메뉴 건너뛰기




Volumn 8, Issue 8, 1999, Pages 1591-1604

Distinguishing between sequential and nonsequentially folded proteins: Implications for folding and misfolding

Author keywords

Building block; Funnels; Hydrophobic folding unit; Misfolding; Protein folding; Sequential folding

Indexed keywords

POLYPEPTIDE;

EID: 0032777204     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.8.1591     Document Type: Article
Times cited : (18)

References (57)
  • 1
    • 0030334822 scopus 로고
    • Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution
    • Alba ED, Jimenez MA, Rico M, Nieto JL. 1995. Conformational investigation of designed short linear peptides able to fold into β-hairpin structures in aqueous solution. Folding Design 1:133-144.
    • (1995) Folding Design , vol.1 , pp. 133-144
    • Alba, E.D.1    Jimenez, M.A.2    Rico, M.3    Nieto, J.L.4
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chain
    • Anfinsen CB. 1973. Principles that govern the folding of protein chain. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0028286471 scopus 로고
    • Kinetics versus thermodynamics in protein folding
    • Baker D, Agard DA. 1994. Kinetics versus thermodynamics in protein folding. Biochemistry 33:7505-7509.
    • (1994) Biochemistry , vol.33 , pp. 7505-7509
    • Baker, D.1    Agard, D.A.2
  • 4
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin RL, Rose GD. 1999. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem Sci 24:26-33.
    • (1999) Trends Biochem Sci , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 5
    • 0001366381 scopus 로고    scopus 로고
    • From topographies to dynamics on multidimensional potential energy surfaces of atomic clusters
    • Ball KD, Berry RS, Kunz RE, Li FY, Proykova A, Wales DJ. 1996. From topographies to dynamics on multidimensional potential energy surfaces of atomic clusters. Science 271:963-966.
    • (1996) Science , vol.271 , pp. 963-966
    • Ball, K.D.1    Berry, R.S.2    Kunz, R.E.3    Li, F.Y.4    Proykova, A.5    Wales, D.J.6
  • 7
    • 0031991297 scopus 로고    scopus 로고
    • Structural classification of αββ and ββα supersecondary structure units in proteins
    • Boutonnet NS, Kajava AV, Rooman MJ. 1998, Structural classification of αββ and ββα supersecondary structure units in proteins. Proteins 30:193-212.
    • (1998) Proteins , vol.30 , pp. 193-212
    • Boutonnet, N.S.1    Kajava, A.V.2    Rooman, M.J.3
  • 8
    • 0026607096 scopus 로고
    • Early hydrogen-bonding events in the folding reaction of ubiquitin
    • Briggs MS, Roder H. 1992. Early hydrogen-bonding events in the folding reaction of ubiquitin. Proc Natl Acad Sci USA 89:2017-2021.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2017-2021
    • Briggs, M.S.1    Roder, H.2
  • 9
    • 0031430923 scopus 로고    scopus 로고
    • Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments
    • Chaffotte AF, Li JH, Georgescu RE, Goldberg ME, Tasayco ML. 1997. Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments. Biochemistry 36:16040-16048.
    • (1997) Biochemistry , vol.36 , pp. 16040-16048
    • Chaffotte, A.F.1    Li, J.H.2    Georgescu, R.E.3    Goldberg, M.E.4    Tasayco, M.L.5
  • 10
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 31:7134-7155.
    • (1990) Biochemistry , vol.31 , pp. 7134-7155
    • Dill, K.A.1
  • 11
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K, Chan HS. 1997. From Levinthal to pathways to funnels. Nature Struct Biol 4:10-19.
    • (1997) Nature Struct Biol , vol.4 , pp. 10-19
    • Dill, K.1    Chan, H.S.2
  • 12
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I. Myohemerythrin
    • Dyson HJ, Merutka G, Waltho JP, Lerner RA, Wright PE. 1992. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding I. Myohemerythrin. J Mol Biol 226:795-817.
    • (1992) J Mol Biol , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lerner, R.A.4    Wright, P.E.5
  • 13
    • 0026685018 scopus 로고
    • Stable substructures of eightfold βα-barrel proteins: Fragment complementation of phosphoribosylanthranilate isomerase
    • Eder J, Kirschner K. 1992. Stable substructures of eightfold βα-barrel proteins: Fragment complementation of Phosphoribosylanthranilate Isomerase. Biochemistry 31:3617-3625.
    • (1992) Biochemistry , vol.31 , pp. 3617-3625
    • Eder, J.1    Kirschner, K.2
  • 14
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell: Competing models of chaperonin function
