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Volumn 12, Issue 7, 2011, Pages 4745-4757

Molecular basis for chiral selection in RNA aminoacylation

Author keywords

Amino acid; Aminoacylation; Extended double helix; Homochirality; Origin of life; RNA; Stereochemistry

Indexed keywords

AMINO ACID; AMINO ACID TRANSFER RNA LIGASE; PHOSPHATE; TRANSFER RNA; AMINOACYL TRANSFER RNA; RNA;

EID: 79960796446     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms12074745     Document Type: Article
Times cited : (19)

References (65)
  • 1
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids: A structure for deoxyribose nucleic acid
    • Watson, J.D.; Crick, F.H.C. Molecular structure of nucleic acids: A structure for deoxyribose nucleic acid. Nature 1953, 171, 737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 2
    • 0014937223 scopus 로고
    • Central dogma of molecular biology
    • Crick, F. Central dogma of molecular biology. Nature 1970, 227, 561-563.
    • (1970) Nature , vol.227 , pp. 561-563
    • Crick, F.1
  • 3
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • Hannon, G.J. RNA interference. Nature 2002, 418, 244-251.
    • (2002) Nature , vol.418 , pp. 244-251
    • Hannon, G.J.1
  • 4
    • 22144489833 scopus 로고    scopus 로고
    • RNAi: The nuts and bolts of the RISC machine
    • Filipowicz, W. RNAi: The nuts and bolts of the RISC machine. Cell 2005, 122, 17-20.
    • (2005) Cell , vol.122 , pp. 17-20
    • Filipowicz, W.1
  • 5
    • 58749096360 scopus 로고    scopus 로고
    • On the road to reading the RNA-interference code
    • Siomi, H.; Siomi, M.C. On the road to reading the RNA-interference code. Nature 2009, 457, 396-404.
    • (2009) Nature , vol.457 , pp. 396-404
    • Siomi, H.1    Siomi, M.C.2
  • 6
    • 3042783024 scopus 로고    scopus 로고
    • Peptide synthesis through evolution
    • Tamura, K.; Alexander, R.W. Peptide synthesis through evolution. Cell. Mol. Life Sci. 2004, 61, 1317-1330.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 1317-1330
    • Tamura, K.1    Alexander, R.W.2
  • 7
    • 79960828298 scopus 로고    scopus 로고
    • Peptide bond formation: RNA's big bang
    • Tamura, K. Peptide bond formation: RNA's big bang. J. Cosmol. 2011, 13, 3800-3810.
    • (2011) J. Cosmol , vol.13 , pp. 3800-3810
    • Tamura, K.1
  • 8
    • 0004231435 scopus 로고    scopus 로고
    • Cline, D.B., Ed.; American Institute of Physics: New York, NY, USA
    • Bonner, W. Physical Origin of Homochirality in Life; Cline, D.B., Ed.; American Institute of Physics: New York, NY, USA, 1996.
    • (1996) Physical Origin of Homochirality in Life
    • Bonner, W.1
  • 9
    • 0023071528 scopus 로고
    • Parity violation and symmetry breaking of a racemic mixture
    • Hegstrom, R.A. Parity violation and symmetry breaking of a racemic mixture. Biosystems 1987, 20, 49-56.
    • (1987) Biosystems , vol.20 , pp. 49-56
    • Hegstrom, R.A.1
  • 11
    • 0029559848 scopus 로고
    • Asymmetric autocatalysis and amplification of enantiomeric excess of a chiral molecule
    • Soai, K.; Shibata, T.; Morioka, H.; Choji, K. Asymmetric autocatalysis and amplification of enantiomeric excess of a chiral molecule. Nature 1995, 378, 767-768.
