메뉴 건너뛰기




Volumn 8, Issue 4, 2016, Pages 409-427

Dynamic light scattering: a practical guide and applications in biomedical sciences

Author keywords

Analytical ultracentrifuge; Diffusion coefficient; Dynamic light scattering; Hydrodynamic radius; Light scattering; Protein ligand interactions; Protein nucleic acid complexes; Protein protein complexes

Indexed keywords

ENTACTIN 1; EXTRACELLULAR MATRIX PROTEIN; NUCLEIC ACID; OVALBUMIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VIRUS RNA;

EID: 85000399690     PISSN: 18672450     EISSN: 18672469     Source Type: Journal    
DOI: 10.1007/s12551-016-0218-6     Document Type: Review
Times cited : (1288)

References (103)
  • 1
    • 79960550648 scopus 로고    scopus 로고
    • Hydrodynamic properties of wormlike macromolecules: Monte Carlo simulation and global analysis of experimental data
    • COI: 1:CAS:528:DC%2BC3MXnvValsL0%3D
    • Amoros D, Ortega A, de la Torre JG (2011) Hydrodynamic properties of wormlike macromolecules: Monte Carlo simulation and global analysis of experimental data. Macromolecules 44:5788–5797. doi:10.1021/ma102697q
    • (2011) Macromolecules , vol.44 , pp. 5788-5797
    • Amoros, D.1    Ortega, A.2    de la Torre, J.G.3
  • 2
    • 84955511805 scopus 로고    scopus 로고
    • Biophysical Characterization of G-Quadruplex Recognition in the PITX1 mRNA by the Specificity Domain of the Helicase RHAU
    • PID: 26649896
    • Ariyo EO et al (2015) Biophysical Characterization of G-Quadruplex Recognition in the PITX1 mRNA by the Specificity Domain of the Helicase RHAU. PLoS One 10:e0144510. doi:10.1371/journal.pone.0144510
    • (2015) PLoS One , vol.10
    • Ariyo, E.O.1
  • 3
    • 33947566823 scopus 로고
    • Some applications of wave-length turbidimetry in the infrared
    • COI: 1:CAS:528:DyaH38XhtFKrtQ%3D%3D
    • Barnett CE (1942) Some applications of wave-length turbidimetry in the infrared. J Phys Chem 46:69–75. doi:10.1021/j150415a009
    • (1942) J Phys Chem , vol.46 , pp. 69-75
    • Barnett, C.E.1
  • 4
    • 84949292675 scopus 로고    scopus 로고
    • Prediction of solution properties and dynamics of RNAs by means of Brownian dynamics simulation of coarse-grained models: Ribosomal 5S RNA and phenylalanine transfer RNA
    • PID: 26629336
    • Benitez AA, Hernandez Cifre JG, Diaz Banos FG, de la Torre JG (2015). Prediction of solution properties and dynamics of RNAs by means of Brownian dynamics simulation of coarse-grained models: Ribosomal 5S RNA and phenylalanine transfer RNA. BMC Biophys 8:11 doi:10.1186/s13628-015-0025-7
    • (2015) BMC Biophys , vol.8 , pp. 11
    • Benitez, A.A.1    Hernandez Cifre, J.G.2    Diaz Banos, F.G.3    de la Torre, J.G.4
  • 6
    • 0019349226 scopus 로고
    • Quasi-elastic light scattering applications in biochemistry and biology
    • COI: 1:CAS:528:DyaL3MXksFOgsbg%3D, PID: 7020580
    • Bloomfield VA (1981) Quasi-elastic light scattering applications in biochemistry and biology. Annu Rev Biophys Bioeng 10:421–450. doi:10.1146/annurev.bb.10.060181.002225
    • (1981) Annu Rev Biophys Bioeng , vol.10 , pp. 421-450
    • Bloomfield, V.A.1
  • 7
    • 0017911002 scopus 로고
    • Quasi-elastic laser light scattering
    • COI: 1:CAS:528:DyaE1cXktVantrs%3D, PID: 345055
    • Bloomfield VA, Lim TK (1978) Quasi-elastic laser light scattering. Methods Enzymol 48:415–494
    • (1978) Methods Enzymol , vol.48 , pp. 415-494
    • Bloomfield, V.A.1    Lim, T.K.2
  • 8
    • 3042733154 scopus 로고    scopus 로고
    • Inhibition of basement membrane formation by a nidogen-binding laminin gamma1-chain fragment in human skin-organotypic cocultures
