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Volumn 61, Issue 4, 2005, Pages 763-768

A tetrapeptide-based method for polyproline II-type secondary structure prediction

Author keywords

Polyproline II type structure; Prediction; Secondary structure; Tetrapeptides

Indexed keywords

GLOBULAR PROTEIN; OLIGOPEPTIDE; PROLINE DERIVATIVE; TETRAPEPTIDE;

EID: 28644436096     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20670     Document Type: Article
Times cited : (12)

References (22)
  • 1
    • 0034636977 scopus 로고    scopus 로고
    • Is polyproline II helix the killer conformation?: A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme
    • Blanch EW, Morozova-Roche LA, Cochran DAE, Doig AJ, Hecht L, Barron LD. Is polyproline II helix the killer conformation?: a Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme. J Mol Biol 2000;301:553-563.
    • (2000) J Mol Biol , vol.301 , pp. 553-563
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Cochran, D.A.E.3    Doig, A.J.4    Hecht, L.5    Barron, L.D.6
  • 3
    • 0035400145 scopus 로고    scopus 로고
    • A retro-inverso peptide mimic of CD28 encompassing the MYPPPY motif adopts a polyproline type II helix and inhibits encephalitogenic T cells in vitro
    • Srinivasan M, Wardrop RM, Gienapp IE, Stuckman SS, Whitaacre CC, Kaumaya PT. A retro-inverso peptide mimic of CD28 encompassing the MYPPPY motif adopts a polyproline type II helix and inhibits encephalitogenic T cells in vitro. J Immunol 2000;167:578-585.
    • (2000) J Immunol , vol.167 , pp. 578-585
    • Srinivasan, M.1    Wardrop, R.M.2    Gienapp, I.E.3    Stuckman, S.S.4    Whitaacre, C.C.5    Kaumaya, P.T.6
  • 4
    • 0029058133 scopus 로고
    • The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides
    • Siligardi G, Drake AF. The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides. Biopolymers 1995;37:281-292.
    • (1995) Biopolymers , vol.37 , pp. 281-292
    • Siligardi, G.1    Drake, A.F.2
  • 5
    • 0035814919 scopus 로고    scopus 로고
    • Glycosylated polyproline II rods with kinks as a structural motif in plant hydroxyproline-rich glycoproteins
    • Ferris PJ, Woessner JP, Waffenschmidt S, Kilz S, Drees J, Goodenough UW. Glycosylated polyproline II rods with kinks as a structural motif in plant hydroxyproline-rich glycoproteins. Biochemistry 2001;40:2978-2987.
    • (2001) Biochemistry , vol.40 , pp. 2978-2987
    • Ferris, P.J.1    Woessner, J.P.2    Waffenschmidt, S.3    Kilz, S.4    Drees, J.5    Goodenough, U.W.6
  • 6
    • 0029910536 scopus 로고    scopus 로고
    • Can a polyproline II helical motif be used in the context of sequence-selective major groove recognition of B-DNA?: A molecular modelling investigation
    • Gresh, N. Can a polyproline II helical motif be used in the context of sequence-selective major groove recognition of B-DNA?: a molecular modelling investigation. J Biomol Struct Dyn 1996;14:255-273
    • (1996) J Biomol Struct Dyn , vol.14 , pp. 255-273
    • Gresh, N.1
  • 7
    • 0032704889 scopus 로고    scopus 로고
    • Conformational studies of the C-terminal domain of bacteriophage Pf1 gene 5 protein
    • Fox, D.G., Cary, P.D., Kneale, G.G. Conformational studies of the C-terminal domain of bacteriophage Pf1 gene 5 protein. Biochim Biophys Acta 1999;1435:138-146.
    • (1999) Biochim Biophys Acta , vol.1435 , pp. 138-146
    • Fox, D.G.1    Cary, P.D.2    Kneale, G.G.3
  • 8
    • 0034753803 scopus 로고    scopus 로고
    • A novel, specific interaction involving the Csk SH3 domain and its natural ligand
    • Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D. A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Nat Struct Biol 2001;8:998-1004.
    • (2001) Nat Struct Biol , vol.8 , pp. 998-1004
    • Ghose, R.1    Shekhtman, A.2    Goger, M.J.3    Ji, H.4    Cowburn, D.5
  • 10
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei AA, Sternberg MJ. 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, A.A.1    Sternberg, M.J.2
