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Volumn 92, Issue 6, 2007, Pages 2108-2119

Electrostatic interactions modulate the conformation of collagen I

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHLORIDE; COLLAGEN TYPE 1; ELECTROLYTE; HYDROXIDE; POTASSIUM CHLORIDE;

EID: 33947679349     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.094284     Document Type: Article
Times cited : (106)

References (69)
  • 1
    • 19644367664 scopus 로고    scopus 로고
    • Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering
    • Lutolf, M. P., and J. A. Hubbell. 2005. Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering. Nat. Biotechnol. 23:47-55.
    • (2005) Nat. Biotechnol , vol.23 , pp. 47-55
    • Lutolf, M.P.1    Hubbell, J.A.2
  • 2
    • 0347859159 scopus 로고
    • Collagen report: A review about the present state
    • Reich, G. 1995. Collagen report: a review about the present state. Leder. 46:192-199.
    • (1995) Leder , vol.46 , pp. 192-199
    • Reich, G.1
  • 4
    • 4344573242 scopus 로고    scopus 로고
    • An imaginary journey to the collagen molecule for a better understanding of leather waste treatments
    • Cot, J. 2004. An imaginary journey to the collagen molecule for a better understanding of leather waste treatments. J. Am. Leather Chem. Assoc. 99:322-350.
    • (2004) J. Am. Leather Chem. Assoc , vol.99 , pp. 322-350
    • Cot, J.1
  • 5
    • 25444463441 scopus 로고    scopus 로고
    • Structure, stability and folding of the collagen triple helix
    • Engel, J., and H. J. Bächinger. 2005. Structure, stability and folding of the collagen triple helix. Top. Curr. Chem. 247:7-33.
    • (2005) Top. Curr. Chem , vol.247 , pp. 7-33
    • Engel, J.1    Bächinger, H.J.2
  • 6
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich, A., and F. H. Crick. 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.2
  • 7
    • 0004291142 scopus 로고
    • Ramachandran, G. N, editor, Academic Press, New York
    • Ramachandran, G. N., editor. 1964. Treatise on Collagen. Academic Press, New York.
    • (1964) Treatise on Collagen
  • 8
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution
    • Bella, J., M. Eaton, B. Brodsky, and H. M. Berman. 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
  • 9
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • Kramer, R. Z., J. Bella, P. Mayville, B. Brodsky, and H. M. Berman. 1999. Sequence dependent conformational variations of collagen triple-helical structure. Nat. Struct. Biol. 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
  • 10
    • 0141621226 scopus 로고    scopus 로고
    • Macromolecular specificity of collagen fibrillogenesis: Fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheath
    • Hansen, U., and P. Bruckner. 2003. Macromolecular specificity of collagen fibrillogenesis: fibrils of collagens I and XI contain a heterotypic alloyed core and a collagen I sheath. J. Biol. Chem. 278:37352-37359.
    • (2003) J. Biol. Chem , vol.278 , pp. 37352-37359
    • Hansen, U.1    Bruckner, P.2
  • 13
    • 0026036378 scopus 로고
    • Analysis of structural design features in collagen
    • Jones, E. Y., and A. J. Miller. 1991. Analysis of structural design features in collagen. J. Mol. Biol. 218:209-219.
    • (1991) J. Mol. Biol , vol.218 , pp. 209-219
    • Jones, E.Y.1    Miller, A.J.2
  • 14
    • 0031465742 scopus 로고    scopus 로고
    • Positional preferences of ionizable residues in Gly-X-Y triplets of the collagen triple-helix
    • Chan, V. C., J. A. M. Ramshaw, A. Kirkpatrick, K. Beck, and B. Brodsky. 1997. Positional preferences of ionizable residues in Gly-X-Y triplets of the collagen triple-helix. J. Biol. Chem. 272:31441-31446.
