메뉴 건너뛰기




Volumn 89, Issue 1, 2005, Pages 9-35

Morphological aspects of oligomeric protein structures

Author keywords

Crystal structure; Interface; Multimer; Oligomer; Protein

Indexed keywords


EID: 16844386953     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2004.07.010     Document Type: Review
Times cited : (66)

References (73)
  • 1
    • 0024046505 scopus 로고
    • An investigation of protein subunit and protein domain interfaces
    • P. Argos An investigation of protein subunit and protein domain interfaces Prot. Eng. 2 1988 101 113
    • (1988) Prot. Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 2
    • 0242299201 scopus 로고    scopus 로고
    • Dissecting subunit interfaces in homodimeric proteins
    • R.P. Bahadur, P. Chakrabarti, F. Rodier, and J. Janin Dissecting subunit interfaces in homodimeric proteins Proteins 53 2003 708 719
    • (2003) Proteins , vol.53 , pp. 708-719
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 3
    • 1042275583 scopus 로고    scopus 로고
    • A dissection of specific and non-specific protein-protein interfaces
    • R.P. Bahadur, P. Chakrabarti, F. Rodier, and J. Janin A dissection of specific and non-specific protein-protein interfaces J. Mol. Biol. 336 2004 943 955
    • (2004) J. Mol. Biol. , vol.336 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 4
    • 0033614008 scopus 로고    scopus 로고
    • A dimeric form of Escherichia coli succinyl-coa synthetase produced by site-directed mutagenesis
    • D.L. Bailey, M.E. Fraser, W.A. Bridger, M.N.G. James, and W.T. Wolodko A dimeric form of Escherichia coli succinyl-coa synthetase produced by site-directed mutagenesis J. Mol. Biol. 285 1999 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.G.4    Wolodko, W.T.5
  • 5
    • 0032893084 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999
    • A. Bairoch, and R. Apweiler The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999 Nucleic Acids Res. 27 1999 49 54
    • (1999) Nucleic Acids Res. , vol.27 , pp. 49-54
    • Bairoch, A.1    Apweiler, R.2
  • 9
    • 0031443249 scopus 로고    scopus 로고
    • Computer-based analysis of the binding steps in protein complex formation
    • D. Bray, and S. Lay Computer-based analysis of the binding steps in protein complex formation Proc. Natl. Acad. Sci. USA 94 1997 13493 13498
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13493-13498
    • Bray, D.1    Lay, S.2
  • 10
    • 0027231876 scopus 로고
    • Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis
    • D. Bray, R.B. Bourret, and M.I. Simon Computer simulation of the phosphorylation cascade controlling bacterial chemotaxis Mol. Biol. Cell 4 1994 469
    • (1994) Mol. Biol. Cell , vol.4 , pp. 469
    • Bray, D.1    Bourret, R.B.2    Simon, M.I.3
  • 11
    • 0030850230 scopus 로고    scopus 로고
    • Protein-protein crystal-packing contacts
    • O. Carugo, and P. Argos Protein-protein crystal-packing contacts Protein Sci. 6 1997 2261 2263
    • (1997) Protein Sci. , vol.6 , pp. 2261-2263
    • Carugo, O.1    Argos, P.2
  • 12
    • 0037093645 scopus 로고    scopus 로고
    • Dissecting protein-protein recognition sites
    • P. Chakrabarti, and J. Janin Dissecting protein-protein recognition sites Proteins 47 2002 334 343
    • (2002) Proteins , vol.47 , pp. 334-343
    • Chakrabarti, P.1    Janin, J.2
  • 14
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • C. Chothia Hydrophobic bonding and accessible surface area in proteins Nature (London) 248 1974 338 339
    • (1974) Nature (London) , vol.248 , pp. 338-339
    • Chothia, C.1
  • 15
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • C. Chothia, and J. Janin Principles of protein-protein recognition Nature 256 1975 705 708
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia, C.1    Janin, J.2
