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Volumn 2, Issue 3, 2011, Pages 608-626

Protein folding absent selection

Author keywords

Evolution; Protein folding; Sequence space

Indexed keywords

HYBRID PROTEIN; UBIQUITIN;

EID: 80053213284     PISSN: None     EISSN: 20734425     Source Type: Journal    
DOI: 10.3390/genes2030608     Document Type: Article
Times cited : (23)

References (66)
  • 1
    • 0037438460 scopus 로고    scopus 로고
    • Reflections on a century of protein chemistry
    • Van Holde, K.E. Reflections on a century of protein chemistry. Biophys. Chem. 2003, 100, 71-79.
    • (2003) Biophys. Chem , vol.100 , pp. 71-79
    • van Holde, K.E.1
  • 2
    • 0002237761 scopus 로고
    • Biomolecules: Where the physics of complexity and simplicity meet
    • Frauenfelder, H.; Wolynes, P.G. Biomolecules: Where the physics of complexity and simplicity meet. Phys. Today 1994, 47, 58-64.
    • (1994) Phys. Today , vol.47 , pp. 58-64
    • Frauenfelder, H.1    Wolynes, P.G.2
  • 3
    • 35848935407 scopus 로고    scopus 로고
    • Biological cosmos of parallel universes: Does protein structural plasticity facilitate evolution
    • Meier, S.; Özbek, S. A Biological cosmos of parallel universes: Does protein structural plasticity facilitate evolution? BioEssays 2007, 29, 1095-1104.
    • (2007) BioEssays , vol.29 , pp. 1095-1104
    • Meier, S.1    Özbek, S.A.2
  • 4
    • 0014421064 scopus 로고
    • Evolutionary rate at the molecular level
    • Kimura, M. Evolutionary rate at the molecular level. Nature 1968, 217, 624-626.
    • (1968) Nature , vol.217 , pp. 624-626
    • Kimura, M.1
  • 5
    • 0014680905 scopus 로고
    • Non-Darwinian evolution
    • King, J.L.; Jukes, T.H. Non-Darwinian evolution. Science 1969 164, 788-98.
    • (1969) Science , vol.164 , pp. 788-798
    • King, J.L.1    Jukes, T.H.2
  • 6
    • 0014691177 scopus 로고
    • Natural selection and the complexity of the gene
    • Salisbury, F.B. Natural selection and the complexity of the gene. Nature 1969, 224, 342-343.
    • (1969) Nature , vol.224 , pp. 342-343
    • Salisbury, F.B.1
  • 7
    • 0014935646 scopus 로고
    • Natural Selection and the Concept of Protein Space
    • Smith, J.M. Natural Selection and the Concept of Protein Space. Nature 1970, 225, 563-564.
    • (1970) Nature , vol.225 , pp. 563-564
    • Smith, J.M.1
  • 8
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe, A.D.; Szostak, J.W. Functional proteins from a random-sequence library. Nature 2001, 410, 715-718.
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 9
    • 34547400959 scopus 로고    scopus 로고
    • The network of sequence flow between protein structures
    • Meyerguz, L.; Kleinberg, J.; Elber, R. The network of sequence flow between protein structures. Proc. Natl. Acad. Sci. USA 2007, 104, 11627-11632.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11627-11632
    • Meyerguz, L.1    Kleinberg, J.2    Elber, R.3
  • 12
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham, B.C.; Wells, J.A. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 1989, 244, 1081-1085.
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 13
    • 0025186676 scopus 로고
    • Searching sequence space by definably random mutagenesis: Improving the catalytic potency of an enzyme
    • Hermes, J.D.; Blacklow, S.C.; Knowles, J.R. Searching sequence space by definably random mutagenesis: Improving the catalytic potency of an enzyme. Proc. Natl. Acad. Sci. USA 1990, 87, 696-700.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 696-700
    • Hermes, J.D.1    Blacklow, S.C.2    Knowles, J.R.3
  • 14
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim, W.A.; Sauer, R.T. The role of internal packing interactions in determining the structure and stability of a protein. J. Mol. Biol. 1991, 219, 359-376.
    • (1991) J. Mol. Biol , vol.219 , pp. 359-376
    • Lim, W.A.1    Sauer, R.T.2
  • 15
    • 0026496539 scopus 로고
    • The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions
    • Hellinga, H.W.; Wynn, R.; Richards, F.M. The hydrophobic core of Escherichia coli thioredoxin shows a high tolerance to nonconservative single amino acid substitutions. Biochemistry 1992, 31, 11203-11209.