  • 11
    • 0028577684 scopus 로고
    • Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building
    • Adzhubei AA, Sternberg MJ. Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building. Protein Sci 1994;3:2395-2410.
    • (1994) Protein Sci , vol.3 , pp. 2395-2410
    • Adzhubei, A.A.1    Sternberg, M.J.2
  • 12
    • 0034870317 scopus 로고    scopus 로고
    • On preprocessing of protein sequences for neural network prediction of polyproline II secondary structures
    • Siermala M, Juhola M, Vihinen M. On preprocessing of protein sequences for neural network prediction of polyproline II secondary structures. Comput Biol Med 2001;31:385-398.
    • (2001) Comput Biol Med , vol.31 , pp. 385-398
    • Siermala, M.1    Juhola, M.2    Vihinen, M.3
  • 13
    • 0027932724 scopus 로고
    • Poly(pro)II helices in globular proteins: Identification and circular dichroic analysis
    • Sreerama N, Woody RW. Poly(pro)II helices in globular proteins: identification and circular dichroic analysis. Biochemistry 1994;33:10022-10025.
    • (1994) Biochemistry , vol.33 , pp. 10022-10025
    • Sreerama, N.1    Woody, R.W.2
  • 14
    • 0032980562 scopus 로고    scopus 로고
    • A survey of left-handed polyproline II helices
    • Stapley BJ, Creamer TP. A survey of left-handed polyproline II helices. Protein Sci 1999;8:587-595.
    • (1999) Protein Sci , vol.8 , pp. 587-595
    • Stapley, B.J.1    Creamer, T.P.2
  • 15
    • 0016262418 scopus 로고
    • Further comparison of predicted and experimentally determined structure of adenilate kinase
    • Kabat EA, Wu TT. Further comparison of predicted and experimentally determined structure of adenilate kinase. Proc Natl Acad Sci USA 1974;71:4217-4220.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4217-4220
    • Kabat, E.A.1    Wu, T.T.2
  • 16
    • 0037312528 scopus 로고    scopus 로고
    • A pentapeptide-based method for protein secondary structure prediction
    • Figureau A, Soto MA, Toha J. A pentapeptide-based method for protein secondary structure prediction. Protein Eng 2003;16:103-107.
    • (2003) Protein Eng , vol.16 , pp. 103-107
    • Figureau, A.1    Soto, M.A.2    Toha, J.3
  • 18
    • 0033562619 scopus 로고    scopus 로고
    • Assigning secondary structure from protein coordinate data
    • King SM, Johnson WC. Assigning secondary structure from protein coordinate data. Proteins 1999;35:313-320.
    • (1999) Proteins , vol.35 , pp. 313-320
    • King, S.M.1    Johnson, W.C.2
  • 19
    • 0032905858 scopus 로고    scopus 로고
    • A brighter future for protein structure prediction
    • Koehl P, Levitt M. A brighter future for protein structure prediction. Nat Struct Biol 1999;6:108-111.
    • (1999) Nat Struct Biol , vol.6 , pp. 108-111
    • Koehl, P.1    Levitt, M.2
  • 20
    • 0034153589 scopus 로고    scopus 로고
    • How do point amino acid substitution affect the protein structure?
    • Ramensky VE, Vlasov PK, Sunyaev SR, Tumanyan VG. How do point amino acid substitution affect the protein structure? Biophysics 2000;45:215-222.
    • (2000) Biophysics , vol.45 , pp. 215-222
    • Ramensky, V.E.1    Vlasov, P.K.2    Sunyaev, S.R.3    Tumanyan, V.G.4
  • 21
    • 0032519692 scopus 로고    scopus 로고
    • Structural diversity of sequentially identical subsequences of proteins: Identical octapeptides can have different conformations
    • Sudarsanam S. Structural diversity of sequentially identical subsequences of proteins: identical octapeptides can have different conformations. Proteins 1998;30:228-231.
    • (1998) Proteins , vol.30 , pp. 228-231
    • Sudarsanam, S.1
  • 22
    • 0030808140 scopus 로고    scopus 로고
    • Classification and prediction of beta-turn types
    • Chou KC, Blinn RB. Classification and prediction of beta-turn types. J Prot Chem 1997;16:575-595.
    • (1997) J Prot Chem , vol.16 , pp. 575-595
    • Chou, K.C.1    Blinn, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.