    • Ellis RJ, Hartl FU. 1996. Protein folding in the cell: Competing models of chaperonin function. FASEB J 10:20-26.
    • (1996) FASEB J , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.U.2
  • 15
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewall KL, Hendrick JP, Houry WA, Hartl FU. 1997. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90:491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewall, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 16
    • 0025124588 scopus 로고
    • Expression of human plasminogen activator inhibitor type-1 (PAI-1) in Escherichia coli as a soluble protein comprised of active and latent forms. Isolation and crystallization of latent PAI-1
    • Franke AE, Danley DE, Kaczmarek FS, Hawrylik SJ, Gerard RD, Lee SE, Geoghegan KF. 1990. Expression of human plasminogen activator inhibitor type-1 (PAI-1) in Escherichia coli as a soluble protein comprised of active and latent forms. Isolation and crystallization of latent PAI-1. Biochim Biophys Acta 1037:16-23.
    • (1990) Biochim Biophys Acta , vol.1037 , pp. 16-23
    • Franke, A.E.1    Danley, D.E.2    Kaczmarek, F.S.3    Hawrylik, S.J.4    Gerard, R.D.5    Lee, S.E.6    Geoghegan, K.F.7
  • 17
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell 5:253-265.
    • (1994) Mol Biol Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 18
  • 19
    • 0031889752 scopus 로고    scopus 로고
    • Domain assignment for protein structures using a consensus approach: Characterization and analysis
    • Jones S, Stewart M, Michie A, Swindells MB, Orengo C, Thornton JM. 1998. Domain assignment for protein structures using a consensus approach: Characterization and analysis. Protein Sci 7:233-242.
    • (1998) Protein Sci , vol.7 , pp. 233-242
    • Jones, S.1    Stewart, M.2    Michie, A.3    Swindells, M.B.4    Orengo, C.5    Thornton, J.M.6
  • 20
    • 0028327236 scopus 로고
    • Protein folding dynamics: The diffusion-collision model and experimental data
    • Karplus M, Weaver DL. 1994. Protein folding dynamics: The diffusion-collision model and experimental data. Protein Sci 3:650-668.
    • (1994) Protein Sci , vol.3 , pp. 650-668
    • Karplus, M.1    Weaver, D.L.2
  • 21
    • 0031214378 scopus 로고    scopus 로고
    • An exceptionally stable helix from the ribosomal protein L9: Implications for protein folding and stability
    • Kuhlman B, Yang HY, Boice JA, Fairman R, Raleigh DP. 1997. An exceptionally stable helix from the ribosomal protein L9: Implications for protein folding and stability. J Mol Biol 270:640-647.
    • (1997) J Mol Biol , vol.270 , pp. 640-647
    • Kuhlman, B.1    Yang, H.Y.2    Boice, J.A.3    Fairman, R.4    Raleigh, D.P.5
  • 22
    • 0031576341 scopus 로고    scopus 로고
    • Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2
    • Ladurner AG, Itzhaki LS, Gay FDP, Fersht AR. 1997. Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2. J Mol Biol 273:317-329.
    • (1997) J Mol Biol , vol.273 , pp. 317-329
    • Ladurner, A.G.1    Itzhaki, L.S.2    Gay, F.D.P.3    Fersht, A.R.4
  • 23
    • 0015222647 scopus 로고
    • The interpretation of protein structures. Estimation of static accessibility
    • Lee BK, Richards FM. 1971. The interpretation of protein structures. Estimation of static accessibility. J Mol Biol 55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 24
    • 0030777763 scopus 로고    scopus 로고
    • Exploring the limits of nearest neighbor secondary structure prediction
    • Levin JM. 1997. Exploring the limits of nearest neighbor secondary structure prediction. Protein Eng 10:771-776.
    • (1997) Protein Eng , vol.10 , pp. 771-776
    • Levin, J.M.1
  • 25
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. 1968. Are there pathways for protein folding? J Chim Phys 65:44-45.
    • (1968) J Chim Phys , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 26
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
    • Lorimer GH. 1996. A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J 10:5-9.
    • (1996) FASEB J , vol.10 , pp. 5-9
    • Lorimer, G.H.1
  • 27
    • 0026742164 scopus 로고
    • Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR
    • Lu J, Dahlquist FW. 1992. Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR. Biochemistry 31:4749-4156.
    • (1992) Biochemistry , vol.31 , pp. 4749-14156
