메뉴 건너뛰기




Volumn 77, Issue 7-8, 1995, Pages 497-505

Principles of protein-protein recognition from structure to thermodynamics

(1)  Janin, J a  

a CNRS   (France)

Author keywords

accessible surface area; protein protein interaction; random energy model; redox complexes; specificity entropy

Indexed keywords

ANTIGEN ANTIBODY COMPLEX; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; COMPUTER SIMULATION; CRYSTAL STRUCTURE; DISSOCIATION; ELECTRON TRANSPORT; ENTHALPY; ENTROPY; ENZYME INHIBITOR COMPLEX; HYDROGEN BOND; MOLECULAR MODEL; MOLECULAR RECOGNITION; OXIDATION REDUCTION REACTION; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 0028853544     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/0300-9084(96)88166-1     Document Type: Article
Times cited : (132)

References (43)
  • 1
    • 0016708122 scopus 로고
    • Principles of protein-protein recognition
    • (1975) Nature , vol.256 , pp. 705-708
    • Chothia1    Janin2
  • 2
    • 0025123333 scopus 로고
    • The structure of protein-protein recognition sites
    • (1990) J Biol Chem , vol.265 , pp. 16027-16030
    • Janin1    Chothia2
  • 3
    • 0028861437 scopus 로고
    • Elusive affinities
    • (1995) Proteins , vol.21 , pp. 30-39
    • Janin1
  • 6
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • (1973) J Mol Biol , vol.79 , pp. 351-371
    • Shrake1    Rupley2
  • 12
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxydase and cytochrome c
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier1    Kraut2
  • 15
    • 0026071385 scopus 로고
    • Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas purida at 30 Å resolution
    • (1991) Biochemistry , vol.30 , pp. 238-247
    • Mathews1    Chen2    Bellamy3
  • 17
    • 0028007253 scopus 로고
    • Molecular and structural basis of electron transfer in tetra- and octa-heme cytochromes
    • (1994) Biochimie , vol.76 , pp. 546-553
    • Czjzek1    Payan2    Haser3
  • 19
    • 0028280409 scopus 로고
    • Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody Hy-HEL5
    • (1994) Biochemistry , vol.33 , pp. 3584-3590
    • Hibbits1    Gill2    Willson3
  • 20
    • 0027942020 scopus 로고
    • Thermodynamics of ferredoxin binding to ferredoxin: NADP reductase and the role of water at the complex interface
    • (1994) Biochemistry , vol.33 , pp. 13321-13327
    • Jelesarov1    Bosshard2
  • 21
    • 0026511652 scopus 로고
    • Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding
    • (1992) J Mol Biol , vol.224 , pp. 715-723
    • Privalov1    Makharatadze2
  • 22
    • 23444450909 scopus 로고
    • Coupling of local folding to site specific binding of proteins to DNA
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar1    Record2
  • 24
    • 0024433591 scopus 로고
    • The photosynthetic reaction centers from the purple bacterium Rhodopseudomonas viridis
    • (1989) Science , vol.245 , pp. 1463-1474
    • Deisenhofer1    Michel2
  • 25
    • 0027938898 scopus 로고
    • Relationship between rate and free energy difference for electron transfer from cytochrome c to the reaction center in Rhodobacter sphaeroides
    • (1994) Biochemistry , vol.33 , pp. 13517-13523
    • Lin1    Williams2    Allen3    Mathis4
  • 26
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • (1992) Protein Sci , vol.1 , pp. 169-181
    • Horton1    Lewis2
  • 28
    • 0016352763 scopus 로고
    • Hydrophobic bonding and accessible surface area in proteins
    • (1974) Nature , vol.248 , pp. 338-339
    • Chothia1
  • 30
    • 4243861085 scopus 로고
    • Random energy model: an exactly solvable model of disordered systems
    • (1981) Phys Rev B , vol.24 , pp. 2613-2626
    • Derrida1
  • 32
    • 0025146274 scopus 로고
    • Implication of thermodynamics of protein folding for evolution of primary sequences
    • (1990) Nature , vol.346 , pp. 773-775
    • Shakhnovich1    Gutin2
  • 35
    • 0028319316 scopus 로고
    • Implications of the random characteristics of protein sequences for their three-dimensional structure
    • (1994) Curr Opin Struct Biol , vol.4 , pp. 422-428
    • Finkelstein1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.