메뉴 건너뛰기




Volumn 16, Issue 11, 2007, Pages 2317-2333

Protein reconstitution and three-dimensional domain swapping: Benefits and constraints of covalency

Author keywords

Cooperativity; Ligand binding; Metastability; Stability; Steric constraints

Indexed keywords

AMYLOID; POLYPEPTIDE;

EID: 35648930538     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.072985007     Document Type: Review
Times cited : (52)

References (117)
  • 1
    • 0030917908 scopus 로고    scopus 로고
    • Loss of translational entropy in binding, folding, and catalysis
    • Amzel, L.M. 1997. Loss of translational entropy in binding, folding, and catalysis. Proteins 28: 144-149.
    • (1997) Proteins , vol.28 , pp. 144-149
    • Amzel, L.M.1
  • 2
    • 0015240523 scopus 로고
    • Specific binding of 3 fragments of staphylococcal nuclease
    • Andria, G., Taniuchi, H., and Cone, J.L. 1971. Specific binding of 3 fragments of staphylococcal nuclease. J. Biol. Chem. 246: 7421-7428.
    • (1971) J. Biol. Chem , vol.246 , pp. 7421-7428
    • Andria, G.1    Taniuchi, H.2    Cone, J.L.3
  • 4
    • 0028204771 scopus 로고
    • Domain swapping - entangling alliances between proteins
    • Bennett, M.J., Choe, S., and Eisenberg, D. 1994. Domain swapping - entangling alliances between proteins. Proc. Natl. Acad. Sci. 91: 3127-3131.
    • (1994) Proc. Natl. Acad. Sci , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 5
    • 33646375442 scopus 로고    scopus 로고
    • Deposition diseases and 3D domain swapping
    • Bennett, M.J., Sawaya, M.R., and Eisenberg, D. 2006. Deposition diseases and 3D domain swapping. Structure 14: 811-824.
    • (2006) Structure , vol.14 , pp. 811-824
    • Bennett, M.J.1    Sawaya, M.R.2    Eisenberg, D.3
  • 6
    • 0035814792 scopus 로고    scopus 로고
    • Fragment complementation studies of protein stabilization by hydrophobic core residues
    • Berggard, T., Julenius, K., Ogard, A., Drakenberg, T., and Linse, S. 2001. Fragment complementation studies of protein stabilization by hydrophobic core residues. Biochemistry 40: 1257-1264.
    • (2001) Biochemistry , vol.40 , pp. 1257-1264
    • Berggard, T.1    Julenius, K.2    Ogard, A.3    Drakenberg, T.4    Linse, S.5
  • 9
    • 0031953508 scopus 로고    scopus 로고
    • Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/β(2)m heterodimer
    • Bouvier, M. and Wiley, D.C. 1998. Structural characterization of a soluble and partially folded class I major histocompatibility heavy chain/β(2)m heterodimer. Nat. Struct. Biol. 5: 377-384.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 377-384
    • Bouvier, M.1    Wiley, D.C.2
  • 11
    • 0242662169 scopus 로고    scopus 로고
    • A protein contortionist: Core mutations of GBI that induce dimerization and domain swapping
    • Byeon, I.J.L., Louis, J.M., and Gronenborn, A.M. 2003. A protein contortionist: Core mutations of GBI that induce dimerization and domain swapping. J. Mol. Biol. 334: 605.
    • (2003) J. Mol. Biol , vol.334 , pp. 605
    • Byeon, I.J.L.1    Louis, J.M.2    Gronenborn, A.M.3
  • 12
    • 0033733510 scopus 로고    scopus 로고
    • A systematic and general proteolytic method for defining structural and functional domains of proteins
    • Carey, J. 2000. A systematic and general proteolytic method for defining structural and functional domains of proteins. Methods Enzymol. 328: 499-514.
    • (2000) Methods Enzymol , vol.328 , pp. 499-514
    • Carey, J.1
  • 14
    • 33744494819 scopus 로고    scopus 로고
    • X-ray structure of a native calicivirus: Structural insights into antigenic diversity and host specificity
    • Chen, R., Neill, J.D., Estes, M.K., and Prasad, B.V.V. 2006. X-ray structure of a native calicivirus: Structural insights into antigenic diversity and host specificity. Proc. Natl. Acad. Sci. 103: 8048-8053.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 8048-8053
    • Chen, R.1    Neill, J.D.2    Estes, M.K.3    Prasad, B.V.V.4
  • 15
    • 0031956609 scopus 로고    scopus 로고
    • Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system
    • Chu, V., Freitag, S., Le Trong, I., Stenkamp, R.E., and Stayton, P.S. 1998. Thermodynamic and structural consequences of flexible loop deletion by circular permutation in the streptavidin-biotin system. Protein Sci. 7: 848-859.
    • (1998) Protein Sci , vol.7 , pp. 848-859
    • Chu, V.1    Freitag, S.2    Le Trong, I.3    Stenkamp, R.E.4    Stayton, P.S.5
  • 16
    • 33746911627 scopus 로고    scopus 로고
    • Dynamic coupling and allosteric behavior in a nonallosteric protein
    • Clarkson, M.W., Gilmore, S.A., Edgell, M.H., and Lee, A.L. 2006. Dynamic coupling and allosteric behavior in a nonallosteric protein. Biochemistry 45: 7693-7699.