    • COI: 1:CAS:528:DC%2BD2cXlsVOjtbk%3D, PID: 15159456
    • Breitkreutz D et al (2004) Inhibition of basement membrane formation by a nidogen-binding laminin gamma1-chain fragment in human skin-organotypic cocultures. J Cell Sci 117:2611–2622. doi:10.1242/jcs.01127
    • (2004) J Cell Sci , vol.117 , pp. 2611-2622
    • Breitkreutz, D.1
  • 9
    • 3743137511 scopus 로고
    • Light diffusion by a homogeneous transparent body
    • Brillouin L (1914) Light diffusion by a homogeneous transparent body. Cr Hebd Acad Sci 158:1331–1334
    • (1914) Cr Hebd Acad Sci , vol.158 , pp. 1331-1334
    • Brillouin, L.1
  • 10
    • 0002049742 scopus 로고
    • Diffusion de la lumière et des rayons X par un corps transparent homogène, influence de l’agitation thermique
    • COI: 1:CAS:528:DyaB38XpvVKl
    • Brillouin L (1922) Diffusion de la lumière et des rayons X par un corps transparent homogène, influence de l’agitation thermique. Annales de Physique (Paris) 17:88–122
    • (1922) Annales de Physique (Paris) , vol.17 , pp. 88-122
    • Brillouin, L.1
  • 11
    • 84896034356 scopus 로고
    • Static and dynamic light scattering from branched polymers and biopolymers
    • Springer, Berlin Heidelberg
    • Burchard W (1983) Static and dynamic light scattering from branched polymers and biopolymers. In: Light scattering from polymers. Springer, Berlin Heidelberg, pp 1–124. doi:10.1007/3-540-12030-0_1
    • (1983) Light scattering from polymers , pp. 1-124
    • Burchard, W.1
  • 12
    • 0002431240 scopus 로고
    • Static and dynamic light scattering approaches to structure determination of biopolymers
    • Harding SE, Settele DB, Bloomfield VA, (eds), Royal Society of Chemistry, Cambridge
    • Burchard W (1992) Static and dynamic light scattering approaches to structure determination of biopolymers. In: Harding SE, Settele DB, Bloomfield VA (eds) Laser light scattering in biochemistry. Royal Society of Chemistry, Cambridge, pp 3–22
    • (1992) Laser light scattering in biochemistry , pp. 3-22
    • Burchard, W.1
  • 13
    • 84948291057 scopus 로고
    • La diffusion moléculaire de la lumière, Vol 16 of Recueil des conférences-rapports de documentation sur la physique
    • Cabannes J, Rocard Y (1929) La diffusion moléculaire de la lumière, Vol 16 of Recueil des conférences-rapports de documentation sur la physique. Les Presses Universitaires de France
    • (1929) Les Presses Universitaires de France
    • Cabannes, J.1    Rocard, Y.2
  • 14
    • 0000952185 scopus 로고
    • Observation of diffusion broadening of Rayleigh scattered light
    • Cummins HZ, Knable N, Yeh Y (1964) Observation of diffusion broadening of Rayleigh scattered light. Phys Rev Lett 12:150–153
    • (1964) Phys Rev Lett , vol.12 , pp. 150-153
    • Cummins, H.Z.1    Knable, N.2    Yeh, Y.3
  • 15
    • 84908087566 scopus 로고
    • Zerstreuung von Röntgenstrahlen
    • Debye P (1915). Zerstreuung von Röntgenstrahlen. Annalen der Physik 351:809–823 doi:10.1002/andp.19153510606
    • (1915) Annalen der Physik , vol.351 , pp. 809-823
    • Debye, P.1
  • 16
    • 84928700934 scopus 로고    scopus 로고
    • Characterization of the termini of the West Nile virus genome and their interactions with the small isoform of the 2′ 5′-oligoadenylate synthetase family
    • COI: 1:CAS:528:DC%2BC2MXms1ais7s%3D, PID: 25871524
    • Deo S et al (2015) Characterization of the termini of the West Nile virus genome and their interactions with the small isoform of the 2′ 5′-oligoadenylate synthetase family. J Struct Biol 190:236–249. doi:10.1016/j.jsb.2015.04.005
    • (2015) J Struct Biol , vol.190 , pp. 236-249
    • Deo, S.1
  • 17