  • 16
    • 0015239530 scopus 로고
    • The quaternary structure of proteins composed of identical subunits
    • A.J. Cornish-Bowden, and D.E.J. Koshland The quaternary structure of proteins composed of identical subunits J. Biol. Chem. 246 1971 3092 3102
    • (1971) J. Biol. Chem. , vol.246 , pp. 3092-3102
    • Cornish-Bowden, A.J.1    Koshland, D.E.J.2
  • 17
    • 0030877077 scopus 로고    scopus 로고
    • Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers
    • S. Dasgupta, G.H. Iyer, S.H. Bryant, C.E. Lawrence, and J.A. Bell Extent and nature of contacts between protein molecules in crystal lattices and between subunits of protein oligomers Proteins 28 1997 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
  • 18
    • 0027944677 scopus 로고
    • Crystal structure of κbungarotoxin at 2.3-Å resolution
    • J.C. Dewan, G.A. Grant, and J.C. Sacchettini Crystal structure of κ -bungarotoxin at 2.3-Å resolution Biochemistry 33 1994 13147 13154
    • (1994) Biochemistry , vol.33 , pp. 13147-13154
    • Dewan, J.C.1    Grant, G.A.2    Sacchettini, J.C.3
  • 19
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • K.A. Dill Dominant forces in protein folding Biochemistry 29 1990 7133 7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 20
    • 0003530127 scopus 로고
    • Principles of Protein X-ray Crystallography
    • Springer, Berlin
    • Drenth, J., 1994. Principles of Protein X-ray Crystallography. Springer Advanced Texts in Chemistry. Springer, Berlin, p. 72.
    • (1994) Springer Advanced Texts in Chemistry , pp. 72
    • Drenth, J.1
  • 21
    • 0027457706 scopus 로고
    • SRS- an indexing and retrieval tool for flat file data libraries
    • T. Etzold, and P. Argos SRS- an indexing and retrieval tool for flat file data libraries Comput. Appl. Biosci. 9 1993 49 57
    • (1993) Comput. Appl. Biosci. , vol.9 , pp. 49-57
    • Etzold, T.1    Argos, P.2
  • 22
    • 0000484499 scopus 로고
    • Hydrophobic parameters π of amino acid side chains from the partitioning of n-acetyl-amino-acid amides
    • J.L. Fauchère, and V. Pliška Hydrophobic parameters π of amino acid side chains from the partitioning of n -acetyl-amino-acid amides Eur. J. Med. Chem. 18 1983 369 375
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchère, J.L.1    Pliška, V.2
  • 23
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • D.R. Flower The lipocalin protein family structure and function Biochem. J. 318 1996 1 14
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 25
    • 0014030843 scopus 로고
    • Symmetry of protein oligomers formed by isologous association
    • K.R. Hanson Symmetry of protein oligomers formed by isologous association J. Mol. Biol. 22 1966 405 409
    • (1966) J. Mol. Biol. , vol.22 , pp. 405-409
    • Hanson, K.R.1
  • 27
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • L. Holm, and C. Sander Mapping the protein universe Science 273 1996 595 602
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 29
    • 0025912338 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • S.J. Hubbard, S.F. Campbell, and J.M. Thornton The interpretation of protein structures estimation of static accessibility J. Mol. Biol. 220 1991 507 530
    • (1991) J. Mol. Biol. , vol.220 , pp. 507-530
    • Hubbard, S.J.1    Campbell, S.F.2    Thornton, J.M.3
  • 30
    • 0031297461 scopus 로고    scopus 로고
    • Specific vs. non-specific contacts in protein crystals
    • J. Janin Specific vs. non-specific contacts in protein crystals Nature Struct. Biol. 4 1997 973 974
    • (1997) Nature Struct. Biol. , vol.4 , pp. 973-974
    • Janin, J.1
  • 31
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • J. Janin, and C. Chothia The structure of protein-protein recognition sites J. Biol. Chem. 26 1990 16027 16030