    • Lu, J.1    Dahlquist, F.W.2
  • 28
  • 29
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of β-hairpin formation
    • Munoz V, Thompson PA, Hofrichter J, Eaton WA. 1997. Folding dynamics and mechanism of β-hairpin formation. Nature 390:196-199.
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 30
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukarykotes
    • Netzer WJ, Hartl FU. 1997. Recombination of protein domains facilitated by co-translational folding in eukarykotes. Nature 388:343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 31
    • 0031565728 scopus 로고    scopus 로고
    • The foldon universe: A survey of structural similarity and self-recognition of independently folding units
    • Panchenko AR, Luthey-Schulten Z, Cole R, Wolynes PG. 1997. The foldon universe: A survey of structural similarity and self-recognition of independently folding units. J Mol Biol 272:95-105.
    • (1997) J Mol Biol , vol.272 , pp. 95-105
    • Panchenko, A.R.1    Luthey-Schulten, Z.2    Cole, R.3    Wolynes, P.G.4
  • 33
    • 0030840018 scopus 로고    scopus 로고
    • Circularly permuted β-lactamase from Staphylococcus aureus PC1
    • Pieper U, Hayakawa K, Li Z, Herzberg O. 1997. Circularly permuted β-lactamase from Staphylococcus aureus PC1. Biochemistry 36:8767-8774.
    • (1997) Biochemistry , vol.36 , pp. 8767-8774
    • Pieper, U.1    Hayakawa, K.2    Li, Z.3    Herzberg, O.4
  • 34
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov PL. 1996. Intermediate states in protein folding. J Mol Biol 258:707-725.
    • (1996) J Mol Biol , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 35
    • 0029891313 scopus 로고    scopus 로고
    • De novo design and structural analysis of a model b-hairpin peptide system
    • Ramirez-Alvarado M, Blanco FJ, Serrano L. 1996. De novo design and structural analysis of a model b-hairpin peptide system. Nature Struct Biol 3:604-612.
    • (1996) Nature Struct Biol , vol.3 , pp. 604-612
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Serrano, L.3
  • 36
    • 0023927904 scopus 로고
    • Identification of structural motifs from protein coordinate data: Secondary structure and first-level supersecondary structure
    • Richards FM, Kundrot CE. 1988. Identification of structural motifs from protein coordinate data: Secondary structure and first-level supersecondary structure. Proteins 3:71-84.
    • (1988) Proteins , vol.3 , pp. 71-84
    • Richards, F.M.1    Kundrot, C.E.2
  • 37
    • 0026674246 scopus 로고
    • Predicting protein secondary structure with a nearest-neighbor algorithm
    • Salzberg S, Cost S. 1992. Predicting protein secondary structure with a nearest-neighbor algorithm. J Mol Biol 227:371-374.
    • (1992) J Mol Biol , vol.227 , pp. 371-374
    • Salzberg, S.1    Cost, S.2
  • 38
    • 0027248899 scopus 로고
    • Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin
    • Shin JC, Merutka G, Waltho JP, Tennant LL, Dyson HJ, Wright PE. 1993. Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin. Biochemistry 32:6356-6364.
    • (1993) Biochemistry , vol.32 , pp. 6356-6364
    • Shin, J.C.1    Merutka, G.2    Waltho, J.P.3    Tennant, L.L.4    Dyson, H.J.5    Wright, P.E.6
  • 39
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms
    • Shrake A, Rupley JA. 1973. Environment and exposure to solvent of protein atoms. J Mol Biol 79:351-371.
    • (1973) J Mol Biol , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 40
    • 0028965118 scopus 로고
    • Prediction of protein secondary structure by combining nearest-neighbor algorithms and multiple sequence alignments
    • Solovyev VV, Salamov AA. 1995. Prediction of protein secondary structure by combining nearest-neighbor algorithms and multiple sequence alignments. J Mol Biol 247:11-15.
    • (1995) J Mol Biol , vol.247 , pp. 11-15
    • Solovyev, V.V.1    Salamov, A.A.2
  • 41
    • 0030461645 scopus 로고    scopus 로고
    • Patterns and conformations of commonly occurring supersecondary structures (basic motifs) in protein data bank
    • Sun Z, Jiang B. 1996. Patterns and conformations of commonly occurring supersecondary structures (basic motifs) in protein data bank. J Protein Chem 15:675-690.
    • (1996) J Protein Chem , vol.15 , pp. 675-690
    • Sun, Z.1    Jiang, B.2
  • 42
    • 0029027777 scopus 로고
    • NMR study of the reconstitution of the β-sheet of thioredoxin by fragment complementation
