메뉴 건너뛰기




Volumn 72, Issue 4, 2008, Pages 1320-1332

Region-specific role of water in collagen unwinding and assembly

Author keywords

Collagen cleavage; Collagenase; Hydration shell; Imino poor region; Labile domain; Microunfolding; Protein folding; Water bridge

Indexed keywords

COLLAGEN; COLLAGEN TYPE 3; COLLAGENASE; HYDROXYPROLINE; IMINO ACID; PROLINE DERIVATIVE; WATER;

EID: 51349144005     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22026     Document Type: Article
Times cited : (55)

References (55)
  • 2
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich A, Crick FHC. The molecular structure of collagen. J Mol Biol 1961;3:483-506.
    • (1961) J Mol Biol , vol.3 , pp. 483-506
    • Rich, A.1    Crick, F.H.C.2
  • 3
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • 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, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 4
    • 0015862613 scopus 로고
    • Hydroxyproline content determines the denaturation temperature of chick tendon collagen
    • Rosenbloom J, Harsch M, Jimenez S. Hydroxyproline content determines the denaturation temperature of chick tendon collagen. Arch Biochem Biophys 1973;158:478-484.
    • (1973) Arch Biochem Biophys , vol.158 , pp. 478-484
    • Rosenbloom, J.1    Harsch, M.2    Jimenez, S.3
  • 5
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen, evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • Berg RA, Prockop DJ. The thermal transition of a non-hydroxylated form of collagen, evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem Biophys Res Commun 1973;52:115-120.
    • (1973) Biochem Biophys Res Commun , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 6
    • 0015852842 scopus 로고
    • A hypothesis on the role of hydroxyproline in stabilizing collagen structure
    • Ramachandran GN, Bansal M, Bhatnagar RS. A hypothesis on the role of hydroxyproline in stabilizing collagen structure. Biochim Biophys Acta 1973;322:166-171.
    • (1973) Biochim Biophys Acta , vol.322 , pp. 166-171
    • Ramachandran, G.N.1    Bansal, M.2    Bhatnagar, R.S.3
  • 7
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella J, Brodsky B, Berman HM. Hydration structure of a collagen peptide. Structure 1995;3:893-906.
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 11
    • 0038369862 scopus 로고    scopus 로고
    • Asymmetry in the triple helix of collagen-like heterotrimers confirms that external bonds stabilize collagen structure
    • Slatter DA, Miles CA, Bailey AJ. Asymmetry in the triple helix of collagen-like heterotrimers confirms that external bonds stabilize collagen structure. J Mol Biol 2003;329:175-183.
    • (2003) J Mol Biol , vol.329 , pp. 175-183
    • Slatter, D.A.1    Miles, C.A.2    Bailey, A.J.3
  • 12
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: A context for hostguest triple-helical peptides
    • Ramshaw JA, Shah NK, Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for hostguest triple-helical peptides. J Struct Biol 1998;122:86-91.
    • (1998) J Struct Biol , vol.122 , pp. 86-91
    • Ramshaw, J.A.1    Shah, N.K.2    Brodsky, B.3
  • 13
    • 0034279084 scopus 로고    scopus 로고
    • The effects of alcoholic compounds on the stability of type I collagen studied by differential scanning calorimetry
    • Fukuda K, Nezu T, Terada Y. The effects of alcoholic compounds on the stability of type I collagen studied by differential scanning calorimetry. Dent Mater J 2000;19:221-228.
    • (2000) Dent Mater J , vol.19 , pp. 221-228
    • Fukuda, K.1    Nezu, T.2    Terada, Y.3
  • 14
    • 0034283338 scopus 로고    scopus 로고
    • Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair
    • Kramer RZ, Venugopal MG, Bella J, Mayville P, Brodsky B, Berman HM. Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair. J Mol Biol 2000;301:1191-1205.
    • (2000) J Mol Biol , vol.301 , pp. 1191-1205
    • Kramer, R.Z.1    Venugopal, M.G.2    Bella, J.3    Mayville, P.4    Brodsky, B.5    Berman, H.M.6
  • 15