    • (1990) J. Biol. Chem. , vol.26 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 32
    • 0029586759 scopus 로고
    • Protein-protein interaction at crystal contacts
    • J. Janin, and F. Rodier Protein-protein interaction at crystal contacts Proteins 23 1995 580 587
    • (1995) Proteins , vol.23 , pp. 580-587
    • Janin, J.1    Rodier, F.2
  • 33
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • S. Jones, and J.M. Thornton Protein-protein interactions a review of protein dimer structures Prog. Biophys. Molec. Biol. 63 1995 31 65
    • (1995) Prog. Biophys. Molec. Biol. , vol.63 , pp. 31-65
    • Jones, S.1    Thornton, J.M.2
  • 35
    • 0031565729 scopus 로고    scopus 로고
    • Analysis of protein-protein interaction sites using surface patches
    • S. Jones, and J.M. Thornton Analysis of protein-protein interaction sites using surface patches J. Mol. Biol. 272 1997 121 132
    • (1997) J. Mol. Biol. , vol.272 , pp. 121-132
    • Jones, S.1    Thornton, J.M.2
  • 36
    • 0031565725 scopus 로고    scopus 로고
    • Prediction of protein-protein interaction sites using patch analysis
    • S. Jones, and J.M. Thornton Prediction of protein-protein interaction sites using patch analysis J. Mol. Biol. 272 1997 133 143
    • (1997) J. Mol. Biol. , vol.272 , pp. 133-143
    • Jones, S.1    Thornton, J.M.2
  • 37
    • 16844386329 scopus 로고    scopus 로고
    • Protein domain interfaces: Characterization and comparison with oligomeric protein interfaces
    • S. Jones, A. Marin, and J.M. Thornton Protein domain interfaces characterization and comparison with oligomeric protein interfaces Prot. Eng. 272 2000 133 143
    • (2000) Prot. Eng. , vol.272 , pp. 133-143
    • Jones, S.1    Marin, A.2    Thornton, J.M.3
  • 38
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 39
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • W. Kauzmann Some factors in the interpretation of protein denaturation Adv. Prot. Chem. 14 1959 1 63
    • (1959) Adv. Prot. Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 42
    • 0026079134 scopus 로고
    • Distribution and complementarity of hydropathy in multisubunit proteins
    • A.P. Korn, and R.M. Burnett Distribution and complementarity of hydropathy in multisubunit proteins Proteins 9 1991 37 55
    • (1991) Proteins , vol.9 , pp. 37-55
    • Korn, A.P.1    Burnett, R.M.2
  • 43
    • 0032522670 scopus 로고    scopus 로고
    • Morphology of protein-protein interfaces
    • T. Larsen, A.J. Olson, and D.S. Goodsell Morphology of protein-protein interfaces Structure 6 1998 421 427
    • (1998) Structure , vol.6 , pp. 421-427
    • Larsen, T.1    Olson, A.J.2    Goodsell, D.S.3
  • 44
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • B. Lee, and F.M. Richards The interpretation of protein structures estimation of static accessibility J. Mol. Biol. 55 1971 379 400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 45
    • 0023010495 scopus 로고
    • Ricin subunit association: Thermodynamics and the role of the disulfide bond in toxicity
    • M.S. Lewis, and R.J. Youle Ricin subunit association thermodynamics and the role of the disulfide bond in toxicity J. Biol. Chem. 261 1986 11571 11577
    • (1986) J. Biol. Chem. , vol.261 , pp. 11571-11577
    • Lewis, M.S.1    Youle, R.J.2
  • 46
    • 0030997363 scopus 로고    scopus 로고
    • Hydrophobic patches on protein subunit interfaces: Characteristics and prediction
    • P. Lijnzaad, and P. Argos Hydrophobic patches on protein subunit interfaces characteristics and prediction Proteins 28 1997 333 343
    • (1997) Proteins , vol.28 , pp. 333-343
    • Lijnzaad, P.1    Argos, P.2
  • 47
    • 0030055023 scopus 로고    scopus 로고
    • Hydrophobic patches on the surfaces of protein structures
