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Volumn 130, Issue 4-6, 2011, Pages 1095-1103

The close-packed triple helix as a possible new structural motif for collagen

Author keywords

Central channel; Close packed structure; Collagen motif; Ion channel; Strain twist coupling; Triple helix

Indexed keywords


EID: 80052865779     PISSN: 1432881X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00214-010-0761-3     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 0003716920 scopus 로고
    • Academic Press, Orlando. ISBN 0-12-146070-3
    • Burns G (1985) Solid State Physics, Academic Press, Orlando. ISBN 0-12-146070-3.
    • (1985) Solid State Physics
    • Burns, G.1
  • 4
    • 77949269041 scopus 로고    scopus 로고
    • The generic geometry of helices and their close-packed structures
    • Olsen K, Bohr J (2010) The generic geometry of helices and their close-packed structures. Theor Chem Acc 125: 207-215.
    • (2010) Theor Chem Acc , vol.125 , pp. 207-215
    • Olsen, K.1    Bohr, J.2
  • 6
    • 0033608997 scopus 로고    scopus 로고
    • Global curvature, thickness and the ideal shapes of knots
    • Gonzalez O, Maddocks JH (1999) Global curvature, thickness and the ideal shapes of knots. PNAS 96: 4769-4773.
    • (1999) Pnas , vol.96 , pp. 4769-4773
    • Gonzalez, O.1    Maddocks, J.H.2
  • 8
    • 0000523566 scopus 로고
    • Structure of collagen
    • Ramachandran GN, Kartha G (1954) Structure of collagen. Nature 174: 269-270.
    • (1954) Nature , vol.174 , pp. 269-270
    • Ramachandran, G.N.1    Kartha, G.2
  • 9
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandran GN, Kartha G (1955) Structure of collagen. Nature 176: 593-595.
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandran, G.N.1    Kartha, G.2
  • 10
    • 32844463093 scopus 로고
    • The structure of collagen
    • Rich A, Crick FHC (1955) The structure of collagen. Nature 176: 915-916.
    • (1955) Nature , vol.176 , pp. 915-916
    • Rich, A.1    Crick, F.H.C.2
  • 11
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich A, Crick FHC (1961) The molecular structure of collagen. J Mol Biol 3: 483-506.
    • (1961) J Mol Biol , vol.3 , pp. 483-506
    • Rich, A.1    Crick, F.H.C.2
  • 13
    • 81855175068 scopus 로고    scopus 로고
    • Collagen: Ramachandran triple helix revisited
    • In: Vijayan M, Yathindra N, Kolaskar AS (eds), University Press, Hyderabad, ISBN 81 7371 254 9
    • Sasisekharan V, Yathindra N (1999) Collagen: Ramachandran triple helix revisited. In: Vijayan M, Yathindra N, Kolaskar AS (eds) Perspectives in structural biology, University Press, Hyderabad, pp 155-168, ISBN 81 7371 254 9.
    • (1999) Perspectives in structural biology , pp. 155-168
    • Sasisekharan, V.1    Yathindra, N.2
  • 14
    • 34548489679 scopus 로고    scopus 로고
    • The variability in type I collagen helical pitch is reflected in the D periodic fibrillar structure
    • Cameron GJ, Cairns DE, Wess TJ (2007) The variability in type I collagen helical pitch is reflected in the D periodic fibrillar structure. J Mol Biol 372: 1097-1107.
    • (2007) J Mol Biol , vol.372 , pp. 1097-1107
    • Cameron, G.J.1    Cairns, D.E.2    Wess, T.J.3
  • 15
    • 33745181159 scopus 로고    scopus 로고
    • Microfibrillar structure of type 1 collagen in situ
    • Orgel JRO, Irving TC, Miller A, Wess TJ (2006) Microfibrillar structure of type 1 collagen in situ. PNAS 103: 9001-9005.
    • (2006) Pnas , vol.103 , pp. 9001-9005
    • Orgel, J.R.O.1    Irving, T.C.2    Miller, A.3    Wess, T.J.4
  • 17
    • 67649500001 scopus 로고    scopus 로고
    • Molecular dynamics investigations on the effect of D amino acids substitution in a triple-helix structure and the stability of collagen
    • Punitha V, Raman SS, Parthasarathi R, Subramanian V, Rao JR, Nair BU, Ramasami T (2009) Molecular dynamics investigations on the effect of D amino acids substitution in a triple-helix structure and the stability of collagen. J Phys Chem B 113: 8983-8992.
