메뉴 건너뛰기




Volumn 70, Issue 4, 2008, Pages 1389-1407

Prolylproline unit in model peptides and in fragments from databases

Author keywords

Cis trans isomerism; Inverse turn; Pro pro conformers; Pseudorotation; Ring puckering; turn types I, III, Via, and VIb

Indexed keywords

COLLAGEN; CYCLOPEPTIDE; DNA GLYCOSYLTRANSFERASE; FORMYLPROLYLPROLINAMIDE; PROLINE; THROMBIN; UNCLASSIFIED DRUG;

EID: 39749164049     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21630     Document Type: Article
Times cited : (12)

References (69)
  • 1
    • 0025113022 scopus 로고
    • β‐Turns and their distortions: a proposed new nomenclature
    • 1 Wilmot CM, Thornton JM. β‐Turns and their distortions: a proposed new nomenclature. Protein Eng 1990 ; 3 (6): 479–493, and references therein.
    • (1990) Protein Eng , vol.3 , Issue.6 , pp. 479-493
    • Wilmot, CM1    Thornton, JM2
  • 2
    • 18844465959 scopus 로고    scopus 로고
    • Vicinal disulfide bridge conformers by experimental methods and by ab initio and DFT molecular computations
    • 2 Hudáky I, Gáspári Z, Carugo O, Čemažar M, Pongor S, Perczel A. Vicinal disulfide bridge conformers by experimental methods and by ab initio and DFT molecular computations. Proteins 2004 ; 55: 152–168, and references therein.
    • (2004) Proteins , vol.55 , pp. 152-168
    • Hudáky, I1    Gáspári, Z2    Carugo, O3    Čemažar, M4    Pongor, S5    Perczel, A6
  • 3
    • 0016390659 scopus 로고
    • Conformation of the lithium ion complex of antamanide, a cyclic decapeptide and ion carrier, in the crystalline state
    • 3 Karle IL. Conformation of the lithium ion complex of antamanide, a cyclic decapeptide and ion carrier, in the crystalline state. J Am Chem Soc 1974 ; 96: 4000–4006.
    • (1974) J Am Chem Soc , vol.96 , pp. 4000-4006
    • Karle, IL1
  • 5
    • 0030914853 scopus 로고    scopus 로고
    • Solution state conformation of an immunosuppressive cyclic dodecapeptide, cycloleonurinin
    • 5 Morita H, Gonda A, Takeya K, Itokawa H, Hirano T, Oka K, Shirota O. Solution state conformation of an immunosuppressive cyclic dodecapeptide, cycloleonurinin. Tetrahedron 1997 ; 53: 7469–7478.
    • (1997) Tetrahedron , vol.53 , pp. 7469-7478
    • Morita, H1    Gonda, A2    Takeya, K3    Itokawa, H4    Hirano, T5    Oka, K6    Shirota, O7
  • 6
    • 0031550605 scopus 로고    scopus 로고
    • Cycloleonuripeptide D, a new proline‐rich cyclic decapeptide from Leonurus heterophyllus
    • 6 Morita H, Gonda A, Takeya K, Itokawa H, Iitaka Y. Cycloleonuripeptide D, a new proline‐rich cyclic decapeptide from Leonurus heterophyllus. Tetrahedron 1997 ; 53: 1617–1626.
    • (1997) Tetrahedron , vol.53 , pp. 1617-1626
    • Morita, H1    Gonda, A2    Takeya, K3    Itokawa, H4    Iitaka, Y5
  • 7
    • 1042268143 scopus 로고    scopus 로고
    • Three‐finger α‐neurotoxins and the nicotonoc acetylcholine receptor, forty years on
    • 7 Nirthanan S, Gwee MCE. Three‐finger α‐neurotoxins and the nicotonoc acetylcholine receptor, forty years on. J Pharmacol Sci 2004 ; 94: 1–17.
    • (2004) J Pharmacol Sci , vol.94 , pp. 1-17
    • Nirthanan, S1    Gwee, MCE2
  • 8
    • 0027371744 scopus 로고
    • NMR solution structure of an α‐bungarotoxin/nicotinic receptor peptide complex
    • 8 Basus VJ, Song G, Hawrot E. NMR solution structure of an α‐bungarotoxin/nicotinic receptor peptide complex. Biochemistry 1993 ; 32: 12290–12298.