    • (1995) Nature , vol.378 , pp. 767-768
    • Soai, K.1    Shibata, T.2    Morioka, H.3    Choji, K.4
  • 12
    • 1942533597 scopus 로고    scopus 로고
    • Asymmetric autocatalysis and its implications for the origin of homochirality
    • Blackmond, D.G. Asymmetric autocatalysis and its implications for the origin of homochirality. Proc. Natl. Acad. Sci. USA 2004, 101, 5732-5736.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5732-5736
    • Blackmond, D.G.1
  • 13
    • 65449159829 scopus 로고    scopus 로고
    • Asymmetric autocatalysis triggered by carbon isotope (13C/12C) chirality
    • Kawasaki, T.; Matsumura, Y.; Tsutsumi, T.; Suzuki, K.; Ito, M.; Soai, K. Asymmetric autocatalysis triggered by carbon isotope (13C/12C) chirality. Science 2009, 324, 492-495.
    • (2009) Science , vol.324 , pp. 492-495
    • Kawasaki, T.1    Matsumura, Y.2    Tsutsumi, T.3    Suzuki, K.4    Ito, M.5    Soai, K.6
  • 14
    • 0023061339 scopus 로고
    • Aminoacyl tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs
    • Schimmel, P. Aminoacyl tRNA synthetases: General scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs. Annu. Rev. Biochem. 1987, 56, 125-158.
    • (1987) Annu. Rev. Biochem , vol.56 , pp. 125-158
    • Schimmel, P.1
  • 15
    • 34447338880 scopus 로고    scopus 로고
    • Simultaneous origin of homochirality, the genetic code and its directionality
    • Root-Bernstein, R. Simultaneous origin of homochirality, the genetic code and its directionality. BioEssays 2007, 29, 689-698.
    • (2007) BioEssays , vol.29 , pp. 689-698
    • Root-Bernstein, R.1
  • 16
    • 0015796802 scopus 로고
    • Synthesis of amino acyl-adenylates under prebiotic conditions
    • Paecht-Horowitz, M.; Katchalsky, A. Synthesis of amino acyl-adenylates under prebiotic conditions. J. Mol. Evol. 1973, 2, 91-98.
    • (1973) J. Mol. Evol , vol.2 , pp. 91-98
    • Paecht-Horowitz, M.1    Katchalsky, A.2
  • 17
    • 0019333922 scopus 로고
    • Efficient metal-ion catalyzed template-directed oligonucleotide synthesis
    • Lohrmann, R.; Bridson, P.K.; Orgel, L.E. Efficient metal-ion catalyzed template-directed oligonucleotide synthesis. Science 1980, 208, 1464-1465.
    • (1980) Science , vol.208 , pp. 1464-1465
    • Lohrmann, R.1    Bridson, P.K.2    Orgel, L.E.3
  • 18
    • 0027436686 scopus 로고
    • An operational RNA code for amino acids and possible relationship to genetic code
    • Schimmel, P.; Giegé, R.; Moras, D.; Yokoyama, S. An operational RNA code for amino acids and possible relationship to genetic code. Proc. Natl. Acad. Sci. USA 1993, 90, 8763-8768.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8763-8768
    • Schimmel, P.1    Giegé, R.2    Moras, D.3    Yokoyama, S.4
  • 19
    • 4344578505 scopus 로고    scopus 로고
    • Chiral-selective aminoacylation of an RNA minihelix
    • Tamura, K.; Schimmel, P. Chiral-selective aminoacylation of an RNA minihelix. Science 2004, 305, 1253.
    • (2004) Science , vol.305 , pp. 1253
    • Tamura, K.1    Schimmel, P.2
  • 20
    • 33748766632 scopus 로고    scopus 로고
    • Chiral-selective aminoacylation of an RNA minihelix: Mechanistic features and chiral suppression
    • Tamura, K.; Schimmel, P.R. Chiral-selective aminoacylation of an RNA minihelix: Mechanistic features and chiral suppression. Proc. Natl. Acad. Sci. USA 2006, 103, 13750-13752.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13750-13752
    • Tamura, K.1    Schimmel, P.R.2
  • 21
    • 39949083745 scopus 로고    scopus 로고
    • Origin of amino acid homochirality: Relationship with the RNA world and origin of tRNA aminoacylation
    • Tamura, K. Origin of amino acid homochirality: Relationship with the RNA world and origin of tRNA aminoacylation. Biosystems 2008, 92, 91-98.