    • P. Lijnzaad, H.J.C. Berendsen, and P. Argos Hydrophobic patches on the surfaces of protein structures Proteins 25 1996 389 397
    • (1996) Proteins , vol.25 , pp. 389-397
    • Lijnzaad, P.1    Berendsen, H.J.C.2    Argos, P.3
  • 48
    • 0029906944 scopus 로고    scopus 로고
    • A method for detecting hydrophobic patches on protein surfaces
    • P. Lijnzaad, H.J.C. Berendsen, and P. Argos A method for detecting hydrophobic patches on protein surfaces Proteins 26 1996 192 203
    • (1996) Proteins , vol.26 , pp. 192-203
    • Lijnzaad, P.1    Berendsen, H.J.C.2    Argos, P.3
  • 49
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • L. Lo Conte, C. Chothia, and J. Janin The atomic structure of protein-protein recognition sites J. Mol. Biol. 185 1999 2177 2198
    • (1999) J. Mol. Biol. , vol.185 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 50
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein-protein interfaces
    • A.J. McCoy, V.C. Epa, and P.M. Colman Electrostatic complementarity at protein-protein interfaces J. Mol. Biol. 268 1997 570 584
    • (1997) J. Mol. Biol. , vol.268 , pp. 570-584
    • McCoy, A.J.1    Epa, V.C.2    Colman, P.M.3
  • 51
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • I.K. McDonald, and J.M. Thornton Satisfying hydrogen bonding potential in proteins J. Mol. Biol. 238 1994 777 793
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 52
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • S. Miller, A.M. Lesk, J. Janin, and C. Chothia The accessible surface area and stability of oligomeric proteins Nature 328 1987 834 836
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 53
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • J. Monod, J. Wyman, and J.-P. Changeux On the nature of allosteric transitions a plausible model J. Mol. Biol. 12 1965 88 118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 54
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • I.M.A. Nooren, and J.M. Thornton Diversity of protein-protein interactions EMBO J. 22 2003 3486 3492
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 55
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterization and functional significance of transient protein-protein interactions
    • I.M.A. Nooren, and J.M. Thornton Structural characterization and functional significance of transient protein-protein interactions J. Mol. Biol. 325 2003 991 1018
    • (2003) J. Mol. Biol. , vol.325 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 56
    • 0037229456 scopus 로고    scopus 로고
    • Analysing six types of protein-protein interfaces
    • Y. Ofran, and B. Rost Analysing six types of protein-protein interfaces J. Mol. Biol. 325 2003 377 387
    • (2003) J. Mol. Biol. , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 57
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • H. Ponstingl, K. Henrick, and J.M. Thornton Discriminating between homodimeric and monomeric proteins in the crystalline state Proteins 41 2000 47 57
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.M.3
  • 58
    • 0141669302 scopus 로고    scopus 로고
    • Automatic inference of protein quaternary structure from crystals
    • H. Ponstingl, T. Kabir, and J.M. Thornton Automatic inference of protein quaternary structure from crystals J. Appl. Cryst. 36 2003 1116 1122
    • (2003) J. Appl. Cryst. , vol.36 , pp. 1116-1122
    • Ponstingl, H.1    Kabir, T.2    Thornton, J.M.3
  • 59
    • 5344244656 scopus 로고    scopus 로고
    • R Foundation for Statistical Computing, Vienna, Austria, ISBN 3-900051-00-3.
    • R Development Core Team, 2004. R: a language and environment for statistical computing. R Foundation for Statistical Computing, Vienna, Austria, ISBN 3-900051-00-3. URL http://www.R-project.org.
