메뉴 건너뛰기




Volumn 53, Issue 10, 2010, Pages 4119-4129

Sequence inversion and phenylalanine surrogates at the β-Turn enhance the antibiotic activity of gramicidin S

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; GRAMICIDIN S; PHENYLALANINE; PROLINE;

EID: 77952727721     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm100143f     Document Type: Article
Times cited : (38)

References (64)
  • 1
    • 41449111997 scopus 로고    scopus 로고
    • Host defense peptides and the new line of defence against multiresistant infections
    • Hirsch, T.; Jacobsen, F.; Steinau, H. U.; Steinstraesser, L. Host defense peptides and the new line of defence against multiresistant infections Protein Pept. Lett. 2008, 15, 238-243
    • (2008) Protein Pept. Lett. , vol.15 , pp. 238-243
    • Hirsch, T.1    Jacobsen, F.2    Steinau, H.U.3    Steinstraesser, L.4
  • 2
    • 37249047440 scopus 로고    scopus 로고
    • Novel alternatives to antibiotics: Bacteriophages, bacterial cell wall hydrolases, and antimicrobial peptides
    • Parisien, A.; Allain, B.; Zhang, J.; Mandeville, R.; Lan, C. Q. Novel alternatives to antibiotics: bacteriophages, bacterial cell wall hydrolases, and antimicrobial peptides J. Appl. Microbiol. 2008, 104, 1-13
    • (2008) J. Appl. Microbiol. , vol.104 , pp. 1-13
    • Parisien, A.1    Allain, B.2    Zhang, J.3    Mandeville, R.4    Lan, C.Q.5
  • 3
    • 0001131165 scopus 로고
    • Gramicidin S and its use in the treatment of infected wounds
    • Gause, G. F. Gramicidin S and its use in the treatment of infected wounds Nature 1944, 154, 703
    • (1944) Nature , vol.154 , pp. 703
    • Gause, G.F.1
  • 5
    • 0032694325 scopus 로고    scopus 로고
    • The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes
    • Prenner, E. J.; Lewis, R. N.; McElhaney, R. N. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes Biochim. Biophys. Acta 1999, 1462, 201-221
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 201-221
    • Prenner, E.J.1    Lewis, R.N.2    McElhaney, R.N.3
  • 6
    • 0018135890 scopus 로고
    • The crystal structure of a hydrated gramicidin S-urea complex
    • Hull, S. E.; Karlsson, R.; Main, P.; Woolfson, M. M.; Dodson, E. J. The crystal structure of a hydrated gramicidin S-urea complex Nature 1978, 275, 206-207
    • (1978) Nature , vol.275 , pp. 206-207
    • Hull, S.E.1    Karlsson, R.2    Main, P.3    Woolfson, M.M.4    Dodson, E.J.5
  • 7
    • 0001166130 scopus 로고
    • A crystallographic study of some derivatives of gramicidin S
    • Schmidt, G. M.; Hodgkin, D. C.; Oughton, B. M. A crystallographic study of some derivatives of gramicidin S Biochem. J. 1957, 65, 744-750
    • (1957) Biochem. J. , vol.65 , pp. 744-750
    • Schmidt, G.M.1    Hodgkin, D.C.2    Oughton, B.M.3
  • 9
    • 0016775558 scopus 로고
    • Conformational states and biological activity of cyclic peptides
    • Ovchinnikov, Y. A.; Ivanov, V. T. Conformational states and biological activity of cyclic peptides Tetrahedron 1975, 31, 2177-2209
    • (1975) Tetrahedron , vol.31 , pp. 2177-2209
    • Ovchinnikov, Y.A.1    Ivanov, V.T.2
  • 10
    • 55949121413 scopus 로고    scopus 로고
    • Interaction of gramicidin S and its aromatic amino-acid analogs with phospholipid membranes
    • Jelokhani-Niaraki, M.; Hodges, R. S.; Meissner, J. E.; Hassenstein, U. E.; Wheaton, L. Interaction of gramicidin S and its aromatic amino-acid analogs with phospholipid membranes Biophys. J. 2008, 95, 3306-3321