    • (2008) Biosystems , vol.92 , pp. 91-98
    • Tamura, K.1
  • 22
    • 36849148382 scopus 로고
    • The RNA world
    • Gilbert, W. The RNA world. Nature 1986, 319, 618.
    • (1986) Nature , vol.319 , pp. 618
    • Gilbert, W.1
  • 24
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada, C.; Gardiner, K.; Marsh, T.; Pace, N.; Altman, S. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 1983, 35, 849-857.
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 25
    • 77949906855 scopus 로고    scopus 로고
    • Molecular handedness of life: Significance of RNA aminoacylation
    • Tamura, K. Molecular handedness of life: Significance of RNA aminoacylation. J. Biosci. 2009, 34, 991-994.
    • (2009) J. Biosci , vol.34 , pp. 991-994
    • Tamura, K.1
  • 26
    • 79952360248 scopus 로고    scopus 로고
    • Amino acid homochirality and the RNA world: Necessities for life on earth
    • Tamura, K. Amino acid homochirality and the RNA world: Necessities for life on earth. J. Cosmol. 2010, 5, 883-889.
    • (2010) J. Cosmol , vol.5 , pp. 883-889
    • Tamura, K.1
  • 27
    • 79960754893 scopus 로고    scopus 로고
    • Origin of asymmetry of amino acids: Relationship to the RNA world
    • Tamura, K. Origin of asymmetry of amino acids: Relationship to the RNA world. Biophysics 2010, 50, 180-181.
    • (2010) Biophysics , vol.50 , pp. 180-181
    • Tamura, K.1
  • 28
    • 79960764256 scopus 로고    scopus 로고
    • RNA-directed molecular asymmetry of amino acids
    • Tamura, K. RNA-directed molecular asymmetry of amino acids. Viva Origino 2010, 38, 18-22.
    • (2010) Viva Origino , vol.38 , pp. 18-22
    • Tamura, K.1
  • 29
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani, G.; Delarue, M.; Poch, O.; Gangloff, J.; Moras, D. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 1990, 347, 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 30
    • 33947480695 scopus 로고
    • The free energy in hydrolytic reactions: The non-ionized compound convention
    • Carpenter, F.H. The free energy in hydrolytic reactions: The non-ionized compound convention. J. Am. Chem. Soc. 1960, 82, 1111-1122.
    • (1960) J. Am. Chem. Soc , vol.82 , pp. 1111-1122
    • Carpenter, F.H.1
  • 31
    • 0001109389 scopus 로고
    • Stereochemistry of reaction paths at carbonyl centre
    • Bürgi, H.B.; Dunitz, J.D.; Lehn, J.M.; Wipff, G. Stereochemistry of reaction paths at carbonyl centre. Tetrahedron 1974, 30, 1563-1572.
    • (1974) Tetrahedron , vol.30 , pp. 1563-1572
    • Bürgi, H.B.1    Dunitz, J.D.2    Lehn, J.M.3    Wipff, G.4
  • 34
    • 84988072575 scopus 로고
    • Abbreviations and symbols for the description of conformations of polynucleotide chains
    • IUPAC-IUB Joint Commission on Biochemical Nomenclature
    • IUPAC-IUB Joint Commission on Biochemical Nomenclature. Abbreviations and symbols for the description of conformations of polynucleotide chains. Eur. J. Biochem. 1983, 131, 9-15.
    • (1983) Eur. J. Biochem , vol.131 , pp. 9-15
  • 35
    • 0347553366 scopus 로고
    • The rotational barrier in ethane
    • Eyring, H.; Grant, D.M.; Hecht, H. The rotational barrier in ethane. J. Chem. Educ. 1962, 39, 466-468.