    • (1997) J. Biol. Chem , vol.272 , pp. 31441-31446
    • Chan, V.C.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Beck, K.4    Brodsky, B.5
  • 15
    • 0029149772 scopus 로고
    • The effect of electrostatic charge interactions on release rates of gentamicin from collagen matrices
    • Singh, M. P., J. Stefko, J. A. Lumpkin, and J. Rosenblatt. 1995. The effect of electrostatic charge interactions on release rates of gentamicin from collagen matrices. Pharm. Res. 12:1205-1210.
    • (1995) Pharm. Res , vol.12 , pp. 1205-1210
    • Singh, M.P.1    Stefko, J.2    Lumpkin, J.A.3    Rosenblatt, J.4
  • 16
    • 0028261035 scopus 로고
    • Electrostatic Interactions in collagen-like triple-helical peptides
    • Venugopal, M. G., J. A. M. Ramshaw, E. Braswell, D. Zhu, and B. Brodsky. 1994. Electrostatic Interactions in collagen-like triple-helical peptides. Biochemistry. 33:7948-7956.
    • (1994) Biochemistry , vol.33 , pp. 7948-7956
    • Venugopal, M.G.1    Ramshaw, J.A.M.2    Braswell, E.3    Zhu, D.4    Brodsky, B.5
  • 17
    • 13444292142 scopus 로고    scopus 로고
    • Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability
    • Persikov, A. V., J. A. M. Ramshaw, A. Kirkpatrick, and B. Brodsky. 2005. Electrostatic interactions involving lysine make major contributions to collagen triple-helix stability. Biochemistry. 44:1414-1422.
    • (2005) Biochemistry , vol.44 , pp. 1414-1422
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Kirkpatrick, A.3    Brodsky, B.4
  • 18
    • 0025319808 scopus 로고
    • Energetics of intrachain salt-linkage formation in collagen
    • Katz, E. P., and C. W. David. 1990. Energetics of intrachain salt-linkage formation in collagen. Biopolymers. 29:791-798.
    • (1990) Biopolymers , vol.29 , pp. 791-798
    • Katz, E.P.1    David, C.W.2
  • 19
    • 0030560866 scopus 로고    scopus 로고
    • Basic thermoanalytical studies of insoluble collagen matrices
    • Friess, W., and G. Lee. 1996. Basic thermoanalytical studies of insoluble collagen matrices. Biomaterials. 17:2289-2294.
    • (1996) Biomaterials , vol.17 , pp. 2289-2294
    • Friess, W.1    Lee, G.2
  • 20
    • 0035219275 scopus 로고    scopus 로고
    • Thermally labile domains in the collagen molecule
    • Miles, C. A., and A. J. Bailey. 2001. Thermally labile domains in the collagen molecule. Micron. 32:325-332.
    • (2001) Micron , vol.32 , pp. 325-332
    • Miles, C.A.1    Bailey, A.J.2
  • 22
    • 0014198141 scopus 로고
    • The role of pH, Temperature, salt type, and salt concentration on the stability of the crystalline, helical and randomly coiled forms of collagen
    • Bianchi, E., and G. Conio. 1967. The role of pH, Temperature, salt type, and salt concentration on the stability of the crystalline, helical and randomly coiled forms of collagen. J. Biol. Chem. 242:1361-1369.
    • (1967) J. Biol. Chem , vol.242 , pp. 1361-1369
    • Bianchi, E.1    Conio, G.2
  • 23
    • 0028918983 scopus 로고
    • The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry
    • Miles, C. A., T. V. Burjanadze, and A. J. Bailey. 1995. The kinetics of the thermal denaturation of collagen in unrestrained rat tail tendon determined by differential scanning calorimetry. J. Mol. Biol. 245:437-446.
    • (1995) J. Mol. Biol , vol.245 , pp. 437-446
    • Miles, C.A.1    Burjanadze, T.V.2    Bailey, A.J.3
  • 24
    • 0032474437 scopus 로고    scopus 로고
    • Denaturation of type I collagen fibrils is an endothermic process accompanied by a noticeable change in the partial heat capacity
    • Tiktopulo, E. I., and A. V. Kajava. 1998. Denaturation of type I collagen fibrils is an endothermic process accompanied by a noticeable change in the partial heat capacity. Biochemistry. 37:8147-8152.
