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Volumn 31, Issue 8, 2013, Pages 862-873

Double thermal transitions of type I collagen in acidic solution

Author keywords

Double thermal transitions; PPII type structure; Thermodynamic; Triple helix structure; Type I collagen

Indexed keywords

COLLAGEN FIBER; COLLAGEN TYPE 1; PHENYLALANINE; TYROSINE;

EID: 84880098477     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2012.715042     Document Type: Article
Times cited : (23)

References (45)
  • 3
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio, B., & Tamburro, A.M. (2002). Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions. Chirality, 14, 782-792.
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 4
    • 0034030776 scopus 로고    scopus 로고
    • Influence of temperature and time on thermally induced forces in corneal collagen and the effect on laser thermokeratoplasty
    • Brinkmann, R., Radt, B., Flamm, C., Kampmeier, J., Koop, N., & Birngruber, R. (2000). Influence of temperature and time on thermally induced forces in corneal collagen and the effect on laser thermokeratoplasty. Journal of Cataract and Refractive Surgery, 26, 744-754.
    • (2000) Journal of Cataract and Refractive Surgery , vol.26 , pp. 744-754
    • Brinkmann, R.1    Radt, B.2    Flamm, C.3    Kampmeier, J.4    Koop, N.5    Birngruber, R.6
  • 5
    • 0030963588 scopus 로고    scopus 로고
    • The collagen triple-helix structure
    • Brodsky, B., & Ramshaw, J.A. (1997). The collagen triple-helix structure. Matrix Biology, 15, 545-554.
    • (1997) Matrix Biology , vol.15 , pp. 545-554
    • Brodsky, B.1    Ramshaw, J.A.2
  • 6
    • 47749145413 scopus 로고    scopus 로고
    • Triple-helical peptides: An approach to collagen conformation, stability, and self-association
    • Brodsky, B., Thiagarajan, G., Madhan, B., & Kar, K. (2008). Triple-helical peptides: An approach to collagen conformation, stability, and self-association. Biopolymers, 89, 345-353.
    • (2008) Biopolymers , vol.89 , pp. 345-353
    • Brodsky, B.1    Thiagarajan, G.2    Madhan, B.3    Kar, K.4
  • 7
    • 34347251868 scopus 로고    scopus 로고
    • FTIR studies of collagen model peptides: Complementary experimental and simulation approaches to conformation and unfolding
    • Bryan, M.A., Brauner, J.W., Anderle, G., Flach, C.R., Brodsky, B., & Mendelsohn, R. (2007). FTIR studies of collagen model peptides: Complementary experimental and simulation approaches to conformation and unfolding. Journal of the American Chemical Society, 129, 7877-7884.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 7877-7884
    • Bryan, M.A.1    Brauner, J.W.2    Anderle, G.3    Flach, C.R.4    Brodsky, B.5    Mendelsohn, R.6
  • 8
    • 34848897219 scopus 로고    scopus 로고
    • Nonpharmacologic therapies for acute and chronic low back pain: A review of the evidence for an American Pain Society/American College of Physicians clinical practice guideline
    • Chou, R., & Huffman, L.H. (2007). Nonpharmacologic therapies for acute and chronic low back pain: A review of the evidence for an American Pain Society/American College of Physicians clinical practice guideline. Annals of Internal Medicine, 147, 492-504.
    • (2007) Annals of Internal Medicine , vol.147 , pp. 492-504
    • Chou, R.1    Huffman, L.H.2
  • 10
    • 0342588050 scopus 로고    scopus 로고
    • Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding
    • Engel, J., & Bachinger, H.P. (2000). Cooperative equilibrium transitions coupled with a slow annealing step explain the sharpness and hysteresis of collagen folding. Matrix Biology, 19, 235-244.
    • (2000) Matrix Biology , vol.19 , pp. 235-244
    • Engel, J.1    Bachinger, H.P.2
  • 11