    • (1992) Biochemistry , vol.31 , pp. 11203-11209
    • Hellinga, H.W.1    Wynn, R.2    Richards, F.M.3
  • 16
    • 0025339507 scopus 로고
    • Accommodation of single amino acid insertions by the native state of staphylococcal nuclease
    • Sondek, J.; Shortle, D. Accommodation of single amino acid insertions by the native state of staphylococcal nuclease. Proteins 1990, 7, 299-305.
    • (1990) Proteins , vol.7 , pp. 299-305
    • Sondek, J.1    Shortle, D.2
  • 17
    • 0027087368 scopus 로고
    • The importance of surface loops for stabilizing an eightfold beta alpha barrel protein
    • Urfer R.; Kirschner, K. The importance of surface loops for stabilizing an eightfold beta alpha barrel protein. Protein Sci. 1992, 1, 31-45.
    • (1992) Protein Sci , vol.1 , pp. 31-45
    • Urfer, R.1    Kirschner, K.2
  • 18
    • 33846515095 scopus 로고    scopus 로고
    • Thermodynamics of neutral protein evolution
    • Bloom, J.D.; Raval, A.; Wilke, C.O. Thermodynamics of neutral protein evolution. Genetics 2007, 175, 255-266.
    • (2007) Genetics , vol.175 , pp. 255-266
    • Bloom, J.D.1    Raval, A.2    Wilke, C.O.3
  • 19
    • 33846264862 scopus 로고    scopus 로고
    • Protein structure: Evolutionary bridges to new folds
    • Yeates, T.O. Protein structure: Evolutionary bridges to new folds. Curr. Biol. 2007, 17, R48-R50.
    • (2007) Curr. Biol , vol.17
    • Yeates, T.O.1
  • 20
    • 0034698298 scopus 로고    scopus 로고
    • One sequence, two ribozymes: Implications for the emergence of new ribozyme folds
    • Schultes, E.; Bartel, D.P. One sequence, two ribozymes: Implications for the emergence of new ribozyme folds. Science 2000, 289, 448-452.
    • (2000) Science , vol.289 , pp. 448-452
    • Schultes, E.1    Bartel, D.P.2
  • 21
    • 1842839788 scopus 로고    scopus 로고
    • Simulating protein evolution in sequence space and structure space
    • Xia, Y.; Levitt, M. Simulating protein evolution in sequence space and structure space. Curr. Opin. Struct. Biol. 2004, 14, 202-207.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 202-207
    • Xia, Y.1    Levitt, M.2
  • 22
    • 0000739733 scopus 로고
    • Synthesis and chemical properties of poly-alpha-amino acids
    • Katchelski, E.; Sela, M. Synthesis and chemical properties of poly-alpha-amino acids. Adv. Prot. Chem. 1958, 13, 243-492.
    • (1958) Adv. Prot. Chem , vol.13 , pp. 243-492
    • Katchelski, E.1    Sela, M.2
  • 23
    • 0015962942 scopus 로고
    • Collapsed structure polymers: A scattergun approach to amino acid copolymers
    • Rao, S.P.; Carlstrom, D.E.; Miller, W.G. Collapsed structure polymers: A scattergun approach to amino acid copolymers. Biochemistry 1974, 13, 943-952.
    • (1974) Biochemistry , vol.13 , pp. 943-952
    • Rao, S.P.1    Carlstrom, D.E.2    Miller, W.G.3
  • 25
    • 0028218304 scopus 로고
    • Folded Proteins Occur Frequently in Libraries of Random Amino Acid Sequences
    • Davidson, A.R.; Sauer, R.T. Folded Proteins Occur Frequently in Libraries of Random Amino Acid Sequences, Proc. Natl. Acad. Sci. USA 1994, 91, 2146-2150.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2146-2150
    • Davidson, A.R.1    Sauer, R.T.2
  • 26
    • 0029120253 scopus 로고
    • Cooperatively folded proteins in random sequence libraries
    • Davidson, A.R.; Lumb, K.J.; Sauer, R.T. Cooperatively folded proteins in random sequence libraries. Nat. Struct. Biol. 1995, 2, 856-864.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 856-864
    • Davidson, A.R.1    Lumb, K.J.2    Sauer, R.T.3
  • 27
    • 21744445913 scopus 로고    scopus 로고
    • High solubility of random-sequence proteins consisting of five kinds of primitive amino acids
    • Doi, N.; Kakukawa, K.; Oishi, Y.; Yanagawa, H. High solubility of random-sequence proteins consisting of five kinds of primitive amino acids. Prot. Eng. Des. Sel. 2005, 18, 279-284.