    • 0035800664 scopus 로고    scopus 로고
    • The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence
    • Kramer RZ, Bella J, Brodsky B, Berman HM. The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J Mol Biol 2001;311:131-147.
    • (2001) J Mol Biol , vol.311 , pp. 131-147
    • Kramer, R.Z.1    Bella, J.2    Brodsky, B.3    Berman, H.M.4
  • 16
    • 0035219275 scopus 로고    scopus 로고
    • Thermally labile domains in the collagen molecule
    • Miles CA, Bailey AJ. Thermally labile domains in the collagen molecule. Micron 2001;32:325-332.
    • (2001) Micron , vol.32 , pp. 325-332
    • Miles, C.A.1    Bailey, A.J.2
  • 17
    • 34548695226 scopus 로고    scopus 로고
    • Spontaneous unwinding of a labile domain in a collagen triple helix
    • Ravikumar KM, Humphery JD, Hwang W. Spontaneous unwinding of a labile domain in a collagen triple helix. J Mech Matl Struct 2007;2:999.
    • (2007) J Mech Matl Struct , vol.2 , pp. 999
    • Ravikumar, K.M.1    Humphery, J.D.2    Hwang, W.3
  • 19
    • 0026333465 scopus 로고
    • A model for interstitial collagen catabolism by mammalian collagenases
    • Fields GB. A model for interstitial collagen catabolism by mammalian collagenases. J Theor Biol 1991;153:585-602.
    • (1991) J Theor Biol , vol.153 , pp. 585-602
    • Fields, G.B.1
  • 21
    • 33746239552 scopus 로고    scopus 로고
    • Molecular dynamics study of onset of water gelation around the collagen triple helix
    • Handgraaf JW, Zerbetto F. Molecular dynamics study of onset of water gelation around the collagen triple helix. Proteins 2006;64:711-718.
    • (2006) Proteins , vol.64 , pp. 711-718
    • Handgraaf, J.W.1    Zerbetto, F.2
  • 22
    • 33646204790 scopus 로고    scopus 로고
    • Triple helical structure and stabilization of collagen-like molecules with 4(R)-hydroxyproline in the Xaa position
    • Radmer RJ, Klein TE. Triple helical structure and stabilization of collagen-like molecules with 4(R)-hydroxyproline in the Xaa position. Biophys J 2006;90:578-588.
    • (2006) Biophys J , vol.90 , pp. 578-588
    • Radmer, R.J.1    Klein, T.E.2
  • 24
    • 0033081673 scopus 로고    scopus 로고
    • Computational investigations of structural changes resulting from point mutations in a collagen-like peptide
    • Klein TE, Huang CC. Computational investigations of structural changes resulting from point mutations in a collagen-like peptide. Biopolymers 1999;49:167-183.
    • (1999) Biopolymers , vol.49 , pp. 167-183
    • Klein, T.E.1    Huang, C.C.2
  • 25
    • 0036300984 scopus 로고    scopus 로고
    • Localized unfolding of collagen explains collagenase cleavage near imino-poor sites
    • Stultz CM. Localized unfolding of collagen explains collagenase cleavage near imino-poor sites. J Mol Biol 2002;319:997-1003.
    • (2002) J Mol Biol , vol.319 , pp. 997-1003
    • Stultz, C.M.1
  • 26
    • 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. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science 1994;266:75-81.
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 27
    • 32844466504 scopus 로고    scopus 로고
    • Evidence that collagen and tendon have monolayer water coverage in the native state
    • Fullerton GD, Amurao MR. Evidence that collagen and tendon have monolayer water coverage in the native state. Cell Biol Intl 2006;30:56-65.
    • (2006) Cell Biol Intl , vol.30 , pp. 56-65
    • Fullerton, G.D.1    Amurao, M.R.2
  • 29
    • 84986512474 scopus 로고    scopus 로고
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. Charmm: A program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 1983;4:187-217.
    • Brooks BR, Bruccoleri RE, Olafson BD, States DJ, Swaminathan S, Karplus M. Charmm: A program for macromolecular energy, minimization, and dynamics calculations. J Comput Chem 1983;4:187-217.
  • 32
    • 0024250301 scopus 로고
    • Polar hydrogen positions in proteins: Empirical energy placement and neutron diffraction comparison
    • Brünger AT, Karplus M. Polar hydrogen positions in proteins: empirical energy placement and neutron diffraction comparison. Proteins 1988;4:148-156.