    • (2006) Biochemistry , vol.45 , pp. 7693-7699
    • Clarkson, M.W.1    Gilmore, S.A.2    Edgell, M.H.3    Lee, A.L.4
  • 18
    • 35649006428 scopus 로고
    • The design of molecular hosts, guests, and their complexes
    • The Nobel Foundation, Stockholm, Sweden
    • Cram, D.J. 1987. The design of molecular hosts, guests, and their complexes. Nobel lecture. The Nobel Foundation, Stockholm, Sweden. http://nobelprize.org/nobel_prizes/chemistry/laureates/1987/cram-lecture.html.
    • (1987) Nobel lecture
    • Cram, D.J.1
  • 19
    • 0030986375 scopus 로고    scopus 로고
    • Protein alchemy: Changing β-sheet into α-helix
    • Dalal, S., Balasubramanian, S., and Regan, L. 1997. Protein alchemy: Changing β-sheet into α-helix. Nat. Struct. Biol. 4: 548-552.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 548-552
    • Dalal, S.1    Balasubramanian, S.2    Regan, L.3
  • 20
    • 0029995708 scopus 로고    scopus 로고
    • Association of complementary fragments and the elucidation of protein folding pathways
    • de Prat-Gay, G. 1996. Association of complementary fragments and the elucidation of protein folding pathways. Protein Eng. 9: 843-847.
    • (1996) Protein Eng , vol.9 , pp. 843-847
    • de Prat-Gay, G.1
  • 21
    • 0027994709 scopus 로고
    • The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: Implications for mechanisms of protein folding
    • de Prat-Gay, G., Ruiz-Sanz, J., Davis, B., and Fersht, A.R. 1994. The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: Implications for mechanisms of protein folding. Proc. Natl. Acad. Sci. 91: 10943-10946.
    • (1994) Proc. Natl. Acad. Sci , vol.91 , pp. 10943-10946
    • de Prat-Gay, G.1    Ruiz-Sanz, J.2    Davis, B.3    Fersht, A.R.4
  • 22
    • 0029904020 scopus 로고    scopus 로고
    • Solution structure of an ATP-binding RNA aptamer reveals a novel fold
    • Dieckmann, T., Suzuki, E., Nakamura, G.K., and Feigon, J. 1996. Solution structure of an ATP-binding RNA aptamer reveals a novel fold. RNA 2: 628-640.
    • (1996) RNA , vol.2 , pp. 628-640
    • Dieckmann, T.1    Suzuki, E.2    Nakamura, G.K.3    Feigon, J.4
  • 23
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C.M. 1999. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24: 329-332.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 24
    • 27644468373 scopus 로고    scopus 로고
    • High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement
    • Dutta, S., Batori, V., Koide, A., and Koide, S. 2005. High-affinity fragment complementation of a fibronectin type III domain and its application to stability enhancement. Protein Sci. 14: 2838-2848
    • (2005) Protein Sci , vol.14 , pp. 2838-2848
    • Dutta, S.1    Batori, V.2    Koide, A.3    Koide, S.4
  • 25
    • 0035856521 scopus 로고    scopus 로고
    • High affinity RNase S-peptide variants obtained by phage display have a novel "hot-spot" of binding energy
    • Dwyer, J.J., Dwyer, M.A., and Kossiakoff, A.A. 2001. High affinity RNase S-peptide variants obtained by phage display have a novel "hot-spot" of binding energy. Biochemistry 40: 13491-13500.
    • (2001) Biochemistry , vol.40 , pp. 13491-13500
    • Dwyer, J.J.1    Dwyer, M.A.2    Kossiakoff, A.A.3
  • 26
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H.J. and Wright, P.E. 2002. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12: 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 27
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J. and Wright, P.E. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6: 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 28
    • 0030052426 scopus 로고    scopus 로고
    • Ekiel, I. and Abrahamson, M. 1996. Folding-related dimerization of human cystatin C. J. Biol. Chem. 271: 1314-1321.
    • Ekiel, I. and Abrahamson, M. 1996. Folding-related dimerization of human cystatin C. J. Biol. Chem. 271: 1314-1321.
  • 29
    • 0026509036 scopus 로고
    • A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene
    • Eriksson, A.E., Baase, W.A., Wozniak, J.A., and Matthews, B.W. 1992. A cavity-containing mutant of T4 lysozyme is stabilized by buried benzene. Nature 355: 371-373.
    • (1992) Nature , vol.355 , pp. 371-373
    • Eriksson, A.E.1    Baase, W.A.2    Wozniak, J.A.3    Matthews, B.W.4
  • 30
    • 0026772739 scopus 로고
    • A study of core domains, and the core domain domain interaction of cytochrome-C fragment-complex
    • Fisher, A. and Taniuchi, H. 1992. A study of core domains, and the core domain domain interaction of cytochrome-C fragment-complex. Arch. Biochem. Biophys. 296: 1-16.
    • (1992) Arch. Biochem. Biophys , vol.296 , pp. 1-16
    • Fisher, A.1    Taniuchi, H.2
  • 32
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P.G.W. 2002. Serpin structure, mechanism, and function. Chem. Rev. 102: 4751-4803.
    • (2002) Chem. Rev , vol.102 , pp. 4751-4803
    • Gettins, P.G.W.1
  • 33
    • 0029859408 scopus 로고    scopus 로고
    • Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase
    • Graf, R. and Schachman, H.K. 1996. Random circular permutation of genes and expressed polypeptide chains: Application of the method to the catalytic chains of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. 93: 11591-11596.