    • (1993) Biochemistry , vol.32 , pp. 12290-12298
    • Basus, VJ1    Song, G2    Hawrot, E3
  • 9
    • 0022943266 scopus 로고
    • The crystal structure of alpha‐bungarotoxin at 2.5 Å resolution: relation to solution structure and binding to acetylcholine receptor
    • 9 Love RA, Stroud RM. The crystal structure of alpha‐bungarotoxin at 2.5 Å resolution: relation to solution structure and binding to acetylcholine receptor. Protein Eng 1986 ; 1: 37–46.
    • (1986) Protein Eng , vol.1 , pp. 37-46
    • Love, RA1    Stroud, RM2
  • 10
    • 0037130458 scopus 로고    scopus 로고
    • The mechanism for acetylcholine receptor inhibition by α‐neurotoxins and species‐specific resistance to α‐bungarotoxin revealed by NMR
    • 10 Samson AO, Scherf T, Eisenstein M, Chill JH, Anglister J. The mechanism for acetylcholine receptor inhibition by α‐neurotoxins and species‐specific resistance to α‐bungarotoxin revealed by NMR. Neuron 2002 ; 35: 319–332.
    • (2002) Neuron , vol.35 , pp. 319-332
    • Samson, AO1    Scherf, T2    Eisenstein, M3    Chill, JH4    Anglister, J5
  • 11
    • 0026613082 scopus 로고
    • 1.9‐Å resolution structure of fasciculin‐1, an anti‐acetylcholinesterase toxin from green mamba snake venom
    • 11 Le Du MH, Marchot P, Bougis PE, Fontecilla‐Camps JC. 1.9‐Å resolution structure of fasciculin‐1, an anti‐acetylcholinesterase toxin from green mamba snake venom. J Biol Chem 1992 ; 267: 22122–22130.
    • (1992) J Biol Chem , vol.267 , pp. 22122-22130
    • Le Du, MH1    Marchot, P2    Bougis, PE3    Fontecilla‐Camps, JC4
  • 12
    • 0028306665 scopus 로고
    • X‐ray Structure at 1.55 Å of toxin γ, a cardiotoxin from Naja nigricolis venom
    • 12 Bilwes A, Rees B, Moras D, Ménez R, Ménez A. X‐ray Structure at 1.55 Å of toxin γ, a cardiotoxin from Naja nigricolis venom. J Mol Biol 1994 ; 239: 122–136.
    • (1994) J Mol Biol , vol.239 , pp. 122-136
    • Bilwes, A1    Rees, B2    Moras, D3    Ménez, R4    Ménez, A5
  • 13
    • 0027217436 scopus 로고
    • Determination of the NMR solution structure of cardiotoxin CTX‐IIb from Naja mossambica mossambica
    • 13 O'Connell JF, Bougis PE, Wuthrich K. Determination of the NMR solution structure of cardiotoxin CTX‐IIb from Naja mossambica mossambica. Eur J Biochem 1993 ; 213: 891–900.
    • (1993) Eur J Biochem , vol.213 , pp. 891-900
    • O'Connell, JF1    Bougis, PE2    Wuthrich, K3
  • 14
    • 0026472379 scopus 로고
    • 3‐dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study
    • 14 Zinn‐Justin S, Roumestand C, Gilquin B, Bontems F, Menez A, Toma F. 3‐dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study. Biochemistry 1992 ; 31: 11335–11347.
    • (1992) Biochemistry , vol.31 , pp. 11335-11347
    • Zinn‐Justin, S1    Roumestand, C2    Gilquin, B3    Bontems, F4    Menez, A5    Toma, F6
  • 15
    • 0344972098 scopus 로고    scopus 로고
    • Three‐dimensional solution structure of conotoxin ψ‐PIIIE, an acetylcholine gated ion channel antagonist
    • 15 Mitchell SS, Shon KJ, Foster MP, Davis DR, Olivera BM, Ireland CM. Three‐dimensional solution structure of conotoxin ψ‐PIIIE, an acetylcholine gated ion channel antagonist. Biochemistry 1998 ; 37: 1215–1220.