    • (1998) Biochemistry , vol.37 , pp. 8147-8152
    • Tiktopulo, E.I.1    Kajava, A.V.2
  • 25
    • 0034159718 scopus 로고    scopus 로고
    • Effect of pH on dimensional stability of rat tail tendon collagen fiber
    • Usha, R., and T. Ramasami. 2000. Effect of pH on dimensional stability of rat tail tendon collagen fiber. J. Appl. Polym. Sci. 75:1577-1584.
    • (2000) J. Appl. Polym. Sci , vol.75 , pp. 1577-1584
    • Usha, R.1    Ramasami, T.2
  • 26
    • 0344443243 scopus 로고    scopus 로고
    • 2 on the thermal denaturation characteristics of intramuscular connective tissue
    • 2 on the thermal denaturation characteristics of intramuscular connective tissue. Thermochim. Acta. 407:105-112.
    • (2003) Thermochim. Acta , vol.407 , pp. 105-112
    • Aktas, N.1
  • 27
    • 0033930562 scopus 로고    scopus 로고
    • Influence of neutral salts on the hydrothermal stability of acid-soluble collagen
    • Brown, E. M., H. M. Farrell, and R. J. Wildermuth. 2000. Influence of neutral salts on the hydrothermal stability of acid-soluble collagen. J. Protein Chem. 19:85-92.
    • (2000) J. Protein Chem , vol.19 , pp. 85-92
    • Brown, E.M.1    Farrell, H.M.2    Wildermuth, R.J.3
  • 30
    • 4143143243 scopus 로고    scopus 로고
    • In vitro reconstitution of fibrillar collagen type I assemblies at reactive polymer surfaces
    • Salchert, K., U. Streller, T. Pompe, N. Herold, M. Grimmer, and C. Werner. 2004. In vitro reconstitution of fibrillar collagen type I assemblies at reactive polymer surfaces. Biomacromolecules. 5:1340-1350.
    • (2004) Biomacromolecules , vol.5 , pp. 1340-1350
    • Salchert, K.1    Streller, U.2    Pompe, T.3    Herold, N.4    Grimmer, M.5    Werner, C.6
  • 32
    • 0023691514 scopus 로고
    • Fourier transform IR spectroscopy of collagen and gelatin solutions: Deconvolution of the amide I band for conformational studies
    • Payne, K. J., and A. Veis. 1988. Fourier transform IR spectroscopy of collagen and gelatin solutions: deconvolution of the amide I band for conformational studies. Biopolymers. 27:1749-1760.
    • (1988) Biopolymers , vol.27 , pp. 1749-1760
    • Payne, K.J.1    Veis, A.2
  • 33
    • 0027988296 scopus 로고
    • Protein secondary structure from circular dichroism spectroscopy
    • Sreerama, N., and R. W. Woody. 1994. Protein secondary structure from circular dichroism spectroscopy. J. Mol. Biol. 242:497-507.
    • (1994) J. Mol. Biol , vol.242 , pp. 497-507
    • Sreerama, N.1    Woody, R.W.2
  • 34
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., S. Y. Venyaminov, and R. W. Woody. 1999. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8:370-380.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 35
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., S. Y. Venyaminov, and R. W. Woody. 2000. Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287:243-251.
    • (2000) Anal. Biochem , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 36
    • 0015455860 scopus 로고
    • Effect of temperature on the circular dichroism spectra of polypeptides in the extended state
    • Tiffany, M. L., and S. Krimm. 1972. Effect of temperature on the circular dichroism spectra of polypeptides in the extended state. Biopolymers. 11:2309-2316.
    • (1972) Biopolymers , vol.11 , pp. 2309-2316
    • Tiffany, M.L.1    Krimm, S.2
  • 37
    • 0027932724 scopus 로고
    • Poly(pro)II helices in globular proteins: Identification and circular dichroic analysis
    • Sreerama, N., and R. W. Woody. 1994. Poly(pro)II helices in globular proteins: identification and circular dichroic analysis. Biochemistry. 33: 10022-10025.