    • (1996) Proc. Natl. Acad. Sci , vol.93 , pp. 11591-11596
    • Graf, R.1    Schachman, H.K.2
  • 34
    • 0029978002 scopus 로고    scopus 로고
    • AV77 hinge mutation stabilizes the helix-turn-helix domain of trp repressor
    • Gryk, M.R. and Jardetzky, O. 1996. AV77 hinge mutation stabilizes the helix-turn-helix domain of trp repressor. J. Mol. Biol. 255: 204-214.
    • (1996) J. Mol. Biol , vol.255 , pp. 204-214
    • Gryk, M.R.1    Jardetzky, O.2
  • 35
    • 0030598361 scopus 로고    scopus 로고
    • Disallowed Ramachandran conformations of amino acid residues in protein structures
    • Gunasekaran, K., Ramakrishnan, C., and Balaram, P. 1996. Disallowed Ramachandran conformations of amino acid residues in protein structures. J. Mol. Biol. 264: 191-198.
    • (1996) J. Mol. Biol , vol.264 , pp. 191-198
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 36
    • 6344219895 scopus 로고    scopus 로고
    • Is allostery an intrinsic property of all dynamic proteins?
    • Gunasekaran, K., Ma, B.Y., and Nussinov, R. 2004. Is allostery an intrinsic property of all dynamic proteins? Proteins 57: 433-443.
    • (2004) Proteins , vol.57 , pp. 433-443
    • Gunasekaran, K.1    Ma, B.Y.2    Nussinov, R.3
  • 37
    • 33744497267 scopus 로고    scopus 로고
    • Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I
    • Guo, Z.F. and Eisenberg, D. 2006. Runaway domain swapping in amyloid-like fibrils of T7 endonuclease I. Proc. Natl. Acad. Sci. 103: 8042-8047.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 8042-8047
    • Guo, Z.F.1    Eisenberg, D.2
  • 38
    • 0015501543 scopus 로고
    • Reactivation of des (119-124, 120-124, or 121-124) ribonuclease-a by mixture with synthetic COOH-terminal peptides of varying lengths
    • Gutte, B., Lin, M.C., Caldi, D.G., and Merrifield, R.B. 1972. Reactivation of des (119-124, 120-124, or 121-124) ribonuclease-a by mixture with synthetic COOH-terminal peptides of varying lengths. J. Biol. Chem. 247: 4763-4767.
    • (1972) J. Biol. Chem , vol.247 , pp. 4763-4767
    • Gutte, B.1    Lin, M.C.2    Caldi, D.G.3    Merrifield, R.B.4
  • 39
    • 0036803980 scopus 로고    scopus 로고
    • The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity?
    • Håkansson, K. 2002. The strand-helix motif is a recurring theme in biological hydrolysis. Does the conformation of the Ramachandran outlier enhance its electrophilicity? Int. J. Biol. Macromol. 30: 273-277.
    • (2002) Int. J. Biol. Macromol , vol.30 , pp. 273-277
    • Håkansson, K.1
  • 40
    • 0017337750 scopus 로고
    • Formation of a biologically active, ordered complex from 2 overlapping fragments of cytochrome c
    • Hantgan, R.R. and Taniuchi, H. 1977. Formation of a biologically active, ordered complex from 2 overlapping fragments of cytochrome c. J. Biol. Chem. 252: 1367-1374.
    • (1977) J. Biol. Chem , vol.252 , pp. 1367-1374
    • Hantgan, R.R.1    Taniuchi, H.2
  • 41
    • 0030989408 scopus 로고    scopus 로고
    • Three-dimensional domain duplication, swapping and stealing
    • Heringa, J. and Taylor, W.R. 1997. Three-dimensional domain duplication, swapping and stealing. Curr. Opin. Struct. Biol. 7: 416-421.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 416-421
    • Heringa, J.1    Taylor, W.R.2
  • 44
    • 0027419166 scopus 로고
    • Stress and strain in staphylococcal nuclease
    • Hodel, A., Kautz, R.A., Jacobs, M.D., and Fox, R.O. 1993. Stress and strain in staphylococcal nuclease. Protein Sci. 2: 838-850.
    • (1993) Protein Sci , vol.2 , pp. 838-850
    • Hodel, A.1    Kautz, R.A.2    Jacobs, M.D.3    Fox, R.O.4
  • 45
    • 33645957777 scopus 로고
    • Thioredoxin-C′ - reconstitution of an active form of Escherichia coli thioredoxin from 2 noncovalently linked cyanogen bromide peptide fragments
    • Holmgren, A. 1972. Thioredoxin-C′ - reconstitution of an active form of Escherichia coli thioredoxin from 2 noncovalently linked cyanogen bromide peptide fragments. FEBS Lett. 24: 351-354.
    • (1972) FEBS Lett , vol.24 , pp. 351-354
    • Holmgren, A.1
  • 46
    • 0036890333 scopus 로고    scopus 로고
    • Protein reconstitution and 3D domain swapping
    • Håkansson, M. and Linse, S. 2002. Protein reconstitution and 3D domain swapping. Curr. Protein Pept. Sci. 3: 629-642.
    • (2002) Curr. Protein Pept. Sci , vol.3 , pp. 629-642
    • Håkansson, M.1    Linse, S.2
  • 47
    • 0035055932 scopus 로고    scopus 로고
    • An extended hydrophobic core induces EF-hand swapping
    • Håkansson, M., Svensson, A., Fast, J., and Linse, S. 2001. An extended hydrophobic core induces EF-hand swapping. Protein Sci. 10: 927-933.