    • 0021715647 scopus 로고
    • A differential scanning calorimetry analysis of the age-related changes in the thermal stability of rat skin collagen
    • Flandin, F., Buffevant, C., & Herbage, D. (1984). A differential scanning calorimetry analysis of the age-related changes in the thermal stability of rat skin collagen. Biochimica et Biophysica Acta, 791, 205-211.
    • (1984) Biochimica et Biophysica Acta , vol.791 , pp. 205-211
    • Flandin, F.1    Buffevant, C.2    Herbage, D.3
  • 13
    • 0031575560 scopus 로고    scopus 로고
    • Characterization of collagen isolation and application of collagen gel as a drug carrier
    • Ho, H.O., Lin, L.H., & Sheu, M.T. (1997). Characterization of collagen isolation and application of collagen gel as a drug carrier. Journal of Controlled Release, 44, 103-112.
    • (1997) Journal of Controlled Release , vol.44 , pp. 103-112
    • Ho, H.O.1    Lin, L.H.2    Sheu, M.T.3
  • 14
    • 0015228624 scopus 로고
    • Reversible and irreversible denaturation of collagen fibers
    • Hormann, H., & Schlebusch, H. (1971). Reversible and irreversible denaturation of collagen fibers. Biochemistry, 10, 932-937.
    • (1971) Biochemistry , vol.10 , pp. 932-937
    • Hormann, H.1    Schlebusch, H.2
  • 15
    • 53849096006 scopus 로고    scopus 로고
    • The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens
    • Krane, S.M. (2008). The importance of proline residues in the structure, stability and susceptibility to proteolytic degradation of collagens. Amino Acids, 35, 703-710.
    • (2008) Amino Acids , vol.35 , pp. 703-710
    • Krane, S.M.1
  • 16
    • 39549109279 scopus 로고    scopus 로고
    • Effect of concentration and temperature on the rheological behavior of collagen solution
    • Lai, G., Li, Y., & Li, G. (2008). Effect of concentration and temperature on the rheological behavior of collagen solution. International Journal of Biological Macromolecules, 42, 285-291.
    • (2008) International Journal of Biological Macromolecules , vol.42 , pp. 285-291
    • Lai, G.1    Li, Y.2    Li, G.3
  • 19
    • 79551687594 scopus 로고    scopus 로고
    • The thermal behavior of collagen in solution: Effect of glycerol and 2-propanol
    • Li, J.H., & Li, G.Y. (2011). The thermal behavior of collagen in solution: Effect of glycerol and 2-propanol. International Journal of Biological Macromolecules, 48, 364-368.
    • (2011) International Journal of Biological Macromolecules , vol.48 , pp. 364-368
    • Li, J.H.1    Li, G.Y.2
  • 20
  • 21
    • 34447570983 scopus 로고    scopus 로고
    • Temperature induced denaturation of collagen in acidic solution
    • Mu, C., Li, D., Lin, W., Ding, Y., & Zhang, G. (2007). Temperature induced denaturation of collagen in acidic solution. Biopolymers, 86, 282-287.
    • (2007) Biopolymers , vol.86 , pp. 282-287
    • Mu, C.1    Li, D.2    Lin, W.3    Ding, Y.4    Zhang, G.5
  • 22
    • 0242659293 scopus 로고    scopus 로고
    • Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus)
    • Muyonga, J.H., Cole, C.G.B., & Duodu, K.G. (2004). Characterisation of acid soluble collagen from skins of young and adult Nile perch (Lates niloticus). Food Chemistry, 85, 81-89.
    • (2004) Food Chemistry , vol.85 , pp. 81-89
    • Muyonga, J.H.1    Cole, C.G.B.2    Duodu, K.G.3
  • 23
    • 33745563365 scopus 로고
    • Generalized 2-dimensional correlation method applicable to infrared, Raman, and other types of spectroscopy
    • Noda, I. (1993). Generalized 2-dimensional correlation method applicable to infrared, Raman, and other types of spectroscopy. Applied Spectroscopy, 47, 1329-1336.
    • (1993) Applied Spectroscopy , vol.47 , pp. 1329-1336
    • Noda, I.1
  • 24
    • 56349098272 scopus 로고    scopus 로고