    • (1994) Biochemistry , vol.33 , pp. 10022-10025
    • Sreerama, N.1    Woody, R.W.2
  • 38
    • 0001183376 scopus 로고
    • Systemin has the characteristics of a poly(L-proline) II type helix
    • Toumadje, A., and W. C. Johnson, Jr. 1995. Systemin has the characteristics of a poly(L-proline) II type helix. J. Am. Chem. Soc. 117:7023-7024.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7023-7024
    • Toumadje, A.1    Johnson Jr., W.C.2
  • 39
    • 0029837626 scopus 로고    scopus 로고
    • Acetyl-terminated and template-assembled collagen-based polypeptides composed of Gly-Pro-Hyp sequences. 2. Synthesis and conformational analysis by circular dichroism, ultraviolet absorbance, and optical rotation
    • Feng, Y., G. Melacini, J. P. Taulane, and M. Goodman. 1996. Acetyl-terminated and template-assembled collagen-based polypeptides composed of Gly-Pro-Hyp sequences. 2. Synthesis and conformational analysis by circular dichroism, ultraviolet absorbance, and optical rotation. J. Am. Chem. Soc. 118:10351-10358.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 10351-10358
    • Feng, Y.1    Melacini, G.2    Taulane, J.P.3    Goodman, M.4
  • 40
    • 0347717818 scopus 로고    scopus 로고
    • A(4R)- or a (4S)-fluoroproline residue in position XAA of the (XAA-YAA-Gly) collagen repeat severely affects triple helix formation
    • Barth, D., A. G. Milbradt, C. Renner, and L. Moroder. 2004. A(4R)- or a (4S)-fluoroproline residue in position XAA of the (XAA-YAA-Gly) collagen repeat severely affects triple helix formation. ChemBioChem. 5:79-86.
    • (2004) ChemBioChem , vol.5 , pp. 79-86
    • Barth, D.1    Milbradt, A.G.2    Renner, C.3    Moroder, L.4
  • 42
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • Kumar, S., and R. Nussinov. 2002. Close-range electrostatic interactions in proteins. ChemBioChem. 3:604-617.
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 43
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z. S., and B. Tidor. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 44
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig, B., and A. Nicholls. 1995. Classical electrostatics in biology and chemistry. Science. 268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 45
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hyperthermophilic proteins
    • Xiao, L., and B. Honig. 1999. Electrostatic contributions to the stability of hyperthermophilic proteins. J. Mol. Biol. 289:1435-1444.
    • (1999) J. Mol. Biol , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 46
    • 0035371061 scopus 로고    scopus 로고
    • Fluctuations in ion pairs and their stabilities in proteins
    • Kumar, S., and R. Nussinov. 2001. Fluctuations in ion pairs and their stabilities in proteins. Proteins Struct. Funct. Genet. 43:433-454.
    • (2001) Proteins Struct. Funct. Genet , vol.43 , pp. 433-454
    • Kumar, S.1    Nussinov, R.2
  • 47
    • 0036708467 scopus 로고    scopus 로고
    • Relationship between ion pair geometries and electrostatic strengths in proteins
    • Kumar, S., and R. Nussinov. 2002. Relationship between ion pair geometries and electrostatic strengths in proteins. Biophys. J. 83:1595-1612.
    • (2002) Biophys. J , vol.83 , pp. 1595-1612
    • Kumar, S.1    Nussinov, R.2
  • 48
    • 0036708444 scopus 로고    scopus 로고
    • Electrostatic contributions to T4 lysozyme stability: Solvent-exposed charges versus semi-buried salt bridges
    • Dong, F., and H. X. Zhou. 2002. Electrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges. Biophys. J. 83:1341-1347.