    • (2001) Protein Sci , vol.10 , pp. 927-933
    • Håkansson, M.1    Svensson, A.2    Fast, J.3    Linse, S.4
  • 48
    • 31944434700 scopus 로고    scopus 로고
    • Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality
    • Ikura, M. and Ames, J.B. 2006. Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: Two ways to promote multifunctionality. Proc. Natl. Acad. Sci. 103: 1159-1164.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 1159-1164
    • Ikura, M.1    Ames, J.B.2
  • 50
    • 0030433170 scopus 로고    scopus 로고
    • Protein dynamics and conformational transitions in allosteric proteins
    • Jardetzky, O. 1996. Protein dynamics and conformational transitions in allosteric proteins. Prog. Biophys. Mol. Biol. 65: 171-219.
    • (1996) Prog. Biophys. Mol. Biol , vol.65 , pp. 171-219
    • Jardetzky, O.1
  • 51
    • 0029946537 scopus 로고    scopus 로고
    • Structural basis of RNA folding and recognition in an AMP-RNA aptamer complex
    • Jiang, F., Kumar, R.A., Jones, R.A., and Patel, D.J. 1996. Structural basis of RNA folding and recognition in an AMP-RNA aptamer complex. Nature 382: 183-186.
    • (1996) Nature , vol.382 , pp. 183-186
    • Jiang, F.1    Kumar, R.A.2    Jones, R.A.3    Patel, D.J.4
  • 52
    • 0037093642 scopus 로고    scopus 로고
    • Coupling of ligand binding and dimerization of helix-loop-helix peptides: Spectroscopic and sedimentation analyses of calbindin D9k EF-hands
    • Julenius, K., Robblee, J., Thulin, E., Finn, B.E., Fairman, R., and Linse, S. 2002. Coupling of ligand binding and dimerization of helix-loop-helix peptides: Spectroscopic and sedimentation analyses of calbindin D9k EF-hands. Proteins 47: 323-333.
    • (2002) Proteins , vol.47 , pp. 323-333
    • Julenius, K.1    Robblee, J.2    Thulin, E.3    Finn, B.E.4    Fairman, R.5    Linse, S.6
  • 54
    • 0033555241 scopus 로고    scopus 로고
    • Structural organization in peptide fragments of cytochrome c by heme binding
    • Kang, X.S. and Carey, J. 1999. Structural organization in peptide fragments of cytochrome c by heme binding. J. Mol. Biol. 285: 463-468.
    • (1999) J. Mol. Biol , vol.285 , pp. 463-468
    • Kang, X.S.1    Carey, J.2
  • 55
    • 0030010605 scopus 로고    scopus 로고
    • Experimentally observed conformation-dependent geometry and hidden strain in proteins
    • Karplus, P.A. 1996. Experimentally observed conformation-dependent geometry and hidden strain in proteins. Protein Sci. 5: 1406-1420.
    • (1996) Protein Sci , vol.5 , pp. 1406-1420
    • Karplus, P.A.1
  • 56
    • 0024338385 scopus 로고
    • Redesigning a sweet protein: Increased stability and renaturability
    • Kim, S.H., Kang, C.H., Kim, R., Cho, J.M., Lee, Y.B., and Lee, T.K. 1989. Redesigning a sweet protein: Increased stability and renaturability. Protein Eng. 2: 571-575.
    • (1989) Protein Eng , vol.2 , pp. 571-575
    • Kim, S.H.1    Kang, C.H.2    Kim, R.3    Cho, J.M.4    Lee, Y.B.5    Lee, T.K.6
  • 58
    • 0012068955 scopus 로고
    • Conformational study on the IgG binding domain of protein G
    • Kobayashi, N., Endo, S., and Munekata, E. 1993. Conformational study on the IgG binding domain of protein G. Peptide Chem. 1992: 278-280.
    • (1993) Peptide Chem , vol.1992 , pp. 278-280
    • Kobayashi, N.1    Endo, S.2    Munekata, E.3
  • 59
    • 0029055171 scopus 로고
    • Complement assembly of 2 fragments of the streptococcal protein-G B1 domain in aqueous-solution
    • Kobayashi, N., Honda, S., Yoshii, H., Uedaira, H., and Munekata, E. 1995. Complement assembly of 2 fragments of the streptococcal protein-G B1 domain in aqueous-solution. FEBS Lett. 366: 99-103.
    • (1995) FEBS Lett , vol.366 , pp. 99-103
    • Kobayashi, N.1    Honda, S.2    Yoshii, H.3    Uedaira, H.4    Munekata, E.5
  • 60
    • 0025489873 scopus 로고
    • Complete amino acid sequence of the sweet protein monellin
    • Kohmura, M., Nio, N., and Ariyoshi, Y. 1990. Complete amino acid sequence of the sweet protein monellin. Agric. Biol. Chem. 54: 2219-2224.
    • (1990) Agric. Biol. Chem , vol.54 , pp. 2219-2224
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 61
    • 85007661605 scopus 로고
    • Solid-phase synthesis of crystalline monellin, a sweet protein
    • Kohmura, M., Nio, N., and Ariyoshi, Y. 1991. Solid-phase synthesis of crystalline monellin, a sweet protein. Agric. Biol. Chem. 55: 539-545.
