410 scopus 로고    scopus 로고
    • Hydrogen bonding and solvent structure in an antigen-antibody interface: Crystal structures and thermodynamic characterization of three fv mutants complexed with lysozyme
    • Fields BA, Goldbaum FA, Dall'Acqua W, Malchiodi EL, Cauerhff A, Schwarz FP, Ysern X, Poljak RJ, Mariuzza RA. Hydrogen bonding and solvent structure in an antigen-antibody interface: crystal structures and thermodynamic characterization of three fv mutants complexed with lysozyme. Biochemistry 1996;35:15494-15503.
    • (1996) Biochemistry , vol.35 , pp. 15494-15503
    • Fields, B.A.1    Goldbaum, F.A.2    Dall'Acqua, W.3    Malchiodi, E.L.4    Cauerhff, A.5    Schwarz, F.P.6    Ysern, X.7    Poljak, R.J.8    Mariuzza, R.A.9
  • 45
    • 0031021982 scopus 로고    scopus 로고
    • Analysis of binding interactions in an idiotope-antiidiotope protein-protein complex by double mutant cycles
    • Goldman ER, Dall'Acqua W, Braden BC, Mariuzza RA. Analysis of binding interactions in an idiotope-antiidiotope protein-protein complex by double mutant cycles. Biochemistry 1997;36:49-56.
    • (1997) Biochemistry , vol.36 , pp. 49-56
    • Goldman, E.R.1    Dall'Acqua, W.2    Braden, B.C.3    Mariuzza, R.A.4
  • 47
    • 0028980629 scopus 로고
    • Structure of an antibody-lysozyme complex unexpected effect of a conservative mutation
    • Chacko D, Silverton E, Kam-Morgan L, Smith-Gill S, Cohen G, Davis D. Structure of an antibody-lysozyme complex unexpected effect of a conservative mutation. J Mol Biol 1995;245:261-274.
    • (1995) J Mol Biol , vol.245 , pp. 261-274
    • Chacko, D.1    Silverton, E.2    Kam-Morgan, L.3    Smith-Gill, S.4    Cohen, G.5    Davis, D.6
  • 48
    • 0028856716 scopus 로고
    • Water molecules participate in proteinase-inhibitor interactions: Crystal structure of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B
    • Huang K, Lu W, Anderson S, Laskowski MJ, James MNG. Water molecules participate in proteinase-inhibitor interactions: crystal structure of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B. Protein Sci 1995;4:1985-1997.
    • (1995) Protein Sci , vol.4 , pp. 1985-1997
    • Huang, K.1    Lu, W.2    Anderson, S.3    Laskowski, M.J.4    James, M.N.G.5
  • 49
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structure analysis of a barnase-barstar complex at 2.0 Å resolution
    • Buckle AM, Schreiber G, Fersht AR. Protein-protein recognition: crystal structure analysis of a barnase-barstar complex at 2.0 Å resolution. Biochemistry 1994;33:8878-8889.
    • (1994) Biochemistry , vol.33 , pp. 8878-8889
    • Buckle, A.M.1    Schreiber, G.2    Fersht, A.R.3
  • 50
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber G, Fersht AR. Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J Mol Biol 1995;248:478-486.
    • (1995) J Mol Biol , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 51
    • 0034283147 scopus 로고    scopus 로고
    • Specificity in protein-protein interactions: The structural basis for dual recognition in endonuclease colicin-immunity protein complexes
    • Kuhlmann UC, Pommer AJ, Moore GR, James R, Kleanthous C. Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes. J Mol Biol 2000;301:1163-1178.
    • (2000) J Mol Biol , vol.301 , pp. 1163-1178
    • Kuhlmann, U.C.1    Pommer, A.J.2    Moore, G.R.3    James, R.4    Kleanthous, C.5
  • 52
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. A hot spot of binding energy in a hormone-receptor interface. Science 1995;267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 53
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells JA. Binding in the growth hormone receptor complex. Proc Natl Acad Sci USA 1996;93:1-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 54
    • 3242797452 scopus 로고    scopus 로고
    • A detailed analysis of ras/effector complex interfaces
    • Kiel C, Serrano L, Herrmann C. A detailed analysis of ras/effector complex interfaces. J Mol Biol 2004;340:1039-1058.