    • (1998) Biochemistry , vol.37 , pp. 1215-1220
    • Mitchell, SS1    Shon, KJ2    Foster, MP3    Davis, DR4    Olivera, BM5    Ireland, CM6
  • 16
    • 0038010721 scopus 로고    scopus 로고
    • Characterization and three‐dimensional solution structure determination of ψ‐conotoxin PIIIF, a novel antagonist of acetylcholine receptors
    • 16 Van Wagoner RM, Jacobsen RB, Olivera BM, Ireland CM. Characterization and three‐dimensional solution structure determination of ψ‐conotoxin PIIIF, a novel antagonist of acetylcholine receptors. Biochemistry 2003 ; 42: 6353–6362.
    • (2003) Biochemistry , vol.42 , pp. 6353-6362
    • Van Wagoner, RM1    Jacobsen, RB2    Olivera, BM3    Ireland, CM4
  • 17
    • 0031569801 scopus 로고    scopus 로고
    • Solution structure of the sodium channel antagonist conotoxin GS: a new molecular caliper for probing sodium channel geometry
    • 17 Hill JM, Alewood PF, Craik DJ. Solution structure of the sodium channel antagonist conotoxin GS: a new molecular caliper for probing sodium channel geometry. Structure 1997 ; 5: 571–583.
    • (1997) Structure , vol.5 , pp. 571-583
    • Hill, JM1    Alewood, PF2    Craik, DJ3
  • 18
    • 0033863552 scopus 로고    scopus 로고
    • Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three‐dimensional solution structure
    • 18 Hill JM, Alewood PF, Craik DJ. Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three‐dimensional solution structure. Eur J Biochem 2000 ; 267: 4649–4657.
    • (2000) Eur J Biochem , vol.267 , pp. 4649-4657
    • Hill, JM1    Alewood, PF2    Craik, DJ3
  • 19
    • 0027078665 scopus 로고
    • Structure–activity relationships of μ‐conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations
    • 19 Wakamatsu K, Kohda D, Hatanaka H, Lancelin J‐M, Ishida Y, Oya M, Nakamura H, Inagaki F, Sato K. Structure–activity relationships of μ‐conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry 1992 ; 31: 12577–12584.
    • (1992) Biochemistry , vol.31 , pp. 12577-12584
    • Wakamatsu, K1    Kohda, D2    Hatanaka, H3    Lancelin, J‐M4    Ishida, Y5    Oya, M6    Nakamura, H7    Inagaki, F8    Sato, K9
  • 20
    • 0030016085 scopus 로고    scopus 로고
    • Three‐dimensional solution structure of μ‐conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels
    • 20 Hill JM, Alewood PF, Craik DJ. Three‐dimensional solution structure of μ‐conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels. Biochemistry 1996 ; 35: 8824–8835.
    • (1996) Biochemistry , vol.35 , pp. 8824-8835
    • Hill, JM1    Alewood, PF2    Craik, DJ3
  • 21
    • 0027177515 scopus 로고
    • The role of thrombin's Tyr–Pro–Pro–Trp motif in the interaction with fibrinogen, thrombomodulin, protein‐C, antithrombin‐III, and the Kunitz inhibitors
    • 21 Le Bonniec BF, Guinto ER, MacGillivray RTA, Stone ST, Esmon CT. The role of thrombin's Tyr–Pro–Pro–Trp motif in the interaction with fibrinogen, thrombomodulin, protein‐C, antithrombin‐III, and the Kunitz inhibitors. J Biol Chem 1993 ; 268: 19055–11961.
    • (1993) J Biol Chem , vol.268 , pp. 19055-11961
    • Le Bonniec, BF1    Guinto, ER2    MacGillivray, RTA3    Stone, ST4    Esmon, CT5
  • 22
    • 0025837452 scopus 로고
    • Crystallographic analysis At 3.0‐Å resolution of the binding to human thrombin of four active site‐directed inhibitors
    • 22 Banner DW, Hadváry P. Crystallographic analysis At 3.0‐Å resolution of the binding to human thrombin of four active site‐directed inhibitors. J Biol Chem 1991 ; 266: 20085–20093.
    • (1991) J Biol Chem , vol.266 , pp. 20085-20093
    • Banner, DW1    Hadváry, P2
  • 23
    • 0033120232 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited
    • 23 Xiao G, Todorova M, Jagadeesh J, Drohat AC, Stivers JT, Gilliland GL. Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited. Proteins Struct Funct Genetics 1999 ; 35: 13–24.