    • (1991) Agric. Biol. Chem , vol.55 , pp. 539-545
    • Kohmura, M.1    Nio, N.2    Ariyoshi, Y.3
  • 62
    • 0028173096 scopus 로고
    • Glycine-85 of the Trp-repressor of Escherichia coli is important in forming the hydrophobic tryptophan binding pocket - Experimental and computational approaches
    • Komeiji, Y., Fujita, I., Honda, N., Tsutsui, M., Tamura, T., and Yamato, I. 1994. Glycine-85 of the Trp-repressor of Escherichia coli is important in forming the hydrophobic tryptophan binding pocket - Experimental and computational approaches. Protein Eng. 7: 1239-1247.
    • (1994) Protein Eng , vol.7 , pp. 1239-1247
    • Komeiji, Y.1    Fujita, I.2    Honda, N.3    Tsutsui, M.4    Tamura, T.5    Yamato, I.6
  • 64
    • 0026354773 scopus 로고
    • High-resolution structure of an oligomeric eye lens β-crystallin - loops, arches, linkers and interfaces in β-B2 dimer compared to a monomeric γ-crystallin
    • Lapatto, R., Nalini, V., Bax, B., Driessen, H., Lindley, P.F., Blundell, T.L., and Slingsby, C. 1991. High-resolution structure of an oligomeric eye lens β-crystallin - loops, arches, linkers and interfaces in β-B2 dimer compared to a monomeric γ-crystallin. J. Mol. Biol. 222: 1067-1083.
    • (1991) J. Mol. Biol , vol.222 , pp. 1067-1083
    • Lapatto, R.1    Nalini, V.2    Bax, B.3    Driessen, H.4    Lindley, P.F.5    Blundell, T.L.6    Slingsby, C.7
  • 65
    • 0027396670 scopus 로고
    • Protein folding - Whats the question?
    • Lattman, E.E. and Rose, G.D. 1993. Protein folding - Whats the question? Proc. Natl. Acad. Sci. 90: 439-441.
    • (1993) Proc. Natl. Acad. Sci , vol.90 , pp. 439-441
    • Lattman, E.E.1    Rose, G.D.2
  • 66
    • 2942587506 scopus 로고    scopus 로고
    • Lawson, C.L., Benoff, B., Berger, T., Berman, H.M., and Carey, J. 2004. E. coli trp forms a domain-swapped array in aqueous alcohol. Structure 12: 1099-1108.
    • Lawson, C.L., Benoff, B., Berger, T., Berman, H.M., and Carey, J. 2004. E. coli trp forms a domain-swapped array in aqueous alcohol. Structure 12: 1099-1108.
  • 67
    • 0030979555 scopus 로고    scopus 로고
    • Circular permutations of natural protein sequences: Structural evidence
    • Lindqvist, Y. and Schneider, G. 1997. Circular permutations of natural protein sequences: Structural evidence. Curr. Opin. Struct. Biol. 7: 422-427.
    • (1997) Curr. Opin. Struct. Biol , vol.7 , pp. 422-427
    • Lindqvist, Y.1    Schneider, G.2
  • 68
    • 0030726470 scopus 로고    scopus 로고
    • Domain organization of calbindin D(28k) as determined from the association of six synthetic EF-hand fragments
    • Linse, S., Thulin, E., Gifford, L.K., Radzewsky, D., Hagan, J., Wilk, R.R., and Akerfeldt, K.S. 1997. Domain organization of calbindin D(28k) as determined from the association of six synthetic EF-hand fragments. Protein Sci. 6: 2385-2396.
    • (1997) Protein Sci , vol.6 , pp. 2385-2396
    • Linse, S.1    Thulin, E.2    Gifford, L.K.3    Radzewsky, D.4    Hagan, J.5    Wilk, R.R.6    Akerfeldt, K.S.7
  • 69
    • 0036108484 scopus 로고    scopus 로고
    • 3D domain swapping: As domains continue to swap
    • Liu, Y. and Eisenberg, D. 2002. 3D domain swapping: As domains continue to swap. Protein Sci. 11: 1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 70
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Liu, Y.S., Gotte, G., Libonati, M., and Eisenberg, D. 2001. A domain-swapped RNase A dimer with implications for amyloid formation. Nat. Struct. Biol. 8: 211-214.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 211-214
    • Liu, Y.S.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 71
    • 0032584210 scopus 로고    scopus 로고
    • The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1 angstrom resolution
    • Liu, Y.S., Hart, P.J., Schlunegger, M.P., and Eisenberg, D. 1998. The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1 angstrom resolution. Proc. Natl. Acad. Sci. 95: 3437-3442.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 3437-3442
    • Liu, Y.S.1    Hart, P.J.2    Schlunegger, M.P.3    Eisenberg, D.4
  • 72
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao, B., Johansson, D.G.A., Hansson, G.C., and Hard, T. 2006. Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat. Struct. Mol. Biol. 13: 71-76.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 71-76
    • Macao, B.1    Johansson, D.G.A.2    Hansson, G.C.3    Hard, T.4
  • 73
    • 0028334097 scopus 로고
    • Decomposition of the free energy of a system in terms of specific interactions: Implications for theoretical and experimental studies
    • Mark, A.E. and van Gunsteren, W.F. 1994. Decomposition of the free energy of a system in terms of specific interactions: Implications for theoretical and experimental studies. J. Mol. Biol. 240: 167-176.
    • (1994) J. Mol. Biol , vol.240 , pp. 167-176
    • Mark, A.E.1    van Gunsteren, W.F.2
  • 74
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor, D.L. and Kim, P.S. 1996. Context-dependent secondary structure formation of a designed protein sequence. Nature 380: 730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor, D.L.1    Kim, P.S.2
  • 75
    • 0023036230 scopus 로고
    • The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability
    • Mitchinson, C. and Baldwin, R.L. 1986. The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability. Proteins 1: 23-33.
