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Volumn 18, Issue 6, 2009, Pages 1321-1325

On the occurrence of linear groups in proteins

Author keywords

helix; sheet; Left handed helix; Linear group; Polyproline; Protein standard conformation; Ramachandran plot; Secondary structure

Indexed keywords

POLYPEPTIDE; PROLINE;

EID: 66349129121     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.133     Document Type: Short Survey
Times cited : (36)

References (34)
  • 1
    • 0006482126 scopus 로고
    • Interatomic distances and bond angles in the polypeptide chain of proteins
    • Corey R, Donohue J (1950) Interatomic distances and bond angles in the polypeptide chain of proteins. Proc Natl Acad Sci USA 72:2899-2900.
    • (1950) Proc Natl Acad Sci USA , vol.72 , pp. 2899-2900
    • Corey, R.1    Donohue, J.2
  • 2
    • 76549252207 scopus 로고
    • The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling L, Corey RB, Branson HR (1951) The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci USA 37:205-211.
    • (1951) Proc Natl Acad Sci USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 3
    • 76549238253 scopus 로고
    • The pleated sheet, a new layer configuration of polypeptide chains
    • Pauling L, Corey RB (1951) The pleated sheet, a new layer configuration of polypeptide chains. Proc Natl Acad Sci USA 37:251-256.
    • (1951) Proc Natl Acad Sci USA , vol.37 , pp. 251-256
    • Pauling, L.1    Corey, R.B.2
  • 4
    • 0001142723 scopus 로고
    • The pi-helix - A hydrogen bonded configuration of the polypeptide chain
    • Low B, Baybutt R (1952) The pi-helix - a hydrogen bonded configuration of the polypeptide chain. J Am Chem Soc 74:5806-5807.
    • (1952) J Am Chem Soc , vol.74 , pp. 5806-5807
    • Low, B.1    Baybutt, R.2
  • 5
    • 0000556407 scopus 로고
    • Hydrogen bonded helical configurations of the polypeptide chain
    • Donohue J (1953) Hydrogen bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci USA 39:470-478.
    • (1953) Proc Natl Acad Sci USA , vol.39 , pp. 470-478
    • Donohue, J.1
  • 6
    • 0014416148 scopus 로고
    • The structure of poly-L-proline II
    • Arnott S, Dover SD (1968) The structure of poly-L-proline II. Acta Crystallogr B 24:599-601.
    • (1968) Acta Crystallogr B , vol.24 , pp. 599-601
    • Arnott, S.1    Dover, S.D.2
  • 7
    • 0001567029 scopus 로고
    • Structure of poly-L-proline II
    • Sasisekharan V (1959) Structure of poly-L-proline II. Acta Crystallogr 12:897-903.
    • (1959) Acta Crystallogr , vol.12 , pp. 897-903
    • Sasisekharan, V.1
  • 9
    • 0014842661 scopus 로고
    • IUPAC-IUB Commission on biochemical nomenclature. Abbreviations and symbols for the description of the conformation of polypeptide chains
    • IUPAC
    • IUPAC (1970) IUPAC-IUB Commission on biochemical nomenclature. Abbreviations and symbols for the description of the conformation of polypeptide chains. Biochemistry 9:3471-3479.
    • (1970) Biochemistry , vol.9 , pp. 3471-3479
  • 16
    • 50449111518 scopus 로고    scopus 로고
    • The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins
    • Beck DA, Alonso DO, Inoyama D, Daggett V (2008) The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins. Proc Natl Acad Sci USA 105:12259-12264.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12259-12264
    • Beck, D.A.1    Alonso, D.O.2    Inoyama, D.3    Daggett, V.4
  • 17
    • 46449114017 scopus 로고    scopus 로고
    • Structures, basins, and energies: A deconstruction of the protein coil library
    • Perskie LL, Street TO, Rose GD (2008) Structures, basins, and energies: A deconstruction of the protein coil library. Protein Sci 17:1151-1161.
    • (2008) Protein Sci , vol.17 , pp. 1151-1161
    • Perskie, L.L.1    Street, T.O.2    Rose, G.D.3
  • 18
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U, Sander C (1994) Enlarged representative set of protein structures. Protein Sci 3:522-524. (Pubitemid 24103723)
    • (1994) Protein Science , vol.3 , Issue.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 19
    • 13444254300 scopus 로고    scopus 로고
    • PDBsum more: New summaries and analyses of the known 3D structures of proteins and nucleic acids
    • DOI 10.1093/nar/gki001
    • Laskowski RA, Chistyakov VV, Thornton JM (2005) PDBsum more: new summaries and analyses of the known 3D structures of proteins and nucleic acids. Nucleic Acids Res 33:D266-D268. (Pubitemid 40207875)
    • (2005) Nucleic Acids Research , vol.33 , Issue.DATABASE ISS
    • Laskowski, R.A.1    Chistyakov, V.V.2    Thornton, J.M.3
  • 20
    • 0030010605 scopus 로고    scopus 로고
    • Experimentally observed conformation-dependent geometry and hidden strain in proteins