    • (1999) Proteins Struct Funct Genetics , vol.35 , pp. 13-24
    • Xiao, G1    Todorova, M2    Jagadeesh, J3    Drohat, AC4    Stivers, JT5    Gilliland, GL6
  • 24
    • 0028934537 scopus 로고
    • Crystal‐structure of human uracil‐DNA glycosylase in complex with a protein inhibitor—protein mimicry of DNA
    • 24 Mol CD, Arvai AS, Sanderson RJ, Slupphaug G, Kavli B, Krokan HE, Mosbaugh DW, Tainer JA. Crystal‐structure of human uracil‐DNA glycosylase in complex with a protein inhibitor—protein mimicry of DNA. Cell 1995 ; 80: 869–878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, CD1    Arvai, AS2    Sanderson, RJ3    Slupphaug, G4    Kavli, B5    Krokan, HE6    Mosbaugh, DW7    Tainer, JA8
  • 25
    • 0028959237 scopus 로고
    • The structural basis of specific base‐excision repair by uracil–DNA glycosylase
    • 25 Savva R, McAuley‐Hecht K, Brown T, Pearl L. The structural basis of specific base‐excision repair by uracil–DNA glycosylase. Nature 1995 ; 373: 487–493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R1    McAuley‐Hecht, K2    Brown, T3    Pearl, L4
  • 26
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: the interaction of proline‐rich motifs in signaling proteins with their cognate domains
    • 26 Kay BK, Williamson MP, Sudol M. The importance of being proline: the interaction of proline‐rich motifs in signaling proteins with their cognate domains. FASEB J 2000 ; 14: 231–241.
    • (2000) FASEB J , vol.14 , pp. 231-241
    • Kay, BK1    Williamson, MP2    Sudol, M3
  • 27
    • 0036008212 scopus 로고    scopus 로고
    • Solution structure of N‐terminal SH3 domain of Vav and the recognition site for Grb2 C‐terminal SH3 domain
    • 27 Ogura K, Nagata K, Horiuchi M, Ebisui E, Hasuda T, Yuzawa S, Nishida M, Hatanaka H, Inagaki F. Solution structure of N‐terminal SH3 domain of Vav and the recognition site for Grb2 C‐terminal SH3 domain. J Biomol NMR 2002 ; 22: 37.
    • (2002) J Biomol NMR , vol.22 , pp. 37
    • Ogura, K1    Nagata, K2    Horiuchi, M3    Ebisui, E4    Hasuda, T5    Yuzawa, S6    Nishida, M7    Hatanaka, H8    Inagaki, F9
  • 28
    • 0032799032 scopus 로고    scopus 로고
    • Molecular and cellular analysis of Grb2 SH3 domain mutants: interaction with Sos and dynamin
    • 28 Vidal M, Goudreau N, Cornille F, Cussac D, Gincel E, Garbay C. Molecular and cellular analysis of Grb2 SH3 domain mutants: interaction with Sos and dynamin. J Mol Biol 1999 ; 290: 717–730.
    • (1999) J Mol Biol , vol.290 , pp. 717-730
    • Vidal, M1    Goudreau, N2    Cornille, F3    Cussac, D4    Gincel, E5    Garbay, C6
  • 29
    • 0032555743 scopus 로고    scopus 로고
    • Crystal structure of the Abl‐SH3 domain complexed with a designed high‐affinity peptide ligand: implications for SH3‐ligand interactions
    • 29 Pisabarro MT, Serrano L, Wilmanns M. Crystal structure of the Abl‐SH3 domain complexed with a designed high‐affinity peptide ligand: implications for SH3‐ligand interactions. J Mol Biol 1998 ; 281: 513–521.
    • (1998) J Mol Biol , vol.281 , pp. 513-521
    • Pisabarro, MT1    Serrano, L2    Wilmanns, M3
  • 31
    • 0034741217 scopus 로고    scopus 로고
    • Ca2+‐independent binding of an EF‐hand domain to a novel motif in the α‐actinin–titin complex
    • 31 Atkinson RA, Joseph C, Kelly G, Muskett FW, Frenkiel TA, Nietlispach D, Pastore A. Ca 2+ ‐independent binding of an EF‐hand domain to a novel motif in the α‐actinin–titin complex. Nat Struct Biol 2001 ; 8: 853–857.