    • (1986) Proteins , vol.1 , pp. 23-33
    • Mitchinson, C.1    Baldwin, R.L.2
  • 77
    • 0030334851 scopus 로고    scopus 로고
    • Toward the complete structural characterization of a protein folding pathway: The structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleationcondensation mechanism
    • Neira, J.L., Davis, B., Ladurner, A.G., Buckle, A.M., Gay, G.D., and Fersht, A.R. 1996. Toward the complete structural characterization of a protein folding pathway: The structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleationcondensation mechanism. Fold. Des. 1: 189-208.
    • (1996) Fold. Des , vol.1 , pp. 189-208
    • Neira, J.L.1    Davis, B.2    Ladurner, A.G.3    Buckle, A.M.4    Gay, G.D.5    Fersht, A.R.6
  • 79
    • 0036468392 scopus 로고    scopus 로고
    • Protein folding and three-dimensional domain swapping: A strained relationship?
    • Newcomer, M.E. 2002. Protein folding and three-dimensional domain swapping: A strained relationship? Curr. Opin. Struct. Biol. 12: 48-53.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 48-53
    • Newcomer, M.E.1
  • 80
    • 2642567686 scopus 로고    scopus 로고
    • Nilsson, M., Wang, X., Rodziewicz-Motowidlo, S., Janowski, R., Lindstrom, V., Onnerfjord, P., Westermark, G., Grzonka, Z., Jaskolski, M., and Grubb, A. 2004. Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C - Use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C. J. Biol. Chem. 279: 24236-24245.
    • Nilsson, M., Wang, X., Rodziewicz-Motowidlo, S., Janowski, R., Lindstrom, V., Onnerfjord, P., Westermark, G., Grzonka, Z., Jaskolski, M., and Grubb, A. 2004. Prevention of domain swapping inhibits dimerization and amyloid fibril formation of cystatin C - Use of engineered disulfide bridges, antibodies, and carboxymethylpapain to stabilize the monomeric form of cystatin C. J. Biol. Chem. 279: 24236-24245.
  • 81
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of Ntn-hydrolases
    • Oinonen, C. and Rouvinen, J. 2000. Structural comparison of Ntn-hydrolases. Protein Sci. 9: 2329-2337.
    • (2000) Protein Sci , vol.9 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 83
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus, H. 2000. Protein splicing and related forms of protein autoprocessing. Annu. Rev. Biochem. 69: 447-496.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 447-496
    • Paulus, H.1
  • 84
    • 0034581622 scopus 로고    scopus 로고
    • Autonomous protein folding units
    • Peng, Z.Y. and Wu, L.C. 2000. Autonomous protein folding units. Adv. Protein Chem. 53: 1-46.
    • (2000) Adv. Protein Chem , vol.53 , pp. 1-46
    • Peng, Z.Y.1    Wu, L.C.2
  • 85
    • 33645101339 scopus 로고    scopus 로고
    • Protein splicing mechanisms and applications
    • Perler, F.B. 2006. Protein splicing mechanisms and applications. IUBMB Life 58: 63.
    • (2006) IUBMB Life , vol.58 , pp. 63
    • Perler, F.B.1
  • 86
    • 0030021923 scopus 로고    scopus 로고
    • Fatty acid binding and conformational stability of mutants of human muscle fatty acid-binding protein
    • Prinsen, C.F.M. and Veerkamp, J.H. 1996. Fatty acid binding and conformational stability of mutants of human muscle fatty acid-binding protein. Biochem. J. 314: 253-260.
    • (1996) Biochem. J , vol.314 , pp. 253-260
    • Prinsen, C.F.M.1    Veerkamp, J.H.2
  • 87
    • 0000356227 scopus 로고
    • On the enzymatic activity of subtilisin-modified ribonuclease
    • Richards, F.M. 1958. On the enzymatic activity of subtilisin-modified ribonuclease. Proc. Natl. Acad. Sci. 44: 162-166.
    • (1958) Proc. Natl. Acad. Sci , vol.44 , pp. 162-166
    • Richards, F.M.1
  • 88
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • Rousseau, F., Schymkowitz, J.W.H., Wilkinson, H.R., and Itzhaki, L.S. 2001. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proc. Natl. Acad. Sci. 98: 5596-5601.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.H.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 89
    • 0037337270 scopus 로고    scopus 로고
    • The unfolding story of three-dimensional domain swapping
    • Rousseau, F., Schymkowitz, J.W., and Itzhaki, L.S. 2003. The unfolding story of three-dimensional domain swapping. Structure 11: 243-251.
    • (2003) Structure , vol.11 , pp. 243-251
    • Rousseau, F.1    Schymkowitz, J.W.2    Itzhaki, L.S.3
  • 90
    • 0028904072 scopus 로고
    • Protein-fragments as models for events in protein-folding pathways - protein engineering analysis of the association of 2 complementary fragments of the barley chymotrypsin inhibitor-2 (Ci-2)
    • Ruiz-Sanz, J., Prat-Gay, G.D., Otzen, D.E., and Fersht, A.R. 1995. Protein-fragments as models for events in protein-folding pathways - protein engineering analysis of the association of 2 complementary fragments of the barley chymotrypsin inhibitor-2 (Ci-2). Biochemistry 34: 1695-1701.