    • (2008) Biophys. J. , vol.95 , pp. 3306-3321
    • Jelokhani-Niaraki, M.1    Hodges, R.S.2    Meissner, J.E.3    Hassenstein, U.E.4    Wheaton, L.5
  • 11
    • 0022553466 scopus 로고
    • Mode of action of gramicidin S on Escherichia coli membrane
    • Katsu, T.; Kobayashi, H.; Fujita, Y. Mode of action of gramicidin S on Escherichia coli membrane Biochim. Biophys. Acta 1986, 860, 608-619
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 608-619
    • Katsu, T.1    Kobayashi, H.2    Fujita, Y.3
  • 14
    • 0014170490 scopus 로고
    • Studies of peptide antibiotics. XII. Syntheses of [2,2′-α,- diaminobutyric acid]-and [2,2′-lysine]-gramicidin S
    • Waki, M.; Abe, O.; Okawa, R.; Kato, T.; Makisumi, S.; Izumiya, N. Studies of peptide antibiotics. XII. Syntheses of [2,2′-α,γ- diaminobutyric acid]-and [2,2′-lysine]-gramicidin S Bull. Chem. Soc. Jpn. 1967, 40, 2904-2909
    • (1967) Bull. Chem. Soc. Jpn. , vol.40 , pp. 2904-2909
    • Waki, M.1    Abe, O.2    Okawa, R.3    Kato, T.4    Makisumi, S.5    Izumiya, N.6
  • 15
    • 0038334471 scopus 로고
    • 4,4′]-GS, by a novel method
    • 4,4′]-GS, by a novel method Bull. Chem. Soc. Jpn. 1988, 61, 2220-2222
    • (1988) Bull. Chem. Soc. Jpn. , vol.61 , pp. 2220-2222
    • Aimoto, S.1
  • 18
    • 14044275667 scopus 로고    scopus 로고
    • Proline residue-modified polycationic analogs of gramicidin S with high antibacterial activity against both Gram-positive and Gram-negative bacteria and low hemolytic activity
    • Kawai, M.; Yamamura, H.; Tanaka, R.; Umemoto, H.; Ohmizo, C.; Higuchi, S.; Katsu, T. Proline residue-modified polycationic analogs of gramicidin S with high antibacterial activity against both Gram-positive and Gram-negative bacteria and low hemolytic activity J. Pept. Res. 2005, 65, 98-104
    • (2005) J. Pept. Res. , vol.65 , pp. 98-104
    • Kawai, M.1    Yamamura, H.2    Tanaka, R.3    Umemoto, H.4    Ohmizo, C.5    Higuchi, S.6    Katsu, T.7
  • 19
    • 0037539998 scopus 로고    scopus 로고
    • Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S
    • Lee, D. L.; Hodges, R. S. Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S Biopolymers 2003, 71, 28-48
    • (2003) Biopolymers , vol.71 , pp. 28-48
    • Lee, D.L.1    Hodges, R.S.2
  • 20
    • 0027324832 scopus 로고
    • Protein β-turn mimetics II: Design, synthesis and evaluation in the cyclic peptide gramicidin S
    • Ripka, W. C.; Delucca, G. V.; Bach, A. C.; Pottorf, R. S.; Blaney, J. M. Protein β-turn mimetics II: Design, synthesis and evaluation in the cyclic peptide gramicidin S Tetrahedron 1993, 49, 3609-3628
    • (1993) Tetrahedron , vol.49 , pp. 3609-3628
    • Ripka, W.C.1    Delucca, G.V.2    Bach, A.C.3    Pottorf, R.S.4    Blaney, J.M.5
  • 21
    • 0022587556 scopus 로고
    • 5,5′]-Gramicidin S predicted from β-turn preference of its partial sequence
    • 5,5′]- Gramicidin S predicted from β-turn preference of its partial sequence Bull. Chem. Soc. Jpn. 1986, 59, 535-538
    • (1986) Bull. Chem. Soc. Jpn. , vol.59 , pp. 535-538
    • Sato, K.1    Kato, R.2    Nagai, U.3
  • 22
    • 0021797568 scopus 로고
    • Synthesis and properties of gramicidin S analogs containing Pro- d -Phe sequence in place of d -Phe-Pro sequence in the β-turn part of the antibiotic