    • Revisiting the molecular structure of collagen
    • Okuyama, K. (2008). Revisiting the molecular structure of collagen. Connective Tissue Research, 49, 299-310.
    • (2008) Connective Tissue Research , vol.49 , pp. 299-310
    • Okuyama, K.1
  • 26
    • 0014737293 scopus 로고
    • Thermal conformational transformation of tropocollagen. I. Calorimetric study
    • Privalov, P.L., & Tiktopulo, E.I. (1970). Thermal conformational transformation of tropocollagen. I. Calorimetric study. Biopolymers, 9, 127-139.
    • (1970) Biopolymers , vol.9 , pp. 127-139
    • Privalov, P.L.1    Tiktopulo, E.I.2
  • 27
    • 44449166039 scopus 로고    scopus 로고
    • Evidence of PPII-like helical conformation and glass transition in a self-assembled solid-state polypeptide-surfactant complex: Poly(L-histidine)/ docylbenzenesulfonic acid
    • Ramani, R., Hanski, S., Laiho, A., Tuma, R., Kilpelainen, S., Tuomisto, F., ... Ikkala, O. (2008). Evidence of PPII-like helical conformation and glass transition in a self-assembled solid-state polypeptide-surfactant complex: Poly(L-histidine)/docylbenzenesulfonic acid. Biomacromolecules, 9, 1390-1397.
    • (2008) Biomacromolecules , vol.9 , pp. 1390-1397
    • Ramani, R.1    Hanski, S.2    Laiho, A.3    Tuma, R.4    Kilpelainen, S.5    Tuomisto, F.6    Ikkala, O.7
  • 28
    • 0031692464 scopus 로고    scopus 로고
    • Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides
    • Ramshaw, J.A., Shah, N.K., & Brodsky, B. (1998). Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides. Journal of Structural Biology, 122, 86-91.
    • (1998) Journal of Structural Biology , vol.122 , pp. 86-91
    • Ramshaw, J.A.1    Shah, N.K.2    Brodsky, B.3
  • 29
    • 0029434529 scopus 로고
    • Recent developments of collagen-based materials for medical applications and drug delivery systems
    • Rao, K.P. (1995). Recent developments of collagen-based materials for medical applications and drug delivery systems. Journal of Biomaterials Science-Polymer Edition, 7, 623-645.
    • (1995) Journal of Biomaterials Science-Polymer Edition , vol.7 , pp. 623-645
    • Rao, K.P.1
  • 30
    • 20344400382 scopus 로고    scopus 로고
    • The structure of "unstructured" regions in peptides and proteins: Role of the polyproline II helix in protein folding and recognition
    • Rath, A., Davidson, A.R., & Deber, C.M. (2005). The structure of "unstructured" regions in peptides and proteins: Role of the polyproline II helix in protein folding and recognition. Biopolymers, 80, 179-185.
    • (2005) Biopolymers , vol.80 , pp. 179-185
    • Rath, A.1    Davidson, A.R.2    Deber, C.M.3
  • 31
    • 33847363476 scopus 로고    scopus 로고
    • Stochastic temperature modulation: A new technique in temperature-modulated DSC
    • Schawe, J.E.K., Hutter, T., Heitz, C., Alig, I., & Lellinger, D. (2006). Stochastic temperature modulation: A new technique in temperature-modulated DSC. Thermochimica Acta, 446, 147-155.
    • (2006) Thermochimica Acta , vol.446 , pp. 147-155
    • Schawe, J.E.K.1    Hutter, T.2    Heitz, C.3    Alig, I.4    Lellinger, D.5
  • 32
    • 59849108384 scopus 로고    scopus 로고
    • Structural transition during thermal denaturation of collagen in the solution and film states
    • Shanmugam, G., & Polavarapu, P.L. (2009). Structural transition during thermal denaturation of collagen in the solution and film states. Chirality, 21, 152-159.
    • (2009) Chirality , vol.21 , pp. 152-159
    • Shanmugam, G.1    Polavarapu, P.L.2
  • 34
    • 33749425694 scopus 로고    scopus 로고
    • Investigating mechanisms of collagen thermal denaturation by high resolution secondharmonic generation imaging