    • (1995) Biochemistry , vol.34 , pp. 1695-1701
    • Ruiz-Sanz, J.1    Prat-Gay, G.D.2    Otzen, D.E.3    Fersht, A.R.4
  • 91
    • 1642368967 scopus 로고    scopus 로고
    • Autoproteolytic activation of human aspartylglucosaminidase
    • Saarela, J., Oinonen, C., Jalanko, A., Rouvinen, J., and Peltonen, L. 2004. Autoproteolytic activation of human aspartylglucosaminidase. Biochem. J. 378: 363-371.
    • (2004) Biochem. J , vol.378 , pp. 363-371
    • Saarela, J.1    Oinonen, C.2    Jalanko, A.3    Rouvinen, J.4    Peltonen, L.5
  • 92
    • 24644510813 scopus 로고    scopus 로고
    • Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure
    • Sambashivan, S., Liu, Y.S., Sawaya, M.R., Gingery, M., and Eisenberg, D. 2005. Amyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure. Nature 437: 266-269.
    • (2005) Nature , vol.437 , pp. 266-269
    • Sambashivan, S.1    Liu, Y.S.2    Sawaya, M.R.3    Gingery, M.4    Eisenberg, D.5
  • 94
    • 0030770294 scopus 로고    scopus 로고
    • Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly
    • Schlunegger, M.P., Bennett, M.J., and Eisenberg, D. 1997. Oligomer formation by 3D domain swapping: A model for protein assembly and misassembly. Adv. Protein Chem. 50: 61-122.
    • (1997) Adv. Protein Chem , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 95
    • 0342895833 scopus 로고    scopus 로고
    • Interactions of ribonuclease S with ligands from random peptide libraries
    • eds. J.E.a.C. B.Z. Ladbury et al, pp, John Wiley and Sons, New York
    • Schultz, D.R., Ladbury, J.E., Smith, G.P., and Fox, R.O. 1998. Interactions of ribonuclease S with ligands from random peptide libraries. In Applications of calorimetry in the biological sciences (eds. J.E.a.C. B.Z. Ladbury et al.), pp. 123-138. John Wiley and Sons, New York.
    • (1998) Applications of calorimetry in the biological sciences , pp. 123-138
    • Schultz, D.R.1    Ladbury, J.E.2    Smith, G.P.3    Fox, R.O.4
  • 96
    • 0028366005 scopus 로고
    • Relative stabilities of synthetic peptide homodimeric and heterodimeric troponin-c domains
    • Shaw, G.S., Hodges, R.S., Kay, C.M., and Sykes, B.D. 1994. Relative stabilities of synthetic peptide homodimeric and heterodimeric troponin-c domains. Protein Sci. 3: 1010-1019.
    • (1994) Protein Sci , vol.3 , pp. 1010-1019
    • Shaw, G.S.1    Hodges, R.S.2    Kay, C.M.3    Sykes, B.D.4
  • 97
    • 0026592651 scopus 로고
    • Functional assembly of a randomly cleaved protein
    • Shiba, K. and Schimmel, P. 1992. Functional assembly of a randomly cleaved protein. Proc. Natl. Acad. Sci. 89: 1880-1884.
    • (1992) Proc. Natl. Acad. Sci , vol.89 , pp. 1880-1884
    • Shiba, K.1    Schimmel, P.2
  • 99
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of nonnative states of proteins by NMR methods
    • Shortle, D.R. 1996. Structural analysis of nonnative states of proteins by NMR methods. Curr. Opin. Struct. Biol. 6: 24-30.
    • (1996) Curr. Opin. Struct. Biol , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 100
    • 33646476301 scopus 로고    scopus 로고
    • Reconstitution of calmodulin from domains and subdomains: Influence of target peptide
    • Shuman, C.F., Jiji, R., Akerfeldt, K.S., and Linse, S. 2006. Reconstitution of calmodulin from domains and subdomains: Influence of target peptide. J. Mol. Biol. 358: 870-881.
    • (2006) J. Mol. Biol , vol.358 , pp. 870-881
    • Shuman, C.F.1    Jiji, R.2    Akerfeldt, K.S.3    Linse, S.4
  • 101
    • 0035109099 scopus 로고    scopus 로고
    • Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: Fragment complementation and circular permutation reveal stable, alternatively folded forms
    • Smith, V.F. and Matthews, C.R. 2001. Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: Fragment complementation and circular permutation reveal stable, alternatively folded forms. Protein Sci. 10: 116-128.
    • (2001) Protein Sci , vol.10 , pp. 116-128
    • Smith, V.F.1    Matthews, C.R.2
  • 102
    • 0027527431 scopus 로고
    • Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution
    • Somoza, J.R., Jiang, F., Tong, L., Kang, C.H., Cho, J.M., and Kim, S.H. 1993. Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution. J. Mol. Biol. 234: 390-404.
    • (1993) J. Mol. Biol , vol.234 , pp. 390-404
    • Somoza, J.R.1    Jiang, F.2    Tong, L.3    Kang, C.H.4    Cho, J.M.5    Kim, S.H.6
  • 103
    • 0028014680 scopus 로고
    • Evidence for strained interactions between side-chains and the polypeptide backbone
    • Stites, W.E., Meeker, A.K., and Shortle, D. 1994. Evidence for strained interactions between side-chains and the polypeptide backbone. J. Mol. Biol. 235: 27-32.