    • Tamaki, M.; Okitsu, T.; Araki, M.; Sakamoto, H.; Takimoto, M.; Muramatsu, I. Synthesis and properties of gramicidin S analogs containing Pro- d -Phe sequence in place of d -Phe-Pro sequence in the β-turn part of the antibiotic Bull. Chem. Soc. Jpn. 1985, 58, 531-535
    • (1985) Bull. Chem. Soc. Jpn. , vol.58 , pp. 531-535
    • Tamaki, M.1    Okitsu, T.2    Araki, M.3    Sakamoto, H.4    Takimoto, M.5    Muramatsu, I.6
  • 24
    • 33845936302 scopus 로고    scopus 로고
    • Synthesis of low-hemolytic antimicrobial dehydropeptides based on gramicidin S
    • Yamada, K.; Shinoda, S. S.; Oku, H.; Komagoe, K.; Katsu, T.; Katakai, R. Synthesis of low-hemolytic antimicrobial dehydropeptides based on gramicidin S J. Med. Chem. 2006, 49, 7592-7595
    • (2006) J. Med. Chem. , vol.49 , pp. 7592-7595
    • Yamada, K.1    Shinoda, S.S.2    Oku, H.3    Komagoe, K.4    Katsu, T.5    Katakai, R.6
  • 26
    • 0034254229 scopus 로고    scopus 로고
    • Diastereoisomeric analogs of gramicidin S: Structure, biological activity and interaction with lipid bilayers
    • Jelokhani-Niaraki, M.; Kondejewski, L. H.; Farmer, S. W.; Hancock, R. E.; Kay, C. M.; Hodges, R. S. Diastereoisomeric analogs of gramicidin S: structure, biological activity and interaction with lipid bilayers Biochem. J. 2000, 349, 747-755
    • (2000) Biochem. J. , vol.349 , pp. 747-755
    • Jelokhani-Niaraki, M.1    Kondejewski, L.H.2    Farmer, S.W.3    Hancock, R.E.4    Kay, C.M.5    Hodges, R.S.6
  • 27
    • 0033532175 scopus 로고    scopus 로고
    • Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity
    • Kondejewski, L. H.; Jelokhani-Niaraki, M.; Farmer, S. W.; Lix, B.; Kay, C. M.; Sykes, B. D.; Hancock, R. E.; Hodges, R. S. Dissociation of antimicrobial and hemolytic activities in cyclic peptide diastereomers by systematic alterations in amphipathicity J. Biol. Chem. 1999, 274, 13181-13192
    • (1999) J. Biol. Chem. , vol.274 , pp. 13181-13192
    • Kondejewski, L.H.1    Jelokhani-Niaraki, M.2    Farmer, S.W.3    Lix, B.4    Kay, C.M.5    Sykes, B.D.6    Hancock, R.E.7    Hodges, R.S.8
  • 28
    • 34548514215 scopus 로고    scopus 로고
    • The relationship between the binding to and permeabilization of phospholipid bilayer membranes by GS14dK4, a designed analog of the antimicrobial peptide gramicidin S
    • Abraham, T.; Marwaha, S.; Kobewka, D. M.; Lewis, R. N.; Prenner, E. J.; Hodges, R. S.; McElhaney, R. N. The relationship between the binding to and permeabilization of phospholipid bilayer membranes by GS14dK4, a designed analog of the antimicrobial peptide gramicidin S Biochim. Biophys. Acta 2007, 1768, 2089-2098
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2089-2098
    • Abraham, T.1    Marwaha, S.2    Kobewka, D.M.3    Lewis, R.N.4    Prenner, E.J.5    Hodges, R.S.6    McElhaney, R.N.7
  • 29
    • 0017871978 scopus 로고
    • Comparison of conformation and antimicrobial activity of synthetic analogs of gramicidin S: Stereochemical considerations of the role of d -phenylalanine in the antibiotic
    • Kawai, M.; Nagai, U. Comparison of conformation and antimicrobial activity of synthetic analogs of gramicidin S: stereochemical considerations of the role of d -phenylalanine in the antibiotic Biopolymers 1978, 17, 1549-1565
    • (1978) Biopolymers , vol.17 , pp. 1549-1565
    • Kawai, M.1    Nagai, U.2
  • 30
    • 0023002443 scopus 로고
    • Gramicidin S analogs with a d -Ala, Gly, or l -Ala residue in place of the d -Phe residue: Molecular conformations and interactions with phospholipid membrane