    • (2005) Prot. Eng. Des. Sel , vol.18 , pp. 279-284
    • Doi, N.1    Kakukawa, K.2    Oishi, Y.3    Yanagawa, H.4
  • 29
    • 33748541979 scopus 로고    scopus 로고
    • Investigation of de novo totally random biosequences. Part II. On the folding frequency in a totally random library of de novo proteins obtained by phage display
    • Chiarabelli, C.; Vrijbloed, J.W.; de Lucrezia, D.; Thomas, R.M.; Stano, P.; Polticelli, F.; Ottone, T.; Papa, E.; Luisi, P.L. Investigation of de novo totally random biosequences. Part II. On the folding frequency in a totally random library of de novo proteins obtained by phage display. Chem. Biodiv. 2006, 3, 840-859.
    • (2006) Chem. Biodiv , vol.3 , pp. 840-859
    • Chiarabelli, C.1    Vrijbloed, J.W.2    de Lucrezia, D.3    Thomas, R.M.4    Stano, P.5    Polticelli, F.6    Ottone, T.7    Papa, E.8    Luisi, P.L.9
  • 30
    • 0027291987 scopus 로고
    • Design of synthetic gene libraries encoding random sequence proteins with desired ensemble characteristics
    • LaBean, T.H.; Kauffman, S.A. Design of synthetic gene libraries encoding random sequence proteins with desired ensemble characteristics. Prot. Sci. 1993, 2, 1249-1254.
    • (1993) Prot. Sci , vol.2 , pp. 1249-1254
    • Labean, T.H.1    Kauffman, S.A.2
  • 31
    • 0024506385 scopus 로고
    • Gene synthesis, expression and processing of human ubiquitin carboxy extension proteins in bacteria and yeast
    • Monia, B.P.; Ecker, D.J.; Jonnalagadda, S.; Marsh, J.; Gotlib, J.L.; Butt, T.R. Gene synthesis, expression and processing of human ubiquitin carboxy extension proteins in bacteria and yeast. J. Biol. Chem. 1989, 264, 4093-4103.
    • (1989) J. Biol. Chem , vol.264 , pp. 4093-4103
    • Monia, B.P.1    Ecker, D.J.2    Jonnalagadda, S.3    Marsh, J.4    Gotlib, J.L.5    Butt, T.R.6
  • 33
    • 0024378471 scopus 로고
    • Synthesis of peptides as cloned ubiquitin extensions
    • Yoo, Y.; Rote, K.; Rechsteiner, M. Synthesis of peptides as cloned ubiquitin extensions. J. Biol. Chem. 1989, 264, 17078-17083.
    • (1989) J. Biol. Chem , vol.264 , pp. 17078-17083
    • Yoo, Y.1    Rote, K.2    Rechsteiner, M.3
  • 34
    • 0029361780 scopus 로고
    • Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin
    • LaBean, T.H.; Kauffman, S.A.; Butt, T.R. Libraries of random-sequence polypeptides produced with high yield as carboxy-terminal fusions with ubiquitin. Mol. Div. 1995, 1, 29-38.
    • (1995) Mol. Div , vol.1 , pp. 29-38
    • Labean, T.H.1    Kauffman, S.A.2    Butt, T.R.3
  • 36
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • Perczel, A.; Hollosi, M.; Tusnady, G.; Fasman, G.D. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins. Prot. Eng. 1991, 4, 669-679.
    • (1991) Prot. Eng , vol.4 , pp. 669-679
    • Perczel, A.1    Hollosi, M.2    Tusnady, G.3    Fasman, G.D.4
  • 37
    • 0020997912 scopus 로고
    • Dictonary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictonary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 39
    • 0019249775 scopus 로고
    • Structural studies on two high-mobility-group proteins from calf thymus, HMG-14 and HMG-20 (ubiquitin), and their interaction with DNA
    • Cary, P.D.; King, D.S.; Crane-Robinson, C.; Bradbury, E.M.; Rabbani, A.; Goodwin, G.H. Structural studies on two high-mobility-group proteins from calf thymus, HMG-14 and HMG-20 (ubiquitin), and their interaction with DNA. Eur. J. Biochem. 1980, 112, 577-580.
    • (1980) Eur. J. Biochem , vol.112 , pp. 577-580
    • Cary, P.D.1    King, D.S.2    Crane-Robinson, C.3    Bradbury, E.M.4    Rabbani, A.5    Goodwin, G.H.6
  • 40
    • 0023785593 scopus 로고
    • Secondary structure of proteins through circular dichroism spectroscopy
    • Johnson, W.C.J. Secondary structure of proteins through circular dichroism spectroscopy. Annu. Rev. Biophys. Biophys. Chem. 1988, 17, 145-166.