    • (1994) J. Mol. Biol , vol.235 , pp. 27-32
    • Stites, W.E.1    Meeker, A.K.2    Shortle, D.3
  • 104
    • 0030783569 scopus 로고    scopus 로고
    • Molecular and biological constraints on ligand-binding affinity and specificity
    • Szwajkajzer, D. and Carey, J. 1997. Molecular and biological constraints on ligand-binding affinity and specificity. Biopolymers 44: 181-198.
    • (1997) Biopolymers , vol.44 , pp. 181-198
    • Szwajkajzer, D.1    Carey, J.2
  • 105
    • 0014690694 scopus 로고
    • An experimental approach to study of folding of staphylococcal nuclease
    • Taniuchi, H. and Anfinsen, C.B. 1969. An experimental approach to study of folding of staphylococcal nuclease. J. Biol. Chem. 244: 3864-3875.
    • (1969) J. Biol. Chem , vol.244 , pp. 3864-3875
    • Taniuchi, H.1    Anfinsen, C.B.2
  • 106
    • 0026596758 scopus 로고
    • Ordered self-assembly of polypeptide fragments to form native-like dimeric trp repressor
    • Tasayco, M.L. and Carey, J. 1992. Ordered self-assembly of polypeptide fragments to form native-like dimeric trp repressor. Science 255: 594-597. www.sciencemag.org.
    • (1992) Science , vol.255 , pp. 594-597
    • Tasayco, M.L.1    Carey, J.2
  • 107
    • 0037317075 scopus 로고    scopus 로고
    • A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia
    • Tranier, S., Iobbi-Nivol, C., Birck, C., Ilbert, M., Mortier-Barriere, I., Mejean, V., and Samama, J.P. 2003. A novel protein fold and extreme domain swapping in the dimeric TorD chaperone from Shewanella massilia. Structure 11: 165-174.
    • (2003) Structure , vol.11 , pp. 165-174
    • Tranier, S.1    Iobbi-Nivol, C.2    Birck, C.3    Ilbert, M.4    Mortier-Barriere, I.5    Mejean, V.6    Samama, J.P.7
  • 108
    • 0033621104 scopus 로고    scopus 로고
    • Folding and binding cascades: Shifts in energy landscapes
    • Tsai, C.J., Ma, B.Y., and Nussinov, R. 1999. Folding and binding cascades: Shifts in energy landscapes. Proc. Natl. Acad. Sci. 96: 9970-9972.
    • (1999) Proc. Natl. Acad. Sci , vol.96 , pp. 9970-9972
    • Tsai, C.J.1    Ma, B.Y.2    Nussinov, R.3
  • 109
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera, A.R., Blanco, F.J., and Serrano, L. 1995. The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247: 670-681.
    • (1995) J. Mol. Biol , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 110
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: A view emerging from NMR spectroscopy
    • Wand, A.J. 2001. Dynamic activation of protein function: A view emerging from NMR spectroscopy. Nat. Struct. Biol. 8: 926-931.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 111
    • 0015528157 scopus 로고
    • Ligand binding and internal equilibria in proteins
    • Weber, G. 1972. Ligand binding and internal equilibria in proteins. Biochemistry 11: 864-878.
    • (1972) Biochemistry , vol.11 , pp. 864-878
    • Weber, G.1
  • 112
    • 0031595862 scopus 로고    scopus 로고
    • Circular permutation of β B2-crystallin changes the hierarchy of domain assembly
    • Wright, G., Basak, A.K., Wieligmann, K., Mayr, E.M., and Slingsby, C. 1998. Circular permutation of β B2-crystallin changes the hierarchy of domain assembly. Protein Sci. 7: 1280-1285.
    • (1998) Protein Sci , vol.7 , pp. 1280-1285
    • Wright, G.1    Basak, A.K.2    Wieligmann, K.3    Mayr, E.M.4    Slingsby, C.5
  • 113
    • 6344219892 scopus 로고    scopus 로고
    • Multi-method global analysis of thermodynamics and kinetics in reconstitution of monellin
    • Xue, W.-F., Carey, J., and Linse, S. 2004. Multi-method global analysis of thermodynamics and kinetics in reconstitution of monellin. Bioinformatics 57: 586-595.
    • (2004) Bioinformatics , vol.57 , pp. 586-595
    • Xue, W.-F.1    Carey, J.2    Linse, S.3
  • 114
    • 33646091307 scopus 로고    scopus 로고
    • Intra- versus intermolecular interactions in monellin: Contribution of surface charges to protein assembly
    • Xue, W.F., Szczepankiewicz, O., Bauer, M.C., Thulin, E., and Linse, S. 2006. Intra- versus intermolecular interactions in monellin: Contribution of surface charges to protein assembly. J. Mol. Biol. 358: 1244-1255.
    • (2006) J. Mol. Biol , vol.358 , pp. 1244-1255
    • Xue, W.F.1    Szczepankiewicz, O.2    Bauer, M.C.3    Thulin, E.4    Linse, S.5
  • 117
    • 0034923263 scopus 로고    scopus 로고
    • Ligand specificity and conformational stability of human fatty acid-binding proteins
    • Zimmerman, A.W., van Moerkerk, H.T.B., and Veerkamp, J.H. 2001. Ligand specificity and conformational stability of human fatty acid-binding proteins. Int. J. Biochem. Cell Biol. 33: 865-876.
    • (2001) Int. J. Biochem. Cell Biol , vol.33 , pp. 865-876
    • Zimmerman, A.W.1    van Moerkerk, H.T.B.2    Veerkamp, J.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.