    • (2009) J Phys Chem B , vol.113 , pp. 8983-8992
    • Punitha, V.1    Raman, S.S.2    Parthasarathi, R.3    Subramanian, V.4    Rao, J.R.5    Nair, B.U.6    Ramasami, T.7
  • 20
    • 33747610222 scopus 로고    scopus 로고
    • Nature designs tough collagen: explaining the nanostructure of collagen fibrils
    • Buehler MJ (2006) Nature designs tough collagen: explaining the nanostructure of collagen fibrils. PNAS USA 103: 12285-12290.
    • (2006) PNAS USA , vol.103 , pp. 12285-12290
    • Buehler, M.J.1
  • 23
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella J, Eaton M, Brodsky B, Berman HM (1994) Crystal and molecular structure of a collagen-like peptide at 1. 9 Å resolution. Science 266: 75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 24
    • 0031657823 scopus 로고    scopus 로고
    • Supercoiled protein motifs: the collagen triple-helix and the α-helical coiled coil
    • Beck K, Brodsky B (1998) Supercoiled protein motifs: the collagen triple-helix and the α-helical coiled coil. J Struct Biol 122: 17-29.
    • (1998) J Struct Biol , vol.122 , pp. 17-29
    • Beck, K.1    Brodsky, B.2
  • 25
    • 0033077144 scopus 로고    scopus 로고
    • 7/2-Helical model for collagen-evidence from model peptides
    • Okuyama K, Nagarajan V, Kamitori S (1999) 7/2-Helical model for collagen-evidence from model peptides. Proc Indian Acad Sci 111: 19-34.
    • (1999) Proc Indian Acad Sci , vol.111 , pp. 19-34
    • Okuyama, K.1    Nagarajan, V.2    Kamitori, S.3
  • 27
    • 9144246166 scopus 로고    scopus 로고
    • Crystal structures of collagen model peptides with Pro-Hyp-Gly repetition sequences at 1.26 Å resolution: implications for proline ring puckering
    • Okuyama K, Hongo C, Fukushima R, Wu G, Narita H, Noguchi K, Tanaka Y, Nishino N (2004) Crystal structures of collagen model peptides with Pro-Hyp-Gly repetition sequences at 1. 26 Å resolution: implications for proline ring puckering. Biopolymers 76: 367-377.
    • (2004) Biopolymers , vol.76 , pp. 367-377
    • Okuyama, K.1    Hongo, C.2    Fukushima, R.3    Wu, G.4    Narita, H.5    Noguchi, K.6    Tanaka, Y.7    Nishino, N.8
  • 28
  • 30
    • 0035318052 scopus 로고    scopus 로고
    • Helical close packings of ideal ropes
    • Przybył S, Pierański P (2001) Helical close packings of ideal ropes. Eur Phys J E 4: 445-449.
    • (2001) Eur Phys J E , vol.4 , pp. 445-449
    • Przybył, S.1    Pierański, P.2
  • 31
    • 0345358678 scopus 로고    scopus 로고
    • Geometry and mechanics of uniform n-plies: from engineering ropes to biological filaments
    • Neukirch S, van der Heijden GHM (2002) Geometry and mechanics of uniform n-plies: from engineering ropes to biological filaments. J Elast 69: 41-72.
    • (2002) J Elast , vol.69 , pp. 41-72
    • Neukirch, S.1    van der Heijden, G.H.M.2
  • 32
    • 81855161913 scopus 로고
    • The tubular structure of collagen fibril
    • Haisa M (1962) The tubular structure of collagen fibril. Bull Chem Soc Jpn 35: 769-774.
    • (1962) Bull Chem Soc Jpn , vol.35 , pp. 769-774
    • Haisa, M.1
  • 33
    • 56349098272 scopus 로고    scopus 로고
    • Revisiting the molecular structure of collagen
    • Okuyama K (2008) Revisiting the molecular structure of collagen. Connect Tissue Res 49: 299-310.
    • (2008) Connect Tissue Res , vol.49 , pp. 299-310
    • Okuyama, K.1
  • 35
    • 33645983486 scopus 로고    scopus 로고
    • Biomineralization and evolutionary history
    • Knoll AH (2003) Biomineralization and evolutionary history. Rev Mineral Geochem 54: 329-356.
    • (2003) Rev Mineral Geochem , vol.54 , pp. 329-356
    • Knoll, A.H.1
  • 36
    • 0001158810 scopus 로고
    • Nuclear magnetic resonance study of collagen hydration
    • Berendsen HJC (1962) Nuclear magnetic resonance study of collagen hydration. J Chem Phys 36: 3297-3305.
    • (1962) J Chem Phys , vol.36 , pp. 3297-3305
    • Berendsen, H.J.C.1
  • 37