    • (2004) J Mol Biol , vol.340 , pp. 1039-1058
    • Kiel, C.1    Serrano, L.2    Herrmann, C.3
  • 55
    • 0031556018 scopus 로고    scopus 로고
    • Analysis of protein-protein interactions and the effects of amino acid mutations on their energetics: The importance of water molecules in the binding epitope
    • Covell DG, Wallqvist A. Analysis of protein-protein interactions and the effects of amino acid mutations on their energetics: the importance of water molecules in the binding epitope. J Mol Biol 1997;269:281-297.
    • (1997) J Mol Biol , vol.269 , pp. 281-297
    • Covell, D.G.1    Wallqvist, A.2
  • 56
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • Guerois R, Nielsen JE, Serrano L. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J Mol Biol 2002;320:369-387.
    • (2002) J Mol Biol , vol.320 , pp. 369-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 57
    • 0037195144 scopus 로고    scopus 로고
    • A simple physical model for the binding energy hot spots in protein-protein complexes
    • Kortemme T, Baker D. A simple physical model for the binding energy hot spots in protein-protein complexes. Proc Natl Acad Sci USA 2002;99:14116-14121.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14116-14121
    • Kortemme, T.1    Baker, D.2
  • 58
    • 0042868638 scopus 로고    scopus 로고
    • Role of water-mediated interactions in protein-protein recognition landscapes
    • Papoian GA, Ulander J, Wolynes PG. Role of water-mediated interactions in protein-protein recognition landscapes. J Am Chem Soc 2003;125:9170-9178.
    • (2003) J Am Chem Soc , vol.125 , pp. 9170-9178
    • Papoian, G.A.1    Ulander, J.2    Wolynes, P.G.3
  • 59
    • 0027146064 scopus 로고
    • The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: The correct modelling of a eight-residue loop
    • Borchert TV, Abagyan R, Kishan KVR, Zeelen JP, Wierenga RK. The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of a eight-residue loop. Structure 1993;1:205-213.
    • (1993) Structure , vol.1 , pp. 205-213
    • Borchert, T.V.1    Abagyan, R.2    Kishan, K.V.R.3    Zeelen, J.P.4    Wierenga, R.K.5
  • 60
    • 0033614008 scopus 로고    scopus 로고
    • A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis
    • Bailey DL, Fraser ME, Bridger WA, James MN, Wolodko WT. A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis. J Mol Biol 1999;285:1655-1666.
    • (1999) J Mol Biol , vol.285 , pp. 1655-1666
    • Bailey, D.L.1    Fraser, M.E.2    Bridger, W.A.3    James, M.N.4    Wolodko, W.T.5
  • 61
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • Kelly CA, Nishiyama M, Ohnishi Y, Beppu T, Birktoft JJ. Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus. Biochemistry 1993;32:3913-3922.
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.A.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 62
    • 0030068478 scopus 로고    scopus 로고
    • Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis
    • Miller MD, Krause KL. Identification of the Serratia endonuclease dimer: structural basis and implications for catalysis. Protein Sci 1996;5:24-33.
    • (1996) Protein Sci , vol.5 , pp. 24-33
    • Miller, M.D.1    Krause, K.L.2
  • 63
    • 0036839243 scopus 로고    scopus 로고
    • The dimeric dihydroorotate dehydrogenase a from Lactococcus lactis dissociates reversibly into inactive monomers
    • Ottosen MB, Björnberg O, Nørager S, Larsen S, Palfey BA, Jensen KF. The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers. Protein Sci 2002;11:2575-2583.
    • (2002) Protein Sci , vol.11 , pp. 2575-2583
    • Ottosen, M.B.1    Björnberg, O.2    Nørager, S.3    Larsen, S.4    Palfey, B.A.5    Jensen, K.F.6
  • 64
    • 2942641889 scopus 로고    scopus 로고
    • Cluster analysis of water molecules in alanine racemase and their putative structural role
    • Mustat G, Briggs JM. Cluster analysis of water molecules in alanine racemase and their putative structural role. Protein Eng 2004;17:223-234.
    • (2004) Protein Eng , vol.17 , pp. 223-234
    • Mustat, G.1    Briggs, J.M.2
  • 65
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan AA, Thorn KS. Anatomy of hot spots in protein interfaces. J Mol Biol 1998;280:1-9.
    • (1998) J Mol Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.