    • (2002) Biophys. J , vol.83 , pp. 1341-1347
    • Dong, F.1    Zhou, H.X.2
  • 49
    • 0037432563 scopus 로고    scopus 로고
    • Contribution of surface salt-bridges to protein stability: Guidelines for protein engineering
    • Makhatadze, G. I., V. V. Loladze, D. N. Ermolenko, X. Chen, and S. T. Thomas. 2003. Contribution of surface salt-bridges to protein stability: guidelines for protein engineering. J. Mol. Biol. 327: 1135-1148.
    • (2003) J. Mol. Biol , vol.327 , pp. 1135-1148
    • Makhatadze, G.I.1    Loladze, V.V.2    Ermolenko, D.N.3    Chen, X.4    Thomas, S.T.5
  • 50
    • 1242317050 scopus 로고    scopus 로고
    • Salt-bridges can stabilize but not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1
    • Molero, B. I., J. A. Zitzewitz, and C. R. Matthews. 2004. Salt-bridges can stabilize but not accelerate the folding of the homodimeric coiled-coil peptide GCN4-p1. J. Mol. Biol. 336:989-996.
    • (2004) J. Mol. Biol , vol.336 , pp. 989-996
    • Molero, B.I.1    Zitzewitz, J.A.2    Matthews, C.R.3
  • 51
    • 21444453832 scopus 로고    scopus 로고
    • Prediction of collagen stability from amino acid sequence
    • Persikov, A. V., J. A. M. Ramshaw, and B. Brodsky. 2005. Prediction of collagen stability from amino acid sequence. J. Biol. Chem. 280: 19343-19349.
    • (2005) J. Biol. Chem , vol.280 , pp. 19343-19349
    • Persikov, A.V.1    Ramshaw, J.A.M.2    Brodsky, B.3
  • 52
    • 0027053121 scopus 로고
    • Unique side-chain conformation encoding for chirality and azimuthal orientation in the molecular packing of skin collagen
    • Katz, E. P., and C. W. David. 1992. Unique side-chain conformation encoding for chirality and azimuthal orientation in the molecular packing of skin collagen. J. Mol. Biol. 228:963-969.
    • (1992) J. Mol. Biol , vol.228 , pp. 963-969
    • Katz, E.P.1    David, C.W.2
  • 53
    • 0342343482 scopus 로고
    • Debye-Hückel theory of model polyelectrolytes
    • Soumpasis, D. 1978. Debye-Hückel theory of model polyelectrolytes. J. Chem. Phys. 69:3190-3196.
    • (1978) J. Chem. Phys , vol.69 , pp. 3190-3196
    • Soumpasis, D.1
  • 54
    • 0023646665 scopus 로고
    • Rational modification of enzyme catalysis by engineering surface charge
    • Russell, A. J., and A. R. Fersht. 1987. Rational modification of enzyme catalysis by engineering surface charge. Nature. 328:496-500.
    • (1987) Nature , vol.328 , pp. 496-500
    • Russell, A.J.1    Fersht, A.R.2
  • 56
    • 0020492960 scopus 로고
    • Anion binding and pH-dependent electrostatic effects in ribonuclease
    • Matthew, J. B., and F. M. Richards. 1982. Anion binding and pH-dependent electrostatic effects in ribonuclease. Biochemistry. 21:4989-4999.
    • (1982) Biochemistry , vol.21 , pp. 4989-4999
    • Matthew, J.B.1    Richards, F.M.2
  • 57
    • 1542440402 scopus 로고    scopus 로고
    • Protein electrostatics: A review of the equations and methods used to model electrostatic equations in biomolecules - applications in biotechnology
    • M. R. El-Gewely, editor. Elsevier/North Holland, Amsterdam
    • Neves-Petersen, M. T., and S. B. Petersen. 2003. Protein electrostatics: a review of the equations and methods used to model electrostatic equations in biomolecules - applications in biotechnology. In Biotechnology Annual Review 9. M. R. El-Gewely, editor. Elsevier/North Holland, Amsterdam.
    • (2003) Biotechnology Annual Review , vol.9
    • Neves-Petersen, M.T.1    Petersen, S.B.2
  • 58
    • 0027231258 scopus 로고
    • On the pH dependence of protein stability
    • Yang, A.-S., and B. Honig. 1993. On the pH dependence of protein stability. J. Mol. Biol. 231:459-474.