    • Higashijima, T.; Miyazawa, T.; Kawai, M.; Nagai, U. Gramicidin S analogs with a d -Ala, Gly, or l -Ala residue in place of the d -Phe residue: molecular conformations and interactions with phospholipid membrane Biopolymers 1986, 25, 2295-2307
    • (1986) Biopolymers , vol.25 , pp. 2295-2307
    • Higashijima, T.1    Miyazawa, T.2    Kawai, M.3    Nagai, U.4
  • 31
    • 0019967509 scopus 로고
    • Studies of peptide antibiotics. XLIII. Syntheses of gramicidin S analogs containing d -serine or dehydroalanine in place of d -phenylalanine and asymmetric hydrogenation of the dehydroalanine residue
    • Ando, S.; Aoyagi, H.; Waki, M.; Kato, T.; Izumiya, N. Studies of peptide antibiotics. XLIII. Syntheses of gramicidin S analogs containing d -serine or dehydroalanine in place of d -phenylalanine and asymmetric hydrogenation of the dehydroalanine residue Tetrahedron Lett. 1982, 23, 2195-2198
    • (1982) Tetrahedron Lett. , vol.23 , pp. 2195-2198
    • Ando, S.1    Aoyagi, H.2    Waki, M.3    Kato, T.4    Izumiya, N.5
  • 34
    • 0030068665 scopus 로고    scopus 로고
    • Crystal structures of peptides and modified peptides
    • Marraud, M.; Aubry, A. Crystal structures of peptides and modified peptides Biopolymers (Pept. Sci.) 1996, 40, 45-83
    • (1996) Biopolymers (Pept. Sci.) , vol.40 , pp. 45-83
    • Marraud, M.1    Aubry, A.2
  • 35
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson, E. G.; Thornton, J. M. A revised set of potentials for beta-turn formation in proteins Protein Sci. 1994, 3, 2207-2216
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 36
    • 0032560953 scopus 로고    scopus 로고
    • β-Turn preferences induced by 2,3-methanophenylalanine chirality
    • Jiménez, A. I.; Cativiela, C.; Aubry, A.; Marraud, M. β-Turn preferences induced by 2,3-methanophenylalanine chirality J. Am. Chem. Soc. 1998, 120, 9452-9459
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9452-9459
    • Jiménez, A.I.1    Cativiela, C.2    Aubry, A.3    Marraud, M.4
  • 37
    • 0035552035 scopus 로고    scopus 로고
    • Control of peptide conformation by the Thorpe-Ingold effect (Cα-tetrasubstitution)
    • Toniolo, C.; Crisma, M.; Formaggio, F.; Peggion, C. Control of peptide conformation by the Thorpe-Ingold effect (Cα-tetrasubstitution) Biopolymers (Pept. Sci.) 2001, 60, 396-419
    • (2001) Biopolymers (Pept. Sci.) , vol.60 , pp. 396-419
    • Toniolo, C.1    Crisma, M.2    Formaggio, F.3    Peggion, C.4
  • 38
    • 0035833093 scopus 로고    scopus 로고
    • Facile synthesis and highly efficient resolution of a constrained cyclopropane analog of phenylalanine
    • Jiménez, A. I.; López, P.; Oliveros, L.; Cativiela, C. Facile synthesis and highly efficient resolution of a constrained cyclopropane analog of phenylalanine Tetrahedron 2001, 57, 6019-6026
    • (2001) Tetrahedron , vol.57 , pp. 6019-6026
    • Jiménez, A.I.1    López, P.2    Oliveros, L.3    Cativiela, C.4
  • 40
    • 33749257457 scopus 로고    scopus 로고
    • Synthesis of enantiomerically pure β,β-diphenylalanine (Dip) and fluorenylglycine (Flg)
    • Royo, S.; Jiménez, A. I.; Cativiela, C. Synthesis of enantiomerically pure β,β-diphenylalanine (Dip) and fluorenylglycine (Flg) Tetrahedron: Asymmetry 2006, 17, 2393-2400
    • (2006) Tetrahedron: Asymmetry , vol.17 , pp. 2393-2400
    • Royo, S.1    Jiménez, A.I.2    Cativiela, C.3
  • 41
    • 3843150624 scopus 로고    scopus 로고
