메뉴 건너뛰기




Volumn 17, Issue 15, 2009, Pages 13102-13115

Terahertz spectroscopic differentiation of microstructures in protein gels

Author keywords

[No Author keywords available]

Indexed keywords

FOURIER TRANSFORM INFRARED SPECTROSCOPY; GELS; IMAGING TECHNIQUES; MICROSTRUCTURE; NEURODEGENERATIVE DISEASES; PROTEINS;

EID: 67749145449     PISSN: None     EISSN: 10944087     Source Type: Journal    
DOI: 10.1364/OE.17.013102     Document Type: Article
Times cited : (40)

References (45)
  • 1
    • 0001894533 scopus 로고    scopus 로고
    • Pulsed terahertz spectroscopy of DNA, bovine serum albumin and collagen between 0.1 and 2.0 THz
    • A. G. Markelz, A. Roitberg, and E. J. Heilweil, "Pulsed terahertz spectroscopy of DNA, bovine serum albumin and collagen between 0.1 and 2.0 THz," Chemical Physics Letters 320, 42-48 (2000).
    • (2000) Chemical Physics Letters , vol.320 , pp. 42-48
    • Markelz, A.G.1    Roitberg, A.2    Heilweil, E.J.3
  • 2
    • 0037038534 scopus 로고    scopus 로고
    • Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy
    • B. M. Fischer, M. Walther, and P. U. Jepsen, "Far-infrared vibrational modes of DNA components studied by terahertz time-domain spectroscopy," Physics in Medicine and Biology 47, 3807-3814 (2002).
    • (2002) Physics in Medicine and Biology , vol.47 , pp. 3807-3814
    • Fischer, B.M.1    Walther, M.2    Jepsen, P.U.3
  • 3
    • 0041843665 scopus 로고    scopus 로고
    • Protein flexibility and conformational state: A comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin
    • S. E. Whitmire, D. Wolpert, A. G. Markelz, J. R. Hillebrecht, J. Galan, and R. R. Birge, "Protein flexibility and conformational state: A comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsin," Biophysical Journal 85, 1269-1277 (2003).
    • (2003) Biophysical Journal , vol.85 , pp. 1269-1277
    • Whitmire, S.E.1    Wolpert, D.2    Markelz, A.G.3    Hillebrecht, J.R.4    Galan, J.5    Birge, R.R.6
  • 5
    • 34347390447 scopus 로고    scopus 로고
    • Protein dynamical transition in terahertz dielectric response
    • A. G. Markelz, J. R. Knab, J. Y. Chen, and Y. He, "Protein dynamical transition in terahertz dielectric response," Chemical Physics Letters 442, 413-417 (2007).
    • (2007) Chemical Physics Letters , vol.442 , pp. 413-417
    • Markelz, A.G.1    Knab, J.R.2    Chen, J.Y.3    He, Y.4
  • 7
    • 33644615447 scopus 로고    scopus 로고
    • Critical hydration and temperature effects on terahertz biomolecu-lar sensing
    • J. O. Jensen and J.-M. Theriault, eds, Proc. SPIE, 59950P
    • J. Knab, B. Shah, J.-Y Chen, and A. Markelz, "Critical hydration and temperature effects on terahertz biomolecu-lar sensing," in Chemical and Biological Standoff Detection III, J. O. Jensen and J.-M. Theriault, eds., Proc. SPIE 5995, 59950P (2005).
    • (2005) Chemical and Biological Standoff Detection III , vol.5995
    • Knab, J.1    Shah, B.2    Chen, J.-Y.3    Markelz, A.4
  • 8
    • 33646170638 scopus 로고    scopus 로고
    • Hydration dependence of conformational dielectric relaxation of lysozyme
    • J. Knab, J.-Y. Chen, and A. Markelz, "Hydration dependence of conformational dielectric relaxation of lysozyme," Biophysical Journal 90, 2576-2581 (2006).
    • (2006) Biophysical Journal , vol.90 , pp. 2576-2581
    • Knab, J.1    Chen, J.-Y.2    Markelz, A.3
  • 10
    • 39449114471 scopus 로고    scopus 로고
    • Terahertz dielectric sensitivity to biomolecular structure and function
    • A. G. Markelz, "Terahertz dielectric sensitivity to biomolecular structure and function," IEEE Journal of Selected Topics in Quantum Electronics 14, 180-190 (2008).
    • (2008) IEEE Journal of Selected Topics in Quantum Electronics , vol.14 , pp. 180-190
    • Markelz, A.G.1
  • 14
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • D. J. Selkoe, "Folding proteins in fatal ways," Nature 426, 900-904 (2003).
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 17
    • 9744228666 scopus 로고    scopus 로고
    • Fibrillar β-Lactoglobulin gels: Part 1. Fibril formation and structure
    • W. S. Gosal, A. H. Clark, and S. B. Ross-Murphy, "Fibrillar β-Lactoglobulin gels: Part 1. Fibril formation and structure," Biomacromolecules 5, 2408-2419 (2004).
    • (2004) Biomacromolecules , vol.5 , pp. 2408-2419
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 18
    • 13844256920 scopus 로고    scopus 로고
    • β- Lactoglobulin gelation and modification: Effect of selected acidulants and heating conditions
    • J. J. Resch, C. R. Daubert, and E. A. Foegeding, "β- Lactoglobulin gelation and modification: Effect of selected acidulants and heating conditions," Journal of Food Science 70, C79-C86 (2005).
    • (2005) Journal of Food Science , vol.70
    • Resch, J.J.1    Daubert, C.R.2    Foegeding, E.A.3
  • 19
    • 0034578634 scopus 로고    scopus 로고
    • Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels
    • T. Lefevre and M. Subirade, "Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels," Biopolymers 54, 578-586 (2000).
    • (2000) Biopolymers , vol.54 , pp. 578-586
    • Lefevre, T.1    Subirade, M.2
  • 23
    • 0000266449 scopus 로고