    • (2001) Nat Struct Biol , vol.8 , pp. 853-857
    • Atkinson, RA1    Joseph, C2    Kelly, G3    Muskett, FW4    Frenkiel, TA5    Nietlispach, D6    Pastore, A7
  • 32
    • 0034681942 scopus 로고    scopus 로고
    • Site‐Specific NMR Monitoring of cis–trans isomerization in the folding of the proline‐rich collagen triple helix
    • 32 Buevich AV, Dai Q‐H, Liu X, Brodsky B, Baum J. Site‐Specific NMR Monitoring of cis–trans isomerization in the folding of the proline‐rich collagen triple helix. Biochemistry 2000 ; 39: 4299–4308, and references therein.
    • (2000) Biochemistry , vol.39 , pp. 4299-4308
    • Buevich, AV1    Dai, Q‐H2    Liu, X3    Brodsky, B4    Baum, J5
  • 33
    • 0032563109 scopus 로고    scopus 로고
    • X‐ray crystallographic determination of a collagen‐like peptide with the repeating sequence (Pro–Pro–Gly)
    • 33 Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM. X‐ray crystallographic determination of a collagen‐like peptide with the repeating sequence (Pro–Pro–Gly). JMol Biol 1998 ; 280: 623–638.
    • (1998) JMol Biol , vol.280 , pp. 623-638
    • Kramer, RZ1    Vitagliano, L2    Bella, J3    Berisio, R4    Mazzarella, L5    Brodsky, B6    Zagari, A7    Berman, HM8
  • 34
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple‐helical structure
    • 34 Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. Sequence dependent conformational variations of collagen triple‐helical structure. Nat Struct Biol 1999 ; 6: 454–457.
    • (1999) Nat Struct Biol , vol.6 , pp. 454-457
    • Kramer, RZ1    Bella, J2    Mayville, P3    Brodsky, B4    Berman, HM5
  • 35
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: implication for structural proteomics
    • 35 Linding R, Jensen LJ, Diella F, Bork P, Gibson TJ, Russell RB. Protein disorder prediction: implication for structural proteomics. Structure 2003 ; 11: 1453–1459.
    • (2003) Structure , vol.11 , pp. 1453-1459
    • Linding, R1    Jensen, LJ2    Diella, F3    Bork, P4    Gibson, TJ5    Russell, RB6
  • 36
    • 1642533607 scopus 로고    scopus 로고
    • The functional benefits of protein disorder
    • 36 Tompa P. The functional benefits of protein disorder. J Mol Struct (THEOCHEM) 2003 ; 666–667: 361–371, and references therein.
    • (2003) J Mol Struct (THEOCHEM) , vol.666–667 , pp. 361-371
    • Tompa, P1
  • 38
    • 0037066342 scopus 로고    scopus 로고
    • Peptide models XXXVIII. Proline conformers from X‐ray crystallographic database and from ab initio computations
    • 38 Hudáky I, Baldoni HA, Perczel A. Peptide models XXXVIII. Proline conformers from X‐ray crystallographic database and from ab initio computations. J Mol Struct (THEOCHEM) 2002 ; 582: 233–249.
    • (2002) J Mol Struct (THEOCHEM) , vol.582 , pp. 233-249
    • Hudáky, I1    Baldoni, HA2    Perczel, A3
  • 39
    • 0036462496 scopus 로고    scopus 로고
    • Quantum mechanical study of the conformational behavior of proline and 4R‐hydroxyproline dipeptide analogues in vacuum and in aqueous solution
    • 39 Benzi C, Improta R, Scalmani G, Barone V. Quantum mechanical study of the conformational behavior of proline and 4 R ‐hydroxyproline dipeptide analogues in vacuum and in aqueous solution. J Comput Chem 2002 ; 23: 341–350.