    • (1993) J. Mol. Biol , vol.231 , pp. 459-474
    • Yang, A.-S.1    Honig, B.2
  • 59
    • 0016207302 scopus 로고
    • Electrostatic effects in myoglobins. Hydrogen ion equilibria in sperm whale ferri-myoglobin
    • Shire, S. J., I. H. Hanania, and F. R. N. Gurd. 1974. Electrostatic effects in myoglobins. Hydrogen ion equilibria in sperm whale ferri-myoglobin. Biochemistry. 13:2967-2974.
    • (1974) Biochemistry , vol.13 , pp. 2967-2974
    • Shire, S.J.1    Hanania, I.H.2    Gurd, F.R.N.3
  • 60
    • 0015520587 scopus 로고
    • Interpretation of protein titration curves. Application to lysozyme
    • Tanford, C., and R. Roxby. 1972. Interpretation of protein titration curves. Application to lysozyme. Biochemistry. 11:2192-2198.
    • (1972) Biochemistry , vol.11 , pp. 2192-2198
    • Tanford, C.1    Roxby, R.2
  • 61
    • 0002183787 scopus 로고    scopus 로고
    • Ionization processes and proton binding in polyprotic systems: Small molecules, proteins, interfaces and polyelectrolytes
    • Borkovec, M., B. Jönsson, and G. J. M. Koper. 2001. Ionization processes and proton binding in polyprotic systems: small molecules, proteins, interfaces and polyelectrolytes. Surf. Colloid Sci. 16:99-339.
    • (2001) Surf. Colloid Sci , vol.16 , pp. 99-339
    • Borkovec, M.1    Jönsson, B.2    Koper, G.J.M.3
  • 62
    • 33947622601 scopus 로고
    • Observations on the isoionic and isoelectric point of acid-processed gelatin from insoluble and citrate-extracted collagen
    • Jackson, D. S., and A. Neuberger. 1957. Observations on the isoionic and isoelectric point of acid-processed gelatin from insoluble and citrate-extracted collagen. Biochim. Biophys. Acta. 26:638-639.
    • (1957) Biochim. Biophys. Acta , vol.26 , pp. 638-639
    • Jackson, D.S.1    Neuberger, A.2
  • 63
    • 33947639987 scopus 로고
    • Microelectrophoretic studies of soluble collagen
    • Gilbert, I. G. F. 1960. Microelectrophoretic studies of soluble collagen. Biochim. Biophys. Acta. 4:156-162.
    • (1960) Biochim. Biophys. Acta , vol.4 , pp. 156-162
    • Gilbert, I.G.F.1
  • 65
    • 0035856061 scopus 로고    scopus 로고
    • Electrokinetic measurements reveal interfacial charge at polymer films caused by simple electrolyte ions
    • Zimmermann, R., S. Dukhin, and C. Werner. 2001. Electrokinetic measurements reveal interfacial charge at polymer films caused by simple electrolyte ions. J. Phys. Chem. B. 105:8544-8549.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 8544-8549
    • Zimmermann, R.1    Dukhin, S.2    Werner, C.3
  • 67
    • 85030509154 scopus 로고    scopus 로고
    • ExPASy Proteomics Server: Swiss-Prot/TrEMBL: P02452 (CO1A1_HUMAN), P08123 (CO1A2_HUMAN).
    • ExPASy Proteomics Server: Swiss-Prot/TrEMBL: P02452 (CO1A1_HUMAN), P08123 (CO1A2_HUMAN).
  • 69
    • 0030963588 scopus 로고    scopus 로고
    • The collagen triple-helix structure
    • Brodsky, B., and J. A. M. Ramshaw. 1997. The collagen triple-helix structure. Matrix Biol. 15:545-554.
    • (1997) Matrix Biol , vol.15 , pp. 545-554
    • Brodsky, B.1    Ramshaw, J.A.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.