    • (1988) Proteins , vol.4 , pp. 148-156
    • Brünger, A.T.1    Karplus, M.2
  • 34
    • 0036838777 scopus 로고    scopus 로고
    • A statistically derived parameterization for the collagen triple-helix
    • Rainey JK, Goh MC. A statistically derived parameterization for the collagen triple-helix. Protein Sci 2002;11:2748-2754.
    • (2002) Protein Sci , vol.11 , pp. 2748-2754
    • Rainey, J.K.1    Goh, M.C.2
  • 35
    • 0000341366 scopus 로고
    • Molecular dynamics simulation of galanin in aqueous and nonaqueous solution
    • Loof HD, Nilsson L, Rigler R. Molecular dynamics simulation of galanin in aqueous and nonaqueous solution. J Am Chem Soc 1992;114:4028-4035.
    • (1992) J Am Chem Soc , vol.114 , pp. 4028-4035
    • Loof, H.D.1    Nilsson, L.2    Rigler, R.3
  • 36
    • 25444463441 scopus 로고    scopus 로고
    • Structure, stability and folding of the collagen triple helix
    • Engel J, Bachinger HP. Structure, stability and folding of the collagen triple helix. Top Curr Chem 2005;247:7-33.
    • (2005) Top Curr Chem , vol.247 , pp. 7-33
    • Engel, J.1    Bachinger, H.P.2
  • 38
    • 19544368282 scopus 로고    scopus 로고
    • Correlations among hydrogen bonds in liquid water
    • Raiteri P, Laio A, Parrinello M. Correlations among hydrogen bonds in liquid water. Phys Rev Lett 2004;93:087 801.
    • (2004) Phys Rev Lett , vol.93 , pp. 087-801
    • Raiteri, P.1    Laio, A.2    Parrinello, M.3
  • 39
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz J. The entropic cost of bound water in crystals and biomolecules. Science 1994;264:670.
    • (1994) Science , vol.264 , pp. 670
    • Dunitz, J.1
  • 40
    • 33744490659 scopus 로고    scopus 로고
    • Matrix metalloproteinase dependent and independent collagen degradation
    • Song F, Wisithphrom K, Zhou J, Windsor LJ. Matrix metalloproteinase dependent and independent collagen degradation. Front Biosci 2006;11:3100-3120.
    • (2006) Front Biosci , vol.11 , pp. 3100-3120
    • Song, F.1    Wisithphrom, K.2    Zhou, J.3    Windsor, L.J.4
  • 41
    • 0031556719 scopus 로고    scopus 로고
    • Orientational disorder and entropy of water in protein cavities
    • Denisov V, Venu K, Peters J, Horlein H, Halle B. Orientational disorder and entropy of water in protein cavities. J Phys Chem B 1997;101:9380-9389.
    • (1997) J Phys Chem B , vol.101 , pp. 9380-9389
    • Denisov, V.1    Venu, K.2    Peters, J.3    Horlein, H.4    Halle, B.5
  • 42
    • 0033578333 scopus 로고    scopus 로고
    • Binding of buried structural water increases the flexibility of proteins
    • Fischer S, Verma CS. Binding of buried structural water increases the flexibility of proteins. Proc Natl Acad Sci USA 1999;96:9613-9615.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9613-9615
    • Fischer, S.1    Verma, C.S.2
  • 43
    • 25844437141 scopus 로고    scopus 로고
    • Translational-entropy gain of solvent upon protein folding
    • Harano Y, Kinoshita M. Translational-entropy gain of solvent upon protein folding. Biophys J 2005;89:2701-2710.
    • (2005) Biophys J , vol.89 , pp. 2701-2710
    • Harano, Y.1    Kinoshita, M.2
  • 44
    • 34250748568 scopus 로고    scopus 로고
    • Effect of the structural water on the mechanical properties of collagen-like microfibrils: A molecular dynamics study
    • Zhang D, Chippada U, Jordan K. Effect of the structural water on the mechanical properties of collagen-like microfibrils: a molecular dynamics study. Ann Biomed Eng 2007;35:1216-1230.
    • (2007) Ann Biomed Eng , vol.35 , pp. 1216-1230
    • Zhang, D.1    Chippada, U.2    Jordan, K.3
  • 45
    • 0027411181 scopus 로고
    • Thermodynamic β-sheet propensities measured using a zinc-finger host peptide
    • Kim CA, Berg JM. Thermodynamic β-sheet propensities measured using a zinc-finger host peptide. Nature 1993;362:267-270.
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 46
    • 33748283319 scopus 로고    scopus 로고
    • Coupling between hydration layer dynamics and unfolding kinetics of HP-36