    • 33846804509 scopus 로고    scopus 로고
    • Collagen structure: The molecular source of the tendon magic angle effect
    • Fullerton GD, Rahal A (2007) Collagen structure: the molecular source of the tendon magic angle effect. J Magn Reson Imag 25: 345-361.
    • (2007) J Magn Resonan Imag , vol.25 , pp. 345-361
    • Fullerton, G.D.1    Rahal, A.2
  • 39
    • 84981666520 scopus 로고
    • Hydration structure of fibrous macromolecules
    • Berendsen HJC, Migchelsen C (1965) Hydration structure of fibrous macromolecules. Annals of the New York Academy of Sciences 125: 365-379.
    • (1965) Ann NY Acad Sci , vol.125 , pp. 365-379
    • Berendsen, H.J.C.1    Migchelsen, C.2
  • 40
    • 0035478472 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics
    • Wallace BA, Janes RW (2001) Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics. Curr Opin Chem Biol 5: 567-571.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 567-571
    • Wallace, B.A.1    Janes, R.W.2
  • 41
    • 0001104239 scopus 로고    scopus 로고
    • Circular dichroism of collagen and related polypeptides
    • In: Fasman GD (eds), Plenum Press, New York, ISBN 0-306-45142-5
    • Bhatnagar RS, Gough CA (1996) Circular dichroism of collagen and related polypeptides. In: Fasman GD (eds), Circular dichroism and the conformational analysis of biomolecules, Plenum Press, New York, pp 184-199, ISBN 0-306-45142-5.
    • (1996) Circular dichroism and the conformational analysis of biomolecules , pp. 184-199
    • Bhatnagar, R.S.1    Gough, C.A.2
  • 42
    • 33644756932 scopus 로고    scopus 로고
    • Theoretical UV circular dichroism of Clyclo(L-Proline-L-Proline)
    • Carlson KL, Lowe SL, Hoffmann MR, Thomasson KA (2006) Theoretical UV circular dichroism of Clyclo(L-Proline-L-Proline). J Phys Chem A 110: 1925-1933.
    • (2006) J Phys Chem A , vol.110 , pp. 1925-1933
    • Carlson, K.L.1    Lowe, S.L.2    Hoffmann, M.R.3    Thomasson, K.A.4
  • 43
    • 0035068434 scopus 로고    scopus 로고
    • Collagens and collagen-related diseases
    • Myllyharju J, Kivirikko KI (2001) Collagens and collagen-related diseases. Ann Med 33: 7-21.
    • (2001) Ann Med , vol.33 , pp. 7-21
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 44
    • 0001406145 scopus 로고
    • On the piezoelectric effect of bone
    • Fukada E, Yasuda I (1957) On the piezoelectric effect of bone. J Phys Soc Jpn 12: 1158-1162.
    • (1957) J Phys Soc Jpn , vol.12 , pp. 1158-1162
    • Fukada, E.1    Yasuda, I.2
  • 45
    • 77952489828 scopus 로고
    • Piezoelectricity in helical polymer chains
    • Kasai K (1969) Piezoelectricity in helical polymer chains. J Phys Soc Jpn 27: 1268-1274.
    • (1969) J Phys Soc Jpn , vol.27 , pp. 1268-1274
    • Kasai, K.1
  • 46
    • 34648846548 scopus 로고    scopus 로고
    • Estimation of helical angles of myosin and collagen by second harmonic generation imaging microscopy
    • Tiaho F, Recher G, Rouède D (2007) Estimation of helical angles of myosin and collagen by second harmonic generation imaging microscopy. Optics Express 15: 12286-12295.
    • (2007) Optics Express , vol.15 , pp. 12286-12295
    • Tiaho, F.1    Recher, G.2    Rouède, D.3
  • 47
    • 37549015952 scopus 로고    scopus 로고
    • Role of hydration in determining the structure and vibrational spectra of L-alanine and N-acetyl L-alanine N'-methylamide in aqueous solution: a combined theoretical and experimental approach
    • Jalkanen KJ, Degtyarenko IM, Nieminen RM, Cao X, Nafie LA, Zhu F, Barron LD (2008) Role of hydration in determining the structure and vibrational spectra of L-alanine and N-acetyl L-alanine N'-methylamide in aqueous solution: a combined theoretical and experimental approach. Theor Chem Acc 119: 191-210.
    • (2008) Theor Chem Acc , vol.119 , pp. 191-210
    • Jalkanen, K.J.1    Degtyarenko, I.M.2    Nieminen, R.M.3    Cao, X.4    Nafie, L.A.5    Zhu, F.6    Barron, L.D.7


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