    • (1962) J. Chem. Educ , vol.39 , pp. 466-468
    • Eyring, H.1    Grant, D.M.2    Hecht, H.3
  • 36
    • 0029128420 scopus 로고
    • UV spectroscopic identification and thermodynamic analysis of protonated third strand deoxycytidine residues at neutrality in the triplex d(C+-T)6:[d(A-G)6d(C-T)6]; evidence for a proton switch
    • Lavelle, L.; Fresco, J.R. UV spectroscopic identification and thermodynamic analysis of protonated third strand deoxycytidine residues at neutrality in the triplex d(C+-T)6:[d(A-G)6d(C-T)6]; evidence for a proton switch. Nucleic Acids Res. 1995, 23, 2692-2705.
    • (1995) Nucleic Acids Res , vol.23 , pp. 2692-2705
    • Lavelle, L.1    Fresco, J.R.2
  • 37
    • 33749032381 scopus 로고    scopus 로고
    • Mg2+-RNA interaction free energies and their relationship to the folding of RNA tertiary structures
    • Grilley, D.; Soto, A.M.; Draper, D.E. Mg2+-RNA interaction free energies and their relationship to the folding of RNA tertiary structures. Proc. Natl. Acad. Sci. USA 2006, 103, 14003-14008.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14003-14008
    • Grilley, D.1    Soto, A.M.2    Draper, D.E.3
  • 38
    • 0032542751 scopus 로고    scopus 로고
    • Na+ binding to cyclic and linear dipeptides. Bond energies, entropies of Na+ complexation, and attachment sites from the dissociation of Na+-bound heterodimers and ab initio calculations
    • Cerda, B.A.; Hoyau, S.; Ohanessian, G.; Wesdemiotis, C. Na+ binding to cyclic and linear dipeptides. Bond energies, entropies of Na+ complexation, and attachment sites from the dissociation of Na+-bound heterodimers and ab initio calculations. J. Am. Chem. Soc. 1998, 120, 2437-2448.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 2437-2448
    • Cerda, B.A.1    Hoyau, S.2    Ohanessian, G.3    Wesdemiotis, C.4
  • 39
    • 84989096273 scopus 로고
    • Proton and sodium ion of affinities of glycine and its sodium salt in the gas phase. Ab initio calculations
    • Bouchonnet, S.; Hoppilliard, Y. Proton and sodium ion of affinities of glycine and its sodium salt in the gas phase. Ab initio calculations. J. Mass Spectrom. 1992, 27, 71-76.
    • (1992) J. Mass Spectrom , vol.27 , pp. 71-76
    • Bouchonnet, S.1    Hoppilliard, Y.2
  • 40
    • 0000568801 scopus 로고
    • Structure and stability of complexes of glycine and glycine methyl analogs with H+, Li+, and Na+
    • Jensen, F. Structure and stability of complexes of glycine and glycine methyl analogs with H+, Li+, and Na+. J. Am. Chem. Soc. 1992, 114, 9533-9537.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 9533-9537
    • Jensen, F.1
  • 42
    • 0028881713 scopus 로고
    • Polymerase structures and function: Variations on a theme?
    • Joyce, C.M.; Steitz, T.A. Polymerase structures and function: Variations on a theme? J. Bacteriol. 1995, 177, 6321-6329.
    • (1995) J. Bacteriol , vol.177 , pp. 6321-6329
    • Joyce, C.M.1    Steitz, T.A.2
  • 43
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T.A. DNA polymerases: Structural diversity and common mechanisms. J. Biol. Chem. 1999, 274, 17395-17398.
    • (1999) J. Biol. Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 44
    • 66149149922 scopus 로고    scopus 로고
    • Determining nucleotide acidity and cation binding constants by 31P NMR
    • Song, Z.; Sims, A.; Eady, J.; Zhao, H.; Olubajo, O. Determining nucleotide acidity and cation binding constants by 31P NMR. Can. J. Anal. Sci. Spec. 2008, 53, 45-51.
    • (2008) Can. J. Anal. Sci. Spec , vol.53 , pp. 45-51
    • Song, Z.1    Sims, A.2    Eady, J.3    Zhao, H.4    Olubajo, O.5
  • 46
    • 0013936167 scopus 로고
    • Codon-anticodon pairing: The wobble hypothesis
    • Crick, F.H.C. Codon-anticodon pairing: The wobble hypothesis. J. Mol. Biol. 1966, 19, 548-555.