    • (1988) Annu. Rev. Biophys. Biophys. Chem , vol.17 , pp. 145-166
    • Johnson, W.C.J.1
  • 42
    • 0025689242 scopus 로고
    • Intrinsic fluorescence of binding-site fragments of the nicotinic acetylcholine receptor: Perturbations produced upon binding alpha-bungarotoxin
    • Pearce S.F.; Hawrot, E. Intrinsic fluorescence of binding-site fragments of the nicotinic acetylcholine receptor: Perturbations produced upon binding alpha-bungarotoxin. Biochemistry 1990, 29, 10649-10659.
    • (1990) Biochemistry , vol.29 , pp. 10649-10659
    • Pearce, S.F.1    Hawrot, E.2
  • 43
    • 0020825021 scopus 로고
    • Comparative study of GuHCl denaturation of globular proteins. II. A phenomenological classification of denaturation profiles of 17 proteins
    • Saito, Y.; Wada, A. Comparative study of GuHCl denaturation of globular proteins. II. A phenomenological classification of denaturation profiles of 17 proteins. Biopolymers 1983, 22, 2123-2132.
    • (1983) Biopolymers , vol.22 , pp. 2123-2132
    • Saito, Y.1    Wada, A.2
  • 44
    • 0025040232 scopus 로고
    • De novo design, expression, and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht, M.H.; Richardson, J.S.; Richardson, D.C.; Ogden, R.C. De novo design, expression, and characterization of Felix: A four-helix bundle protein of native-like sequence. Science 1990, 249, 884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 45
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from first principles
    • Regan, L.; DeGrado, W.F. Characterization of a helical protein designed from first principles. Science 1988, 241, 976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    Degrado, W.F.2
  • 46
  • 50
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O.B. Molten globule and protein folding. Adv. Prot. Chem. 1995, 47, 83-229.
    • (1995) Adv. Prot. Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 51
    • 0030759786 scopus 로고    scopus 로고
    • Global similarities in nucleotide base composition among disparate functional classes of single-stranded RNA imply adaptive evolutionary convergence
    • Schultes, E.; Hraber, P.T.; LaBean, T.H. Global similarities in nucleotide base composition among disparate functional classes of single-stranded RNA imply adaptive evolutionary convergence. RNA 1997, 3, 792-806.
    • (1997) RNA , vol.3 , pp. 792-806
    • Schultes, E.1    Hraber, P.T.2    Labean, T.H.3
  • 52
    • 0003041817 scopus 로고    scopus 로고
    • A parameterization of RNA sequence space
    • Schultes, E.; Hraber, P.T.; LaBean, T.H. A parameterization of RNA sequence space. Complexity 1999, 4, 61-71.
    • (1999) Complexity , vol.4 , pp. 61-71
    • Schultes, E.1    Hraber, P.T.2    Labean, T.H.3
  • 53
    • 0033013683 scopus 로고    scopus 로고
    • Estimating the contributions of selection and self-organization in RNA secondary structures
    • Schultes, E.; Hraber, P.T.; LaBean, T.H. Estimating the contributions of selection and self-organization in RNA secondary structures. J. Mol. Evol. 1999, 49, 76-83.
    • (1999) J. Mol. Evol , vol.49 , pp. 76-83
    • Schultes, E.1    Hraber, P.T.2    Labean, T.H.3
  • 54
    • 29844452150 scopus 로고    scopus 로고
    • Natural selection is not required to explain universal compositional patterns in rRNA secondary structure categories
    • Smit, S.; Yarus, M.; Knight, R. Natural selection is not required to explain universal compositional patterns in rRNA secondary structure categories. RNA 2006, 12, 1-14.
    • (2006) RNA , vol.12 , pp. 1-14
    • Smit, S.1    Yarus, M.2    Knight, R.3
  • 55
    • 63249135361 scopus 로고    scopus 로고
    • RNA structure prediction from evolutionary patterns of nucleotide composition
    • Smit, S.; Yarus, M.; Knight, R. RNA structure prediction from evolutionary patterns of nucleotide composition. Nucl. Acids Res. 2009, 37, 1378-1386.