    • Sun, Y., Chen, W.L., Lin, S.J., Jee, S.H., Chen, Y.F., Lin, L.C., ... Dong, C.Y. (2006). Investigating mechanisms of collagen thermal denaturation by high resolution secondharmonic generation imaging. Biophysical Journal, 91, 2620-2625.
    • (2006) Biophysical Journal , vol.91 , pp. 2620-2625
    • Sun, Y.1    Chen, W.L.2    Lin, S.J.3    Jee, S.H.4    Chen, Y.F.5    Lin, L.C.6    Dong, C.Y.7
  • 35
    • 0036157963 scopus 로고    scopus 로고
    • A Raman optical activity study of rheomorphism in caseins, synucleins and tau - New insight into the structure and behaviour of natively unfolded proteins
    • Syme, C.D., Blanch, E.W., Holt, C., Jakes, R., Goedert, M., Hecht, L., & Barron, L.D. (2002). A Raman optical activity study of rheomorphism in caseins, synucleins and tau - new insight into the structure and behaviour of natively unfolded proteins. European Journal of Biochemistry, 269, 148-156.
    • (2002) European Journal of Biochemistry , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.D.7
  • 36
    • 0035452722 scopus 로고    scopus 로고
    • A mixture theory for heat-induced alterations in hydration and mechanical properties in soft tissues
    • Tao, L., Humphrey, J.D., & Rajagopal, K.R. (2001). A mixture theory for heat-induced alterations in hydration and mechanical properties in soft tissues. International Journal of Engineering Science, 39, 1535-1556.
    • (2001) International Journal of Engineering Science , vol.39 , pp. 1535-1556
    • Tao, L.1    Humphrey, J.D.2    Rajagopal, K.R.3
  • 39
    • 1042302160 scopus 로고    scopus 로고
    • The effects of urea and n-propanol on collagen denaturation: Using DSC, circular dicroism and viscosity
    • Usha, R., & Ramasami, T. (2004). The effects of urea and n-propanol on collagen denaturation: Using DSC, circular dicroism and viscosity. Thermochimica Acta, 409, 201-206.
    • (2004) Thermochimica Acta , vol.409 , pp. 201-206
    • Usha, R.1    Ramasami, T.2
  • 40
    • 37349057888 scopus 로고    scopus 로고
    • Stability of collagen with polyols against guanidine denaturation
    • Usha, R., & Ramasami, T. (2008). Stability of collagen with polyols against guanidine denaturation. Colloids Surf B Biointerfaces, 61, 39-42.
    • (2008) Colloids Surf B Biointerfaces , vol.61 , pp. 39-42
    • Usha, R.1    Ramasami, T.2
  • 41
    • 36749057761 scopus 로고    scopus 로고
    • Thermal denaturation of collagen analyzed by isoconversional method
    • Vyazovkin, S., Vincent, L., & Sbirrazzuoli, N. (2007). Thermal denaturation of collagen analyzed by isoconversional method. Macromolecular Bioscience, 7, 1181-1186.
    • (2007) Macromolecular Bioscience , vol.7 , pp. 1181-1186
    • Vyazovkin, S.1    Vincent, L.2    Sbirrazzuoli, N.3
  • 43
    • 0036405394 scopus 로고    scopus 로고
    • Denaturation of collagen via heating: An irreversible rate process
    • Wright, N.T., & Humphrey, J.D. (2002). Denaturation of collagen via heating: An irreversible rate process. Annual Review of Biomedical Engineering, 4, 109-128.
    • (2002) Annual Review of Biomedical Engineering , vol.4 , pp. 109-128
    • Wright, N.T.1    Humphrey, J.D.2
  • 45
    • 70350451569 scopus 로고    scopus 로고
    • Direct calculations of vibrational absorption and circular dichroism spectra of alanine dipeptide analog in water: Quantum mechanical/molecular mechanical molecular dynamics simulations
    • Yang, S., & Cho, M. (2009). Direct calculations of vibrational absorption and circular dichroism spectra of alanine dipeptide analog in water: Quantum mechanical/molecular mechanical molecular dynamics simulations. Journal of Chemical Physics, 131, 135102-135109.
    • (2009) Journal of Chemical Physics , vol.131 , pp. 135102-135109
    • Yang, S.1    Cho, M.2


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