    • Synthesis and modification of dibenzylglycine derivatives via the Suzuki-Miyaura coupling reaction
    • Kotha, S.; Behera, M. Synthesis and modification of dibenzylglycine derivatives via the Suzuki-Miyaura coupling reaction J. Pept. Res. 2004, 64, 72-85
    • (2004) J. Pept. Res. , vol.64 , pp. 72-85
    • Kotha, S.1    Behera, M.2
  • 42
    • 0028129407 scopus 로고
    • Convenient one-pot method for formylation of amines and alcohols using formic acid and 1,1′-oxalyldiimidazole
    • Kitagawa, T.; Arita, J.; Nogahata, A. Convenient one-pot method for formylation of amines and alcohols using formic acid and 1,1′- oxalyldiimidazole Chem. Pharm. Bull. (Tokyo) 1994, 42, 1655-1657
    • (1994) Chem. Pharm. Bull. (Tokyo) , vol.42 , pp. 1655-1657
    • Kitagawa, T.1    Arita, J.2    Nogahata, A.3
  • 43
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of the nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of the nearest-neighbor effects J. Biomol. NMR 1995, 5, 67-81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 45
    • 0034744426 scopus 로고    scopus 로고
    • β chemical shifts as a tool to delineate β-hairpin structures in peptides
    • β chemical shifts as a tool to delineate β-hairpin structures in peptides J. Biomol. NMR 2001, 19, 331-345
    • (2001) J. Biomol. NMR , vol.19 , pp. 331-345
    • Santiveri, C.M.1    Rico, M.2    Jiménez, M.A.3
  • 46
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S.; Sykes, B. D.; Richards, F. M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure J. Mol. Biol. 1991, 222, 311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 47
    • 0034488879 scopus 로고    scopus 로고
    • Position effect of cross-strand side-chain interactions on beta-hairpin formation
    • Santiveri, C. M.; Rico, M.; Jiménez, M. A. Position effect of cross-strand side-chain interactions on beta-hairpin formation Protein Sci. 2000, 9, 2151-2160
    • (2000) Protein Sci. , vol.9 , pp. 2151-2160
    • Santiveri, C.M.1    Rico, M.2    Jiménez, M.A.3
  • 49
    • 0037016737 scopus 로고    scopus 로고
    • Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework
    • Kondejewski, L. H.; Lee, D. L.; Jelokhani-Niaraki, M.; Farmer, S. W.; Hancock, R. E. W.; Hodges, R. S. Optimization of microbial specificity in cyclic peptides by modulation of hydrophobicity within a defined structural framework J. Biomol. Chem. 2002, 1, 67-74
    • (2002) J. Biomol. Chem. , vol.1 , pp. 67-74
    • Kondejewski, L.H.1    Lee, D.L.2    Jelokhani-Niaraki, M.3    Farmer, S.W.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 50
    • 0034640414 scopus 로고    scopus 로고
    • Development of the structural basis for antimicrobial and hemolytic activities of peptides based on gramicidin S and design of novel analogs using NMR spectroscopy
    • McInnes, C.; Kondejewski, L. H.; Hodges, R. S.; Sykes, B. D. Development of the structural basis for antimicrobial and hemolytic activities of peptides based on gramicidin S and design of novel analogs using NMR spectroscopy J. Biol. Chem. 2000, 275, 14287-14294
    • (2000) J. Biol. Chem. , vol.275 , pp. 14287-14294
    • McInnes, C.1    Kondejewski, L.H.2    Hodges, R.S.3    Sykes, B.D.4
  • 51
    • 33845973364 scopus 로고    scopus 로고
    • The medicinal chemistry of short lactoferricin-based antibacterial peptides
    • Haug, B. E.; Strøm, M. B.; Svendsen, J. S. The medicinal chemistry of short lactoferricin-based antibacterial peptides Curr. Med. Chem. 2007, 14, 1-18