    • Bandyopadhyay S, Chakraborty S, Bagchi B. Coupling between hydration layer dynamics and unfolding kinetics of HP-36. J Chem Phys 2006;125:084 912.
    • (2006) J Chem Phys , vol.125 , pp. 084-912
    • Bandyopadhyay, S.1    Chakraborty, S.2    Bagchi, B.3
  • 47
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • Griebenow K, Klibanov AM. On protein denaturation in aqueous-organic mixtures but not in pure organic solvents. J Am Chem Soc 1996;118:11695-11700.
    • (1996) J Am Chem Soc , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.M.2
  • 48
    • 0028847040 scopus 로고
    • Lyophilization-induced reversible changes in the secondary structure of proteins
    • Griebenow K, Klibanov AM. Lyophilization-induced reversible changes in the secondary structure of proteins. Proc Natl Acad Sci USA 1995;92:10969-10976.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10969-10976
    • Griebenow, K.1    Klibanov, A.M.2
  • 49
    • 0028078724 scopus 로고
    • Direct measurement of forces between self-assembled proteins: Temperature-dependent exponential forces between collagen triple helices
    • Leikin S, Rau DC, Parsegian VA. Direct measurement of forces between self-assembled proteins: temperature-dependent exponential forces between collagen triple helices. Proc Natl Acad Sci USA 1994;91:276-280.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 276-280
    • Leikin, S.1    Rau, D.C.2    Parsegian, V.A.3
  • 50
    • 0028967611 scopus 로고
    • Temperature-favoured assembly of collagen is driven by hydrophilic not hydrophobic interactions
    • Leikin S, Rau DC, Parsegian VA. Temperature-favoured assembly of collagen is driven by hydrophilic not hydrophobic interactions. Nat Struct Biol 1995;2:205-210.
    • (1995) Nat Struct Biol , vol.2 , pp. 205-210
    • Leikin, S.1    Rau, D.C.2    Parsegian, V.A.3
  • 51
    • 0030875806 scopus 로고    scopus 로고
    • Raman spectral evidence for hydration forces between collagen triple helices
    • Leikin S, Parsegian VA, Yang W, Walrafen GE. Raman spectral evidence for hydration forces between collagen triple helices. Proc Natl Acad Sci USA 1997;94:11312-11317.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11312-11317
    • Leikin, S.1    Parsegian, V.A.2    Yang, W.3    Walrafen, G.E.4
  • 52
    • 24644452139 scopus 로고    scopus 로고
    • Strain-controlled enzymatic cleavage of collagen in loaded matrix
    • Ruberti JW, Hallab NJ. Strain-controlled enzymatic cleavage of collagen in loaded matrix. Biochem Biophys Res Commun 2005;336: 483-489.
    • (2005) Biochem Biophys Res Commun , vol.336 , pp. 483-489
    • Ruberti, J.W.1    Hallab, N.J.2
  • 53
    • 0017345134 scopus 로고
    • Mechanochemical studies of enzymatic degradation of insoluble collagen fibers
    • Huang C, Yannas IV. Mechanochemical studies of enzymatic degradation of insoluble collagen fibers. J Biomed Mater Res 1977;11:137-154.
    • (1977) J Biomed Mater Res , vol.11 , pp. 137-154
    • Huang, C.1    Yannas, I.V.2
  • 54
    • 0029940647 scopus 로고    scopus 로고
    • Uniaxial tension inhibits tendon collagen degradation by collagenase in vitro
    • Nabeshima Y, Grood ES, Sakurai A, Herman JH. Uniaxial tension inhibits tendon collagen degradation by collagenase in vitro. J Orthop Res 1996;14:123-130.
    • (1996) J Orthop Res , vol.14 , pp. 123-130
    • Nabeshima, Y.1    Grood, E.S.2    Sakurai, A.3    Herman, J.H.4
  • 55
    • 33846152960 scopus 로고    scopus 로고
    • Inflammatory cells do not decrease the ultimate tensile strength of intact tendons in vivo and in vitro: Protective role of mechanical loading
    • Marsolais D, Duchesne E, Côté CH, Frenette J. Inflammatory cells do not decrease the ultimate tensile strength of intact tendons in vivo and in vitro: protective role of mechanical loading. J Appl Physiol 2007;102:11-17.
    • (2007) J Appl Physiol , vol.102 , pp. 11-17
    • Marsolais, D.1    Duchesne, E.2    Côté, C.H.3    Frenette, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.