    • (2002) J Comput Chem , vol.23 , pp. 341-350
    • Benzi, C1    Improta, R2    Scalmani, G3    Barone, V4
  • 41
    • 84962446557 scopus 로고    scopus 로고
    • Determination of the potentials of mean force for rotation about CαCα virtual bonds in polypeptides from the ab initio energy surfaces of terminally blocked glycine, alanine, and proline
    • 41 Oldziej S, Kozlovska U, Liwo A, Scheraga HA. Determination of the potentials of mean force for rotation about C α C α virtual bonds in polypeptides from the ab initio energy surfaces of terminally blocked glycine, alanine, and proline. J Phys Chem 2003 ; 107: 8035–8046.
    • (2003) J Phys Chem , vol.107 , pp. 8035-8046
    • Oldziej, S1    Kozlovska, U2    Liwo, A3    Scheraga, HA4
  • 43
    • 0038292973 scopus 로고
    • Peptide Models. 1. Topology of selected peptide conformational potential‐energy surfaces (glycine and alanine derivatives)
    • 43 Perczel A, Ángyán JG, Kajtár M, Viviani W, Rivail J‐L, Marcoccia JF, Csizmadia IG. Peptide Models. 1. Topology of selected peptide conformational potential‐energy surfaces (glycine and alanine derivatives). J Am Chem Soc 1991 ; 113: 6256–6265.
    • (1991) J Am Chem Soc , vol.113 , pp. 6256-6265
    • Perczel, A1    Ángyán, JG2    Kajtár, M3    Viviani, W4    Rivail, J‐L5    Marcoccia, JF6    Csizmadia, IG7
  • 44
    • 0038506965 scopus 로고    scopus 로고
    • Ab initio analysis of the conformational changes of the prolylproline model peptide
    • 44 Hudáky I, Perczel A. Ab initio analysis of the conformational changes of the prolylproline model peptide. J Mol Struct (THEOCHEM) 2003 ; 630: 135–140.
    • (2003) J Mol Struct (THEOCHEM) , vol.630 , pp. 135-140
    • Hudáky, I1    Perczel, A2
  • 45
    • 0027080914 scopus 로고
    • Pyrrolidine ring puckering in cis and trans‐proline residues in proteins and polypeptides
    • 45 Milner‐White EJ, Bell LH, Maccallum PH. Pyrrolidine ring puckering in cis and trans‐proline residues in proteins and polypeptides. J Mol Biol 1992 ; 228: 725–734.
    • (1992) J Mol Biol , vol.228 , pp. 725-734
    • Milner‐White, EJ1    Bell, LH2    Maccallum, PH3
  • 47
    • 0025113022 scopus 로고
    • β‐Turns and their distortions: a proposed new nomenclature
    • 47 Wilmot CM, Thornton JM. β‐Turns and their distortions: a proposed new nomenclature. Protein Eng 1990 ; 3: 479–493.
    • (1990) Protein Eng , vol.3 , pp. 479-493
    • Wilmot, CM1    Thornton, JM2
  • 48
    • 0040154253 scopus 로고
    • Peptide models 6. New beta‐turn conformations from ab initio calculations confirmed by X‐ray data of proteins
    • 48 Perczel A, Mcallister MA, Csaszar P, Csizmadia IG. Peptide models 6. New beta‐turn conformations from ab initio calculations confirmed by X‐ray data of proteins. J Am Chem Soc 1993 ; 115: 4849–4858.
    • (1993) J Am Chem Soc , vol.115 , pp. 4849-4858
    • Perczel, A1    Mcallister, MA2    Csaszar, P3    Csizmadia, IG4
  • 49
    • 0000123690 scopus 로고
    • Peptide models 9. A complete conformational set of For–Ala–Ala–NH2 from ab inito computations
    • 49 Perczel A, McAlister MA, Császár P, Csizmadia IG. Peptide models 9. A complete conformational set of For–Ala–Ala–NH 2 from ab inito computations. Can J Chem 1994 ; 72: 2050–2070.
    • (1994) Can J Chem , vol.72 , pp. 2050-2070
    • Perczel, A1    McAlister, MA2    Császár, P3    Csizmadia, IG4
  • 51
    • 84986524957 scopus 로고
    • Convergence acceleration of iterative sequences—the case of SCF iteration
    • 51 Pulay P. Convergence acceleration of iterative sequences—the case of SCF iteration. Chem Phys Lett 1980 ; 73: 393–398.