    • (2009) Nucl. Acids Res , vol.37 , pp. 1378-1386
    • Smit, S.1    Yarus, M.2    Knight, R.3
  • 56
    • 75149149474 scopus 로고    scopus 로고
    • Natural and artificial RNAs occupy the same restricted region of sequence space
    • Kennedy, R.; Lladser, M.E.; Wu, Z.; Zhang, C.; Yarus, M.; de Sterck, H.; Knight, R. Natural and artificial RNAs occupy the same restricted region of sequence space. RNA 2010, 16, 280-289.
    • (2010) RNA , vol.16 , pp. 280-289
    • Kennedy, R.1    Lladser, M.E.2    Wu, Z.3    Zhang, C.4    Yarus, M.5    de Sterck, H.6    Knight, R.7
  • 57
    • 28544445024 scopus 로고    scopus 로고
    • Compact and ordered collapse in randomly generated RNA sequences
    • Schultes, E.A.; Spasic, A.; Mohanty, U.; Bartel, D.P. Compact and ordered collapse in randomly generated RNA sequences. Nat. Struct. Mol. Bio. 2005, 12, 1130-1136.
    • (2005) Nat. Struct. Mol. Bio , vol.12 , pp. 1130-1136
    • Schultes, E.A.1    Spasic, A.2    Mohanty, U.3    Bartel, D.P.4
  • 58
    • 0027488624 scopus 로고
    • Isolation of new ribozymes from a large pool of random sequences
    • Bartel, D.P.; Szostak, J.W. Isolation of new ribozymes from a large pool of random sequences. Science 1993, 261, 1411-1418.
    • (1993) Science , vol.261 , pp. 1411-1418
    • Bartel, D.P.1    Szostak, J.W.2
  • 59
    • 0022432579 scopus 로고
    • Analytical studies of 'mixed sequence' oligodeoxyribonucleotides synthesized by competitive coupling of either methylor beta-cyanoethyl-N,N-diisopropylamino phosphoramidite reagents, including 2'-deoxyinosine
    • Zon, G.; Gallo, K.A.; Samson, C.J.; Shao, K.L.; Summers, M.F.; Byrd, R.A. Analytical studies of 'mixed sequence' oligodeoxyribonucleotides synthesized by competitive coupling of either methylor beta-cyanoethyl-N,N-diisopropylamino phosphoramidite reagents, including 2'-deoxyinosine. Nucl. Acids Res. 1985, 13, 8181-8196.
    • (1985) Nucl. Acids Res , vol.13 , pp. 8181-8196
    • Zon, G.1    Gallo, K.A.2    Samson, C.J.3    Shao, K.L.4    Summers, M.F.5    Byrd, R.A.6
  • 60
    • 0025232583 scopus 로고
    • A method for construction of long randomized open reading frames and polypeptides
    • Mandecki, W.A. A method for construction of long randomized open reading frames and polypeptides. Prot. Eng. 1990, 3, 221-226.
    • (1990) Prot. Eng , vol.3 , pp. 221-226
    • Mandecki, W.A.1
  • 62
    • 0021921011 scopus 로고
    • Maximizing gene expression from plasmid vectors containing the lambda PL promoter: Strategies for overproducing transcription termination factor rho
    • Mott, J.E.; Grant, R.A.; Ho, Y.S.; Platt, T. Maximizing gene expression from plasmid vectors containing the lambda PL promoter: Strategies for overproducing transcription termination factor rho. Proc. Natl. Acad. Sci. USA 1985, 82, 88-92.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 88-92
    • Mott, J.E.1    Grant, R.A.2    Ho, Y.S.3    Platt, T.4
  • 63
    • 0023039206 scopus 로고
    • Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase
    • Wilkinson, K.D.; Cox, M.J.; Mayer, A.N.; Frey, T. Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase. Biochemistry 1986, 25, 6644-6649.
    • (1986) Biochemistry , vol.25 , pp. 6644-6649
    • Wilkinson, K.D.1    Cox, M.J.2    Mayer, A.N.3    Frey, T.4
  • 64
    • 0021785105 scopus 로고
    • Investigation of amino acid composition in the crystalline region of silk fibroin
    • Nadiger, G.S.; Bhat, N.V.; Padhye, M.R. Investigation of amino acid composition in the crystalline region of silk fibroin. J. App. Pol. Sci. 1985, 30, 221-225.
    • (1985) J. App. Pol. Sci , vol.30 , pp. 221-225
    • Nadiger, G.S.1    Bhat, N.V.2    Padhye, M.R.3
  • 65
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnády, G.E.; Simon, I. Principles governing amino acid composition of integral membrane proteins: Application to topology prediction. J. Mol. Bio. 1998, 283, 489-506.
    • (1998) J. Mol. Bio , vol.283 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 66
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002, 27, 527-533.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1


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