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1-18
    • Haug, B.E.1    Strøm, M.B.2    Svendsen, J.S.3
  • 54
    • 0034424412 scopus 로고    scopus 로고
    • Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa
    • Zhang, L.; Dhillon, P.; Yan, H.; Farmer, S.; Hancock, R. E. Interactions of bacterial cationic peptide antibiotics with outer and cytoplasmic membranes of Pseudomonas aeruginosa Antimicrob. Agents Chemother. 2000, 44, 3317-3321
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3317-3321
    • Zhang, L.1    Dhillon, P.2    Yan, H.3    Farmer, S.4    Hancock, R.E.5
  • 56
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnölzer, M.; Alewood, P.; Jones, A.; Alewood, D.; Kent, S. B. In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences Int. J. Pept. Protein Res. 1992, 40, 180-193
    • (1992) Int. J. Pept. Protein Res. , vol.40 , pp. 180-193
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 57
    • 0014772602 scopus 로고
    • Color test for detection of free terminal amino groups in solid-phase synthesis of peptides
    • Kaiser, E.; Colescott, R. L.; Bossinger, C. D.; Cook, P. I. Color test for detection of free terminal amino groups in solid-phase synthesis of peptides Anal. Biochem. 1970, 34, 595-598
    • (1970) Anal. Biochem. , vol.34 , pp. 595-598
    • Kaiser, E.1    Colescott, R.L.2    Bossinger, C.D.3    Cook, P.I.4
  • 59
    • 0022713369 scopus 로고
    • Two-dimensional nuclear magnetic resonance spectroscopy
    • Bax, A.; Lerner, L. Two-dimensional nuclear magnetic resonance spectroscopy Science 1986, 232, 960-967
    • (1986) Science , vol.232 , pp. 960-967
    • Bax, A.1    Lerner, L.2
  • 60
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids: IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy
    • Markley, J. L.; Bax, A.; Arata, Y.; Hilbers, C. W.; Kaptein, R.; Sykes, B. D.; Wright, P. E.; Wüthrich, K. Recommendations for the presentation of NMR structures of proteins and nucleic acids-IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy J. Biomol. NMR 1998, 12, 1-23 (Pubitemid 128512831)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.1 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6    Wright, P.E.7    Wuthrich, K.8
  • 61
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich, K.; Billeter, M.; Braun, W. Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances J. Mol. Biol. 1984, 180, 715-740
    • (1984) J. Mol. Biol. , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 62
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert, P. Automated NMR structure calculation with CYANA Methods Mol. Biol. 2004, 278, 353-378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 63
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R.; Billeter, M.; Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graphics 1996, 14 (51-55) 29-32
    • (1996) J. Mol. Graphics , vol.14 , Issue.51-55 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 64
    • 0001752768 scopus 로고    scopus 로고
    • The cambridge structural database: A quarter of a million crystal structures and rising
    • Allen, F. H. The Cambridge Structural Database: a quarter of a million crystal structures and rising Acta Crystallogr., Sect. B: Struct. Sci. 2002, 58, 380-388
    • (2002) Acta Crystallogr., Sect. B: Struct. Sci. , vol.58 , pp. 380-388
    • Allen, F.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.