    • Karplus PA (1996) Experimentally observed conformation-dependent geometry and hidden strain in proteins. Protein Sci 5:1406-1420. (Pubitemid 26239448)
    • (1996) Protein Science , vol.5 , Issue.7 , pp. 1406-1420
    • Karplus, P.A.1
  • 21
    • 0030589514 scopus 로고    scopus 로고
    • Phi/Psi-chology: Ramachandran revisited
    • Kleywegt GJ, Jones TA (1996) Phi/psi-chology: Ramachandran revisited. Structure 4:1395-1400. (Pubitemid 27050273)
    • (1996) Structure , vol.4 , Issue.12 , pp. 1395-1400
    • Kleywegt, G.J.1    Jones, T.A.2
  • 23
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 24
    • 0014347799 scopus 로고
    • Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
    • Venkatachalam CM (1968) Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biopolymers 6:1425-1436.
    • (1968) Biopolymers , vol.6 , pp. 1425-1436
    • Venkatachalam, C.M.1
  • 25
    • 34547559253 scopus 로고    scopus 로고
    • Physical-chemical determinants of turn conformations in globular proteins
    • DOI 10.1110/ps.072898507
    • Street TO, Fitzkee NC, Perskie LL, Rose GD (2007) Physical-chemical determinants of turn conformations in globular proteins. Protein Sci 16:1720-1727. (Pubitemid 47195698)
    • (2007) Protein Science , vol.16 , Issue.8 , pp. 1720-1727
    • Street, T.O.1    Fitzkee, N.C.2    Perskie, L.L.3    Rose, G.D.4
  • 26
    • 0017615801 scopus 로고
    • Logical analysis of the mechanism of protein folding. IV. Super secondary structures
    • DOI 10.1016/S0022-2836(77)80032-6
    • Nagano K (1977) Logical analysis of the mechanism of protein folding. IV. Super-secondary structures. J Mol Biol 109:235-250. (Pubitemid 8027702)
    • (1977) Journal of Molecular Biology , vol.109 , Issue.2 , pp. 235-250
    • Nagano, K.1
  • 27
    • 0033978466 scopus 로고    scopus 로고
    • The pi-helix translates structure into function
    • Weaver TM (2000) The pi-helix translates structure into function. Protein Sci 9:201-206.
    • (2000) Protein Sci , vol.9 , pp. 201-206
    • Weaver, T.M.1
  • 28
    • 0036276409 scopus 로고    scopus 로고
    • Occurrence, conformational features and amino acid propensities for the pihelix
    • Fodje MN, Al-Karadaghi S (2002) Occurrence, conformational features and amino acid propensities for the pihelix. Protein Eng 15:353-358. (Pubitemid 34601726)
    • (2002) Protein Engineering , vol.15 , Issue.5 , pp. 353-358
    • Fodje, M.N.1    Al-Karadaghi, S.2
  • 29
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS (1981) The anatomy and taxonomy of protein structure. Adv Protein Chem 34:167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 30
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • DOI 10.1006/jmbi.1993.1047
    • Adzhubei AA, Sternberg MJ (1993) Left-handed polyproline II helices commonly occur in globular proteins. J Mol Biol 229:472-493. (Pubitemid 23080393)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.2 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 31
    • 0032980562 scopus 로고    scopus 로고
    • A survey of left-handed polyproline II helices
    • Stapley BJ, Creamer TP (1999) A survey of left-handed polyproline II helices. Protein Sci 8:587-595. (Pubitemid 29117973)
    • (1999) Protein Science , vol.8 , Issue.3 , pp. 587-595
    • Stapley, B.J.1    Creamer, T.P.2
  • 32
    • 0036400325 scopus 로고    scopus 로고
    • Is polyproline II a major backbone conformation in unfolded proteins?
    • Shi Z, Woody RW, Kallenbach NR (2002) Is polyproline II a major backbone conformation in unfolded proteins? Adv Protein Chem 62:163-240.
    • (2002) Adv Protein Chem , vol.62 , pp. 163-240
    • Shi, Z.1    Woody, R.W.2    Kallenbach, N.R.3
  • 33
    • 0036402323 scopus 로고    scopus 로고
    • Determinants of the polyproline II helix from modeling studies
    • DOI 10.1016/S0065-3233(02)62010-8
    • Creamer TP, Campbell MN (2002) Determinants of the polyproline II helix from modeling studies. Adv Protein Chem 62:263-282. (Pubitemid 35204873)
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 263-282
    • Creamer, T.P.1    Campbell, M.N.2
  • 34
    • 17644422781 scopus 로고    scopus 로고
    • Urea promotes polyproline II helix formation: Implications for protein denatured states
    • DOI 10.1021/bi050124u
    • Whittington SJ, Chellgren BW, Hermann VM, Creamer TP (2005) Urea promotes polyproline II helix formation: implications for protein denatured states. Biochemistry 44:6269-6275. (Pubitemid 40570720)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6269-6275
    • Whittington, S.J.1    Chellgren, B.W.2    Hermann, V.M.3    Creamer, T.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.