    • Tasayco ML, Chao K. 1995. NMR study of the reconstitution of the β-sheet of thioredoxin by fragment complementation. Proteins 22:41-44.
    • (1995) Proteins , vol.22 , pp. 41-44
    • Tasayco, M.L.1    Chao, K.2
  • 43
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai CJ, Kumar S, Ma B, Nussinov R. 1999. Folding funnels, binding funnels, and protein function. Protein Sci 8:1181-1190.
    • (1999) Protein Sci , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 44
    • 0030602896 scopus 로고    scopus 로고
    • A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique
    • Tsai CJ, Lin SL, Wolfson HJ, Nussinov R. 1996. A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique. J Mol Biol 260:604-620.
    • (1996) J Mol Biol , vol.260 , pp. 604-620
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 45
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai CJ, Lin SL, Wolfson HJ, Nussinov R. 1997. Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect. Protein Sci 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
  • 46
    • 0031012563 scopus 로고    scopus 로고
    • Hydrophobic folding units derived from dissimilar monomer structures and their interactions
    • Tsai CJ, Nussinov R. 1997. Hydrophobic folding units derived from dissimilar monomer structures and their interactions. Protein Sci 6:24-42.
    • (1997) Protein Sci , vol.6 , pp. 24-42
    • Tsai, C.J.1    Nussinov, R.2
  • 47
    • 0031868211 scopus 로고    scopus 로고
    • Protein folding via binding, and vice versa
    • Tsai CJ, Xu D, Nussinov R. 1998. Protein folding via binding, and vice versa. Folding Design 3:R71-R80.
    • (1998) Folding Design , vol.3
    • Tsai, C.J.1    Xu, D.2    Nussinov, R.3
  • 48
    • 0028932770 scopus 로고
    • The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera AR, Blanco FJ, 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
  • 49
    • 0027165688 scopus 로고
    • Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G-and H-helices of myoglobin
    • Waltho JP, Feher VA, Merutka G, Dyson HJ, Wright PE. 1993. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G-and H-helices of myoglobin. Biochemistry 32:6337-6347.
    • (1993) Biochemistry , vol.32 , pp. 6337-6347
    • Waltho, J.P.1    Feher, V.A.2    Merutka, G.3    Dyson, H.J.4    Wright, P.E.5
  • 50
    • 0029786948 scopus 로고    scopus 로고
    • A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease
    • Wang Y, Shortle D. 1996. A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease. Protein Sci 5:1898-1906.
    • (1996) Protein Sci , vol.5 , pp. 1898-1906
    • Wang, Y.1    Shortle, D.2
  • 52
    • 0028212643 scopus 로고
    • Autonomous subdomains in protein folding
    • Wu LC, Grandori R, Carey J. 1994. Autonomous subdomains in protein folding. Protein Sci 3:359-371.
    • (1994) Protein Sci , vol.3 , pp. 359-371
    • Wu, L.C.1    Grandori, R.2    Carey, J.3
  • 53
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D, Tsai CJ, Nussinov R. 1997. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng 10:999-1012.
    • (1997) Protein Eng , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 54
    • 0027199670 scopus 로고
    • Protein secondary structure prediction using nearest-neighbor methods
    • Yi TM, Lander ES. 1993. Protein secondary structure prediction using nearest-neighbor methods. J Mol Biol 232:1117-1129.
    • (1993) J Mol Biol , vol.232 , pp. 1117-1129
    • Yi, T.M.1    Lander, E.S.2
  • 55
    • 0027297660 scopus 로고
    • Improved calculations of compactness and a reevaluation of continuous compact units
    • Zehfus MH. 1993. Improved calculations of compactness and a reevaluation of continuous compact units. Proteins 16:293-300.
    • (1993) Proteins , vol.16 , pp. 293-300
    • Zehfus, M.H.1
  • 56
    • 0023055758 scopus 로고
    • Compact units in proteins
    • Zehfus MH, Rose GD. 1986. Compact units in proteins. Biochemistry 25:5759-5765.
    • (1986) Biochemistry , vol.25 , pp. 5759-5765
    • Zehfus, M.H.1    Rose, G.D.2
  • 57
    • 0029926618 scopus 로고    scopus 로고
    • In vitro evolution of thermodynamically stable turns
    • Zhou HX, Hoess RH, DeGrado WF. 1996. In vitro evolution of thermodynamically stable turns. Nat Struct Biol 3:446-451.
    • (1996) Nat Struct Biol , vol.3 , pp. 446-451
    • Zhou, H.X.1    Hoess, R.H.2    Degrado, W.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.