메뉴 건너뛰기




Volumn 3695 LNBI, Issue , 2005, Pages 163-174

Detection of protein assemblies in crystals

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTALLOGRAPHY; CRYSTALS; ENTROPY; GRAPH THEORY; OLIGOMERS;

EID: 33646195686     PISSN: 03029743     EISSN: 16113349     Source Type: Book Series    
DOI: 10.1007/11560500_15     Document Type: Conference Paper
Times cited : (248)

References (28)
  • 2
    • 0032169688 scopus 로고    scopus 로고
    • PQS: A protein quaternary structure file server
    • Henrick, K. and Thornton, J.: PQS: a protein quaternary structure file server. Trends in Biochem.l Sci. 23 (1998) 358-361.
    • (1998) Trends in Biochem.l Sci. , vol.23 , pp. 358-361
    • Henrick, K.1    Thornton, J.2
  • 3
    • 0141669302 scopus 로고    scopus 로고
    • Automatic inference of protein quaternary structure from crystals
    • Ponstingl, H., Kabir, T. and Thornton, J.: 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.3
  • 4
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl, H., Henrick, K., and Thornton, J.: 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.3
  • 5
    • 2342491596 scopus 로고    scopus 로고
    • Common subgraph isomorphism detection by back-tracking search
    • Krissinel, E. and Henrick, K.: Common subgraph isomorphism detection by back-tracking search. Softw. Pract. Exper. 34 (2004) 591-607.
    • (2004) Softw. Pract. Exper. , vol.34 , pp. 591-607
    • Krissinel, E.1    Henrick, K.2
  • 7
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin, J., Miller, S., and Chothia, C.: Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204 (1988) 155-164.
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 8
    • 0024046505 scopus 로고
    • An investigation of protein subunit and domain interfaces
    • Argos, P.: An investigation of protein subunit and domain interfaces. Protein Eng. 2 (1988) 101-113.
    • (1988) Protein Eng. , vol.2 , pp. 101-113
    • Argos, P.1
  • 9
    • 0024846203 scopus 로고
    • The structure of interfaces between subunits ofdimeric and tetrameric proteins
    • Miller, S.: The structure of interfaces between subunits ofdimeric and tetrameric proteins. Protein Eng. 3 (1989) 77-83.
    • (1989) Protein Eng. , vol.3 , pp. 77-83
    • Miller, S.1
  • 10
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • Janin J. and Chothia, C.: The structure of protein-protein recognition sites, J. Biol. Chem. 265 (1990) 16027-16030.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16027-16030
    • Janin, J.1    Chothia, C.2
  • 11
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • Horton, N. and Lewis, M.: Calculation of the free energy of association for protein complexes. Protein Sci. 1 (1992) 169-181.
    • (1992) Protein Sci. , vol.1 , pp. 169-181
    • Horton, N.1    Lewis, M.2
  • 12
    • 0029586759 scopus 로고
    • Protein-protein interaction at crystal contacts
    • Janin, J. and Kodier, F.: Protein-protein interaction at crystal contacts. Proteins: Struc. Func. Genet. 23 (1995) 580-587.
    • (1995) Proteins: Struc. Func. Genet. , vol.23 , pp. 580-587
    • Janin, J.1    Kodier, F.2
  • 13
    • 0029109468 scopus 로고
    • Protein-protein interactions: A review of protein dimer structures
    • Jones, S. and Thornton, J.M.: 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
  • 14
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones, S. and Thornton, J.M.: Principles of protein-protein interactions. Proc. Natl. Acad. Sci. USA 93 (1996) 13-20.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 15
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu, D., Tsai, C.-J. and Nussinov, R.: Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Engng. 10 (1997) 999-1012.
    • (1997) Protein Engng. , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 16
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D. and McLachlan, A.D.: Solvation energy in protein folding and binding. Nature 319 (1986) 199-203.
    • (1986) Nature , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 17
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I. and Thornton J.: Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238 (1994) 777-93.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.1    Thornton, J.2
  • 18
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace C., Shirley B., McNutt M. and Gajiwala K.: Forces contributing to the conformational stability of proteins. FASEB J. 10 (1996) 75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.1    Shirley, B.2    McNutt, M.3    Gajiwala, K.4
  • 19
    • 33646195474 scopus 로고
    • The hydrogen bond in molecular recognition
    • Fersht A.: The hydrogen bond in molecular recognition. Trends Biochem. Sci. 12 (1987) 3214-3219.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 3214-3219
    • Fersht, A.1
  • 20
    • 0025663105 scopus 로고
    • Strength and cooperativity of contributions of surface salt bridges to protein stability
    • Horovitz A., Serrano L., Avron B., Bycroft M. and Fersht A.: Strength and cooperativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216 (1990) 1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.5
  • 21
    • 0025327584 scopus 로고
    • Protein stability and electrostatic interactions between solvent exposed charged side chains
    • Akke M. and Forsen S.: Protein stability and electrostatic interactions between solvent exposed charged side chains. Proteins: Struct. Funct. Genet. 8 (1990) 23-29.
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 23-29
    • Akke, M.1    Forsen, S.2
  • 22
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page, M.I. and Jencks, W.P.: Entropic Contributions to Rate Accelerations in Enzymic and Intramolecular Reactions and the Chelate Effect. Proc. Natl. Acad. Sci. USA 68 (1971) 1678-1683.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 24
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • Murray, C.W. and Verdonk, M.L.: The consequences of translational and rotational entropy lost by small molecules on binding to proteins. J. Comput.-Aided Mol. Design 16 (2002) 741-753.
    • (2002) J. Comput.-aided Mol. Design , vol.16 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 25
    • 0024745871 scopus 로고
    • The price of lost freedom: Entropy of bimolecular complex formation
    • Finkelstein, A.V. and Janin, J.: The price of lost freedom: entropy of bimolecular complex formation. Protein Eng. 3 (1989) 1-3.
    • (1989) Protein Eng. , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 26
    • 0000913277 scopus 로고    scopus 로고
    • Estimating the entropic cost of self-assembly of multiparticle hydrogen-bonded aggregates based on the cyanuric acidMelamine lattice
    • Mammen, J., Shakhnovich, E.I., Deutch, J.M. and Whitesides G.M.: Estimating the Entropic Cost of Self-Assembly of Multiparticle Hydrogen-Bonded Aggregates Based on the Cyanuric AcidMelamine Lattice. J. Org. Chem. 63 (1998) 3821-3830.
    • (1998) J. Org. Chem. , vol.63 , pp. 3821-3830
    • Mammen, J.1    Shakhnovich, E.I.2    Deutch, J.M.3    Whitesides, G.M.4
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.: The CCP4 Suite: Programs for Protein Crystallography. Acta Cryst. D 50 (1994) 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.