    • (1966) J. Mol. Biol , vol.19 , pp. 548-555
    • Crick, F.H.C.1
  • 48
    • 0026574207 scopus 로고
    • Recent evidence for evolution of the genetic code
    • Osawa, S.; Jukes, T.H.; Watanabe, K.; Muto, A. Recent evidence for evolution of the genetic code. Microbiol. Rev. 1992, 56, 229-264.
    • (1992) Microbiol. Rev , vol.56 , pp. 229-264
    • Osawa, S.1    Jukes, T.H.2    Watanabe, K.3    Muto, A.4
  • 49
    • 0033562547 scopus 로고    scopus 로고
    • Structural properties of DNA: RNA duplexes containing 2′-O-methyl and 2′-S-methyl substitutions: A molecular dynamics investigation
    • Venkateswarlu, D.; Lind, K.E.; Mohan, V.; Manoharan, M.; Ferguson, D.M. Structural properties of DNA:RNA duplexes containing 2′-O-methyl and 2′-S-methyl substitutions: A molecular dynamics investigation. Nucleic Acids Res. 1999, 27, 2189-2195.
    • (1999) Nucleic Acids Res , vol.27 , pp. 2189-2195
    • Venkateswarlu, D.1    Lind, K.E.2    Mohan, V.3    Manoharan, M.4    Ferguson, D.M.5
  • 50
    • 0036306877 scopus 로고    scopus 로고
    • Structural differences in the NOE-derived structure of G-T mismatched DNA relative to normal DNA are correlated with differences in 13C relaxation-based internal dynamics
    • Isaacs, R.J.; Rayens, W.S.; Spielmann, H.P. Structural differences in the NOE-derived structure of G-T mismatched DNA relative to normal DNA are correlated with differences in 13C relaxation-based internal dynamics. J. Mol. Biol. 2002, 319, 191-207.
    • (2002) J. Mol. Biol , vol.319 , pp. 191-207
    • Isaacs, R.J.1    Rayens, W.S.2    Spielmann, H.P.3
  • 52
    • 0005822936 scopus 로고
    • Improved estimation of secondary structure in ribonucleic acids
    • Tinoco, I., Jr.; Borer, P.N.; Dengler, B.; Levine, M.D. Improved estimation of secondary structure in ribonucleic acids. Nat. New Biol. 1973, 246, 40-41.
    • (1973) Nat. New Biol , vol.246 , pp. 40-41
    • Tinoco Jr., I.1    Borer, P.N.2    Dengler, B.3    Levine, M.D.4
  • 53
    • 2642655274 scopus 로고    scopus 로고
    • RNA-directed amino acid homochirality
    • Bailey, J.M. RNA-directed amino acid homochirality. FASEB J. 1998, 12, 503-507.
    • (1998) FASEB J , vol.12 , pp. 503-507
    • Bailey, J.M.1
  • 54
    • 0021119937 scopus 로고
    • Stereoselective aminoacylation of a dinucleotide monophosphate by the imidazolides of DL-alanine and N-(tert-butoxycarbonyl)-DL-alanine
    • Profy, A.T.; Usher, D.A. Stereoselective aminoacylation of a dinucleotide monophosphate by the imidazolides of DL-alanine and N-(tert-butoxycarbonyl)-DL-alanine. J. Mol. Evol. 1984, 20, 147-156.
    • (1984) J. Mol. Evol , vol.20 , pp. 147-156
    • Profy, A.T.1    Usher, D.A.2
  • 55
    • 0015215867 scopus 로고
    • Evidence for the interaction of nucleotides with immobilized amino-acids and its significance for the origin of the genetic code
    • Saxinger, C.; Ponnamperuma, C.; Woese, C. Evidence for the interaction of nucleotides with immobilized amino-acids and its significance for the origin of the genetic code. Nat. New Biol. 1971, 234, 172-174.