    • Interactions of a-lactalbumin and bovine serum-albumin with β-lactoglobulin in thermally induced gelation
    • M. E. Hines and E. A. Foegeding, "Interactions of a-lactalbumin and bovine serum-albumin with β-lactoglobulin in thermally induced gelation," Journal of Agricultural and Food Chemistry 41, 341-346 (1993).
    • (1993) Journal of Agricultural and Food Chemistry , vol.41 , pp. 341-346
    • Hines, M.E.1    Foegeding, E.A.2
  • 25
    • 12344272183 scopus 로고    scopus 로고
    • Aggregation across the length-scales in β-lactoglobulin
    • E. H. C. Bromley, M. R. H. Krebs, and A. M. Donald, "Aggregation across the length-scales in β-lactoglobulin," Faraday Discussions 128, 13-27 (2005).
    • (2005) Faraday Discussions , vol.128 , pp. 13-27
    • Bromley, E.H.C.1    Krebs, M.R.H.2    Donald, A.M.3
  • 26
    • 33846839238 scopus 로고    scopus 로고
    • Protein particulates: Another generic form of protein aggregation?
    • M. R. H. Krebs, G. L. Devlin, and A. M. Donald, "Protein particulates: Another generic form of protein aggregation?" Biophysical Journal 92, 1336-1342 (2007).
    • (2007) Biophysical Journal , vol.92 , pp. 1336-1342
    • Krebs, M.R.H.1    Devlin, G.L.2    Donald, A.M.3
  • 27
  • 28
    • 0034228736 scopus 로고    scopus 로고
    • Heat-induced gelation of β-lactoglobulin. 1. Time-resolved dynamic light scattering
    • S. I. Takata, T. Norisuye, N. Tanaka, and M. Shibayama, "Heat-induced gelation of β-lactoglobulin. 1. Time-resolved dynamic light scattering," Macromolecules 33, 5470-5475 (2000).
    • (2000) Macromolecules , vol.33 , pp. 5470-5475
    • Takata, S.I.1    Norisuye, T.2    Tanaka, N.3    Shibayama, M.4
  • 29
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B
    • J. I. Boye, C. Y. Ma, A. Ismail, V. R. Harwalkar, and M. Kalab, "Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B," Journal of Agricultural and Food Chemistry 45, 1608-1618 (1997).
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 1608-1618
    • Boye, J.I.1    Ma, C.Y.2    Ismail, A.3    Harwalkar, V.R.4    Kalab, M.5
  • 30
    • 33845611464 scopus 로고    scopus 로고
    • Mechanisms of structure formation in particulate gels of β-lactoglobulin formed near the isoelectric point
    • E. H. C. Bromley, M. R. H. Krebs, and A. M. Donald, "Mechanisms of structure formation in particulate gels of β-lactoglobulin formed near the isoelectric point," European Physical Journal E 21, 145-152 (2006).
    • (2006) European Physical Journal E , vol.21 , pp. 145-152
    • Bromley, E.H.C.1    Krebs, M.R.H.2    Donald, A.M.3
  • 31
    • 0342374989 scopus 로고    scopus 로고
    • Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation
    • C. Le Bon, T. Nicolai, and D. Durand, "Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation," Macromolecules 32, 6120-6127 (1999).
    • (1999) Macromolecules , vol.32 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 32
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
    • C. M. Bryant and D. J. McClements, "Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey," Trends in Food Science & Technology 9, 143-151 (1998).
    • (1998) Trends in Food Science & Technology , vol.9 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 33
    • 9744282630 scopus 로고    scopus 로고
    • Fibrillar β-Lactoglobulin gels: Part 2. Dynamic mechanical characterization of heat-set systems
    • W. S. Gosal, A. H. Clark, and S. B. Ross-Murphy, "Fibrillar β-Lactoglobulin gels: Part 2. Dynamic mechanical characterization of heat-set systems," Biomacromolecules 5, 2420-2429 (2004).
    • (2004) Biomacromolecules , vol.5 , pp. 2420-2429
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 34
    • 9744255442 scopus 로고    scopus 로고
    • Fibrillar β-lactoglobulin gels: Part 3. Dynamic mechanical characterization of solvent-induced systems
    • W. S. Gosal, A. H. Clark, and S. B. Ross-Murphy, "Fibrillar β-lactoglobulin gels: Part 3. Dynamic mechanical characterization of solvent-induced systems," Biomacromolecules 5, 2430-2438 (2004).
    • (2004) Biomacromolecules , vol.5 , pp. 2430-2438
    • Gosal, W.S.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 36
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
    • M. A. de la Fuente, H. Singh, and Y. Hemar, "Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins," Trends in Food Science & Technology 13, 262-274 (2002).
    • (2002) Trends in Food Science & Technology , vol.13 , pp. 262-274
    • de la Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 37
    • 11244340520 scopus 로고    scopus 로고
    • Thermally induced fibrillar aggregation of hen egg white lysozyme
    • L. N. Arnaudov and R. de Vries, "Thermally induced fibrillar aggregation of hen egg white lysozyme," Biophysical Journal 88, 515-526 (2005).
    • (2005) Biophysical Journal , vol.88 , pp. 515-526
    • Arnaudov, L.N.1    de Vries, R.2
  • 44
    • 0003173090 scopus 로고
    • Mechanics of freezing in living cells and tissues
    • H. T. Meryman, "Mechanics of freezing in living cells and tissues," Science 124, 515-521 (1956).
    • (1956) Science , vol.124 , pp. 515-521
    • Meryman, H.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.