    • (2004) R: A Language and Environment for Statistical Computing
  • 60
    • 0028009317 scopus 로고
    • High-resolution crystallographic analysis of a co-operative dimeric hemoglobin
    • W.E. Royer Jr. High-resolution crystallographic analysis of a co-operative dimeric hemoglobin J. Mol. Biol. 235 1994 657 681
    • (1994) J. Mol. Biol. , vol.235 , pp. 657-681
    • Royer Jr., W.E.1
  • 61
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • Y. Shamoo, and T.A. Steitz Building a replisome from interacting pieces sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex Cell 99 1999
    • (1999) Cell , vol.99
    • Shamoo, Y.1    Steitz, T.A.2
  • 62
    • 0017294711 scopus 로고
    • Accessible area, packing volumes and interaction surfaces of globular proteins
    • D.C. Teller Accessible area, packing volumes and interaction surfaces of globular proteins Nature 260 1976 729 731
    • (1976) Nature , vol.260 , pp. 729-731
    • Teller, D.C.1
  • 63
    • 0035831535 scopus 로고    scopus 로고
    • Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium
    • T.B. Topping, R.L. Woodbury, D.L. Diamond, S.J.S. Hardy, and L.L. Randall Direct demonstration that homotetrameric chaperone SecB undergoes a dynamic dimer-tetramer equilibrium J. Biol. Chem. 276 2001 7437 7441
    • (2001) J. Biol. Chem. , vol.276 , pp. 7437-7441
    • Topping, T.B.1    Woodbury, R.L.2    Diamond, D.L.3    Hardy, S.J.S.4    Randall, L.L.5
  • 64
    • 0029988383 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: Architectures and interactions in protein-protein interfaces and in protein cores
    • C.-J. Tsai, S.L. Lin, H.J. Wolfson, and R. Nussinov Studies of protein-protein interfaces architectures and interactions in protein-protein interfaces and in protein cores Crit. Rev. Biochem. Mol. Biol. 31 1996 127 152
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 127-152
    • Tsai, C.-J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 65
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • C.-J. Tsai, S.L. Lin, H.J. Wolfson, and R. Nussinov Studies of protein-protein interfaces a statistical analysis of the hydrophobic effect Protein Sci. 6 1997 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
  • 66
    • 0033516705 scopus 로고    scopus 로고
    • The packing density in proteins: Standard radii and volumes
    • J. Tsai, R. Taylor, C. Chothia, and M. Gerstein The packing density in proteins standard radii and volumes J. Mol. Biol. 290 1999 253 266
    • (1999) J. Mol. Biol. , vol.290 , pp. 253-266
    • Tsai, J.1    Taylor, R.2    Chothia, C.3    Gerstein, M.4
  • 67
    • 0017857244 scopus 로고
    • Occurrence of 'large' and 'small' forms of succinate thiokinase in diverse organisms
    • P.D.J. Weitzman, and H.A. Kinghorn Occurrence of 'large' and 'small' forms of succinate thiokinase in diverse organisms FEBS Lett. 88 1978 255 258
    • (1978) FEBS Lett. , vol.88 , pp. 255-258
    • Weitzman, P.D.J.1    Kinghorn, H.A.2
  • 68
    • 0036424666 scopus 로고    scopus 로고
    • Structural basis of macromolecular recognition
    • S.J. Wodak, and J. Janin Structural basis of macromolecular recognition Adv. Prot. Chem. 61 2002 9 73
    • (2002) Adv. Prot. Chem. , vol.61 , pp. 9-73
    • Wodak, S.J.1    Janin, J.2
  • 69
    • 0023055735 scopus 로고
    • Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-coA synthetases from porcine heart and Escherichia coli
    • W.T. Wolodko, C.M. Kay, and W.A. Bridger Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-coA synthetases from porcine heart and Escherichia coli Biochemistry 25 1986 5420 5425
    • (1986) Biochemistry , vol.25 , pp. 5420-5425
    • Wolodko, W.T.1    Kay, C.M.2    Bridger, W.A.3
  • 70
    • 0025194445 scopus 로고
    • 2.2 Å resolution structure analysis of two refined n-acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes
    • C.S. Wright 2.2 Å resolution structure analysis of two refined n -acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes J. Mol. Biol. 215 1990 635 651
    • (1990) J. Mol. Biol. , vol.215 , pp. 635-651
    • Wright, C.S.1
  • 71
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • H. Wu, J.W. Lustbader, Y. Liu, R.E. Canfield, and W.A. Hendrickson Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein Structure 2 1994 245 258
    • (1994) Structure , vol.2 , pp. 245-258
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 72
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • D. Xu, C.-J. Tsai, and R. Nussinov Hydrogen bonds and salt bridges across protein-protein interfaces Prot. Eng. 10 1997 999 1012
    • (1997) Prot. Eng. , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 73
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • L. Young, R.L. Jernigan, and D.G. Covell A role for surface hydrophobicity in protein-protein recognition Protein Sci. 3 1994 717 729
    • (1994) Protein Sci. , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.