    • (1980) Chem Phys Lett , vol.73 , pp. 393-398
    • Pulay, P1
  • 52
    • 44349162071 scopus 로고
    • Improved SCF convergence acceleration
    • 52 Pulay P. Improved SCF convergence acceleration. J Comput Chem 1982 ; 3: 556–560.
    • (1982) J Comput Chem , vol.3 , pp. 556-560
    • Pulay, P1
  • 53
    • 0002077637 scopus 로고
    • Geometry optimization by direct inversion in the iterative subspace
    • 53 Császár P, Pulay P. Geometry optimization by direct inversion in the iterative subspace. J Mol Struct (THEOCHEM) 1984 ; 114: 31–34.
    • (1984) J Mol Struct (THEOCHEM) , vol.114 , pp. 31-34
    • Császár, P1    Pulay, P2
  • 54
    • 0036144974 scopus 로고    scopus 로고
    • Methods for optimizing large molecules—Part III. An improved algorithm for geometry optimization using direct inversion in the iterative subspace (GDIIS)
    • 54 Farkas Ö, Schlegel B. Methods for optimizing large molecules—Part III. An improved algorithm for geometry optimization using direct inversion in the iterative subspace (GDIIS). Phys Chem Chem Phys Lett 2002 ; 4: 11–15.
    • (2002) Phys Chem Chem Phys Lett , vol.4 , pp. 11-15
    • Farkas, Ö1    Schlegel, B2
  • 55
    • 0001752768 scopus 로고    scopus 로고
    • The Cambridge Structural Database: a quarter of a million crystal structures and rising
    • 55 Allen FH. The Cambridge Structural Database: a quarter of a million crystal structures and rising. Acta Crystallogr B 2002 ; 58: 380–388.
    • (2002) Acta Crystallogr B , vol.58 , pp. 380-388
    • Allen, FH1
  • 56
    • 85120594095 scopus 로고    scopus 로고
    • 56 http://www.chem.qmw.ac.uk/iupac/misc/ppep1.html.
  • 57
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • 57 Hobohm U, Sander C. Enlarged representative set of protein structures. Protein Sci 1994 ; 3: 522–524.
    • (1994) Protein Sci , vol.3 , pp. 522-524
    • Hobohm, U1    Sander, C2
  • 58
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • 58 MacArthur MW, Thornton JM. Influence of proline residues on protein conformation. J Mol Biol 1991 ; 218: 397–412.
    • (1991) J Mol Biol , vol.218 , pp. 397-412
    • MacArthur, MW1    Thornton, JM2
  • 59
    • 24944454358 scopus 로고    scopus 로고
    • The Ramachandran plots of glycine and pre‐proline
    • 59 Ho BK, Brasseur R. The Ramachandran plots of glycine and pre‐proline. BMC Struct Biol 2005 ; 5: 14, and references therein.
    • (2005) BMC Struct Biol , vol.5 , pp. 14
    • Ho, BK1    Brasseur, R2
  • 60
    • 33644543406 scopus 로고    scopus 로고
    • Electronic control of amide cis–trans isomerism via aromatic‐prolyl interaction
    • 60 Thomas KM, Naduthambi D, Zondlo NJ. Electronic control of amide cis–trans isomerism via aromatic‐prolyl interaction. J Am Chem Soc 2006 ; 128: 2216–2217.
    • (2006) J Am Chem Soc , vol.128 , pp. 2216-2217
    • Thomas, KM1    Naduthambi, D2    Zondlo, NJ3
  • 61
    • 33645730970 scopus 로고    scopus 로고
    • Effects of i and i+3 residue identity on cis–trans isomerism of the aromatic i+1–prolyli+2 amide bond: implications for type VI β‐turn formation
    • 61 Meng HY, Thomas KM, Lee AE, Zondlo NJ. Effects of i and i +3 residue identity on cis–trans isomerism of the aromatic i +1–prolyl i +2 amide bond: implications for type VI β‐turn formation. Biopolymers 2006 ; 84: 192–204.
    • (2006) Biopolymers , vol.84 , pp. 192-204
    • Meng, HY1    Thomas, KM2    Lee, AE3    Zondlo, NJ4
  • 62
    • 4043082766 scopus 로고    scopus 로고
    • Solvation model induced structural changes in peptides. A quantum chemical study on Ramachandran surfaces and conformers of alanine diamide using the polarizable continuum model
    • 62 Hudáky I, Hudáky P, Perczel A. Solvation model induced structural changes in peptides. A quantum chemical study on Ramachandran surfaces and conformers of alanine diamide using the polarizable continuum model. J Comput Chem 2004 ; 25: 1522–1531.
