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Volumn 5, Issue 6, 1996, Pages 991-1000

Protein folding for realists: A timeless phenomenon

Author keywords

denatured state; folding intermediates; hydrophobic bundles; protein folding; stability gradients; structure prediction

Indexed keywords

POLYPEPTIDE;

EID: 0029900442     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050602     Document Type: Review
Times cited : (45)

References (25)
  • 1
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphytococcal nuclease: A heteronuclear NMR study
    • Alexandrescu AT, Abeygunawardana C, Shortle D. 1994. Structure and dynamics of a denatured 131-residue fragment of staphytococcal nuclease: A heteronuclear NMR study. Biochemistry 33:1063-1072.
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 2
    • 0029044324 scopus 로고
    • NMR structure of a stable "OB-fold" subdomain isolated from staphylococcal nuclease
    • Alexandrescu AT, Gittis AG, Abeygunawardana C, Shortle D. 1995. NMR structure of a stable "OB-fold" subdomain isolated from staphylococcal nuclease. J Mol Biol 250:134-143.
    • (1995) J Mol Biol , vol.250 , pp. 134-143
    • Alexandrescu, A.T.1    Gittis, A.G.2    Abeygunawardana, C.3    Shortle, D.4
  • 3
    • 0027491725 scopus 로고
    • Structural argument for N-terminal initiation of protein folding
    • Alexandrov N. 1993. Structural argument for N-terminal initiation of protein folding. Protein Sci 2:1989-1992.
    • (1993) Protein Sci , vol.2 , pp. 1989-1992
    • Alexandrov, N.1
  • 4
    • 0028883794 scopus 로고
    • Determination of the conformation of folding initiation sites in proteins by computer simulation
    • Avbelj F, Moult J. 1995. Determination of the conformation of folding initiation sites in proteins by computer simulation. Proteins Struct Funct Genet 23:129-141.
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 129-141
    • Avbelj, F.1    Moult, J.2
  • 5
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW. 1995. Protein folding intermediates: Native-state hydrogen exchange. Science 259:192-197.
    • (1995) Science , vol.259 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 6
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou PY, Fasman GD. 1974. Prediction of protein conformation. Biochemistry 13:222-245.
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill KA, Shortle D. 1991. Denatured states of proteins. Annu Rev Biochem 60:795-825.
    • (1991) Annu Rev Biochem , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 10
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration of glycerol-water mixtures
    • Gekko K, Timasheff SN. 1981. Mechanism of protein stabilization by glycerol: Preferential hydration of glycerol-water mixtures. Biochemistry 20:4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 11
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen PA. 1989. Spin labeling of proteins. Methods Enzymol 177:86-121.
    • (1989) Methods Enzymol , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 12
    • 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
  • 13
    • 0013943915 scopus 로고
    • Validity of the "two-state" hypothesis for conformational transitions of proteins
    • Lumry R, Biltonen R, Brandis JF. 1966. Validity of the "two-state" hypothesis for conformational transitions of proteins. Biopolymers 4:917-944.
    • (1966) Biopolymers , vol.4 , pp. 917-944
    • Lumry, R.1    Biltonen, R.2    Brandis, J.F.3
  • 14
    • 0029022609 scopus 로고
    • Structure of a compact peptide from staphylococcal nuclease determined by circular dichroism and NMR spectroscopy
    • Maciejewski MW, Zehfus MH. 1995. Structure of a compact peptide from staphylococcal nuclease determined by circular dichroism and NMR spectroscopy. Biochemistry 34:5795-5800.
    • (1995) Biochemistry , vol.34 , pp. 5795-5800
    • Maciejewski, M.W.1    Zehfus, M.H.2
  • 15
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews CR. 1993. Pathways of protein folding. Annu Rev Biochem 62:653-683.
    • (1993) Annu Rev Biochem , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 16
    • 0028864205 scopus 로고
    • A critical assessment of comparative molecular modeling of tertiary structures of proteins
    • Mosimann S, Meleshkdo R, James MNG. 1995. A critical assessment of comparative molecular modeling of tertiary structures of proteins. Proteins Struct Funct Genet 23:301-317.
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 301-317
    • Mosimann, S.1    Meleshkdo, R.2    James, M.N.G.3
  • 17
    • 0025906759 scopus 로고
    • Analysis of protein folding pathways
    • Moult J, Unger R. 1991. Analysis of protein folding pathways. Biochemistry 30:3816-3824.
    • (1991) Biochemistry , vol.30 , pp. 3816-3824
    • Moult, J.1    Unger, R.2
  • 18
    • 2642677446 scopus 로고
    • A critical evaluation of methods for prediction of protein secondary structures
    • Schultz GE. 1988. A critical evaluation of methods for prediction of protein secondary structures. Annu Rev Biophys Bioeng 12:183-210.
    • (1988) Annu Rev Biophys Bioeng , vol.12 , pp. 183-210
    • Schultz, G.E.1
  • 19
    • 0027394283 scopus 로고
    • Denatured states of proteins and their roles in folding and stability
    • Shortle D. 1993. Denatured states of proteins and their roles in folding and stability. Curr Opin Struct Biol 3:66-74.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 66-74
    • Shortle, D.1
  • 20
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle D. 1996a. Structural analysis of non-native 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.1
  • 21
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle D. 1996b. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J 10:27-34.
    • (1996) FASEB J , vol.10 , pp. 27-34
    • Shortle, D.1
  • 22
    • 0029055313 scopus 로고
    • LINUS: A hierarchical procedure to predict the fold of a protein
    • Srinivasan R, Rose GD. 1995. LINUS: A hierarchical procedure to predict the fold of a protein. Proteins Struct Funct Genet 22:81-99.
    • (1995) Proteins Struct Funct Genet , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 23
    • 0028841399 scopus 로고
    • Simple protein folding algorithm using a binary code and secondary structure constraints
    • Sun S, Thomas PD, Dill KA. 1995. Simple protein folding algorithm using a binary code and secondary structure constraints. Protien Eng 8:769-778.
    • (1995) Protien Eng , vol.8 , pp. 769-778
    • Sun, S.1    Thomas, P.D.2    Dill, K.A.3
  • 24
    • 0029653886 scopus 로고
    • Initial studies of the equilibrium folding pathway of staphylococcal nuclease
    • Wang Y, Alexandrescu AT, Shortle D. 1995. Initial studies of the equilibrium folding pathway of staphylococcal nuclease. Philos Trans R Soc Lond [Biol] 348:27-34.
    • (1995) Philos Trans R Soc Lond [Biol] , vol.348 , pp. 27-34
    • Wang, Y.1    Alexandrescu, A.T.2    Shortle, D.3
  • 25
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions
    • Wang Y, Shortle D. 1995. The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions. Biochemistry 34:15895-15905.
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.