    • (1971) Nat. New Biol , vol.234 , pp. 172-174
    • Saxinger, C.1    Ponnamperuma, C.2    Woese, C.3
  • 56
    • 0017529971 scopus 로고
    • Nucleotide-binding site data and the origin of the genetic code
    • Walker, G.W. Nucleotide-binding site data and the origin of the genetic code. Biosystems 1977, 9, 139-150.
    • (1977) Biosystems , vol.9 , pp. 139-150
    • Walker, G.W.1
  • 57
    • 0020318628 scopus 로고
    • Molecular basis for the genetic code
    • Shimizu, M. Molecular basis for the genetic code. J. Mol. Evol. 1982, 18, 297-303.
    • (1982) J. Mol. Evol , vol.18 , pp. 297-303
    • Shimizu, M.1
  • 58
    • 0024295779 scopus 로고
    • A specific amino acid binding site composed of RNA
    • Yarus, M. A specific amino acid binding site composed of RNA. Science 1988, 240, 1751-1758.
    • (1988) Science , vol.240 , pp. 1751-1758
    • Yarus, M.1
  • 59
    • 0029257975 scopus 로고
    • Direct interaction between amino acids and nucleotides as a possible physicochemical basis for the origin of the genetic code
    • Hobish, M.K.; Wickramasinghe, N.S.; Ponnamperuma, C. Direct interaction between amino acids and nucleotides as a possible physicochemical basis for the origin of the genetic code. Adv. Space Res. 1995, 13, 365-382.
    • (1995) Adv. Space Res , vol.13 , pp. 365-382
    • Hobish, M.K.1    Wickramasinghe, N.S.2    Ponnamperuma, C.3
  • 60
    • 0034002683 scopus 로고    scopus 로고
    • RNA-ligand chemistry: A testable source for the genetic code
    • Yarus, M. RNA-ligand chemistry: A testable source for the genetic code. RNA 2000, 6, 475-484.
    • (2000) RNA , vol.6 , pp. 475-484
    • Yarus, M.1
  • 61
    • 21244459165 scopus 로고    scopus 로고
    • A more complex isoleucine aptamer with a cognate triplet
    • Legiewicz, M.; Yarus, M. A more complex isoleucine aptamer with a cognate triplet. J. Biol. Chem. 2005, 280, 19815-19822.
    • (2005) J. Biol. Chem , vol.280 , pp. 19815-19822
    • Legiewicz, M.1    Yarus, M.2
  • 62
    • 24744452849 scopus 로고    scopus 로고
    • RNA affinity for molecular L-histidine; genetic code origins
    • Majerfield, I.; Puthenvedu, D.; Yarus, M. RNA affinity for molecular L-histidine; genetic code origins. J. Mol. Evol. 2005, 61, 226-235.
    • (2005) J. Mol. Evol , vol.61 , pp. 226-235
    • Majerfield, I.1    Puthenvedu, D.2    Yarus, M.3
  • 63
    • 26944478623 scopus 로고    scopus 로고
    • A diminutive and specific RNA binding site for L-tryptophan
    • Majerfield, I.; Yarus, M. A diminutive and specific RNA binding site for L-tryptophan. Nucleic Acids Res. 2005, 33, 5482-5493.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5482-5493
    • Majerfield, I.1    Yarus, M.2
  • 64
    • 0019037440 scopus 로고
    • Structures of polypeptides with L- and D-residues, part III: Experimental evidence for enrichment in enantiomers
    • Brack, A.; Spach, G. Structures of polypeptides with L- and D-residues, part III: Experimental evidence for enrichment in enantiomers. J. Mol. Evol. 1980, 15, 231-238.
    • (1980) J. Mol. Evol , vol.15 , pp. 231-238
    • Brack, A.1    Spach, G.2
  • 65
    • 0019546705 scopus 로고
    • Enantiomer enrichment in early peptides
    • Brack, A.; Spach, G. Enantiomer enrichment in early peptides. Orig. Life 1981, 11, 135-142.
    • (1981) Orig. Life , vol.11 , pp. 135-142
    • Brack, A.1    Spach, G.2


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