    • (2004) J Comput Chem , vol.25 , pp. 1522-1531
    • Hudáky, I1    Hudáky, P2    Perczel, A3
  • 63
    • 1242290405 scopus 로고
    • Crystal structure of cyclo‐(Gly–L‐Pro–L‐Pro–Gly–L‐Pro–L‐Pro) trihydrate. Unusual conformational characteristics of a cyclic hexapeptide
    • 63 Czugler M, Sasvári K, Hollósi M. Crystal structure of cyclo‐(Gly–L ‐Pro–L ‐Pro–Gly–L ‐Pro–L ‐Pro) trihydrate. Unusual conformational characteristics of a cyclic hexapeptide. J Am Chem Soc 1982 ; 104: 4465–4469.
    • (1982) J Am Chem Soc , vol.104 , pp. 4465-4469
    • Czugler, M1    Sasvári, K2    Hollósi, M3
  • 64
    • 85120587899 scopus 로고
    • 64 Fuess H, Bats J.W. Am Cryst Assoc, Abstr Papers (Summer), 1983 ; 29.
    • (1983) , pp. 29
    • Fuess, H1    Bats, J.W2
  • 65
    • 24844463012 scopus 로고
    • Structure of cyclo(–L‐Pro–L‐Pro–Gly–L‐Pro–L‐Leu–Gly–) methanol molvate monohydrate, C25H38N6O6.CH3OH.H2O
    • 65 Nakashima T, Yamane T, Tanaka I, Ashida T. Structure of cyclo(–L ‐Pro–L ‐Pro–Gly–L ‐Pro–L ‐Leu–Gly–) methanol molvate monohydrate, C 25 H 38 N 6 O 6.CH 3 OH.H 2 O. Acta Crystallogr C 1984 ; 40: 171–174.
    • (1984) Acta Crystallogr C , vol.40 , pp. 171-174
    • Nakashima, T1    Yamane, T2    Tanaka, I3    Ashida, T4
  • 66
    • 0038650995 scopus 로고    scopus 로고
    • Relative stability of major types of beta‐turns as a function of amino acid composition: a study based on ab initio energetic and natural abundance data
    • 66 Perczel A, Jákli I, McAllister MA, Csizmadia I.G. Relative stability of major types of beta‐turns as a function of amino acid composition: a study based on ab initio energetic and natural abundance data. Chem‐Eur J 2003 ; 9: 2551–2566.
    • (2003) Chem‐Eur J , vol.9 , pp. 2551-2566
    • Perczel, A1    Jákli, I2    McAllister, MA3    Csizmadia, I.G4
  • 67
    • 0027474991 scopus 로고
    • Left‐handed polyproline II helices commonly occur in globular proteins
    • 67 Adzhubei AA, Sternberg MJE. Left‐handed polyproline II helices commonly occur in globular proteins. J Mol Biol 1993 ; 229: 472–493.
    • (1993) J Mol Biol , vol.229 , pp. 472-493
    • Adzhubei, AA1    Sternberg, MJE2
  • 68
    • 12944281484 scopus 로고    scopus 로고
    • On the stability of polyproline‐I and II structures of proline oligopeptides
    • 68 Kakinoki S, Hirano Y, Oka M. On the stability of polyproline‐I and II structures of proline oligopeptides. Polym Bull 2005 ; 53: 109–115.
    • (2005) Polym Bull , vol.53 , pp. 109-115
    • Kakinoki, S1    Hirano, Y2    Oka, M3
  • 69
    • 0035045552 scopus 로고    scopus 로고
    • Structural bases of collagen stabilization induced by proline hydroxilation
    • 69 Vitagliano L, Berisio R, Mazzarella L, Zagari A. Structural bases of collagen stabilization induced by proline hydroxilation. Biopolymers 2001 ; 58: 459–464.
    • (2001) Biopolymers , vol.58 , pp. 459-464
    • Vitagliano, L1    Berisio, R2    Mazzarella, L3    Zagari, A4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.