    • 84898609165 scopus 로고    scopus 로고
    • Activation of 2′ 5′-oligoadenylate synthetase by stem loops at the 5′-end of the West Nile virus genome
    • PID: 24651762
    • Deo S et al (2014) Activation of 2′ 5′-oligoadenylate synthetase by stem loops at the 5′-end of the West Nile virus genome. PLoS One 9:e92545. doi:10.1371/journal.pone.0092545
    • (2014) PLoS One , vol.9
    • Deo, S.1
  • 18
    • 84873142658 scopus 로고    scopus 로고
    • Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1
    • COI: 1:CAS:528:DC%2BC3sXislChsro%3D, PID: 23319625
    • Donovan J, Dufner M, Korennykh A (2013) Structural basis for cytosolic double-stranded RNA surveillance by human oligoadenylate synthetase 1. Proc Natl Acad Sci U S A 110:1652–1657. doi:10.1073/pnas.1218528110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 1652-1657
    • Donovan, J.1    Dufner, M.2    Korennykh, A.3
  • 19
    • 84891034536 scopus 로고    scopus 로고
    • Solution conformation of adenovirus virus associated RNA-I and its interaction with PKR
    • COI: 1:CAS:528:DC%2BC3sXitVSht7fO, PID: 24291322
    • Dzananovic E et al (2014) Solution conformation of adenovirus virus associated RNA-I and its interaction with PKR. J Struct Biol 185:48–57. doi:10.1016/j.jsb.2013.11.007
    • (2014) J Struct Biol , vol.185 , pp. 48-57
    • Dzananovic, E.1
  • 20
    • 84874337377 scopus 로고    scopus 로고
    • Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR
    • COI: 1:CAS:528:DC%2BC3sXjt1Wgu7s%3D, PID: 23329698
    • Dzananovic E, Patel TR, Deo S, McEleney K, Stetefeld J, McKenna SA (2013).Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR. RNA 19:333–344 doi:10.1261/rna.035931.112
    • (2013) RNA , vol.19 , pp. 333-344
    • Dzananovic, E.1    Patel, T.R.2    Deo, S.3    McEleney, K.4    Stetefeld, J.5    McKenna, S.A.6
  • 21
    • 84978256394 scopus 로고
    • Über einen die Erzeugung und Verwandlung des Lichtes betreffenden heuristischen Gesichtspunkt
    • Einstein A (1905) Über einen die Erzeugung und Verwandlung des Lichtes betreffenden heuristischen Gesichtspunkt. Annalen Der Physik 322:132–148. doi:10.1002/andp.19053220607
    • (1905) Annalen Der Physik , vol.322 , pp. 132-148
    • Einstein, A.1
  • 22
    • 84976701037 scopus 로고
    • Zur Theorie der Brownschen Bewegung
    • Einstein A (1906). Zur Theorie der Brownschen Bewegung. Annalen Der Physik 324:371–381 doi:10.1002/andp.19063240208
    • (1906) Annalen Der Physik , vol.324 , pp. 371-381
    • Einstein, A.1
  • 23
    • 0001626416 scopus 로고
    • Theory of opalescence of homogenous liquids and liquid mixtures near critical conditions
    • COI: 1:CAS:528:DyaD28XmvFc%3D
    • Einstein A (1910) Theory of opalescence of homogenous liquids and liquid mixtures near critical conditions. Annalen Der Physik 33:1275–1298
    • (1910) Annalen Der Physik , vol.33 , pp. 1275-1298
    • Einstein, A.1
  • 24
    • 0026972625 scopus 로고
    • Data Analysis of Multi-Angle Photon Correlation measurements without and with prior knowledge
    • COI: 1:CAS:528:DyaK3sXksFKqurc%3D
    • Finsy R, Degroen P, Deriemaeker L, Gelade E, Joosten J (1992). Data Analysis of Multi-Angle Photon Correlation measurements without and with prior knowledge. Part Part Syst Char 9:237–251 doi:10.1002/ppsc.19920090133
    • (1992) Part Part Syst Char , vol.9 , pp. 237-251
    • Finsy, R.1    Degroen, P.2    Deriemaeker, L.3    Gelade, E.4    Joosten, J.5
  • 25
    • 0345652175 scopus 로고
    • Singular value analysis and reconstruction of photon correlation data equidistant in time
    • COI: 1:CAS:528:DyaK3cXosV2rsQ%3D%3D
    • Finsy R, Degroen P, Deriemaeker L, Vanlaethem M (1989) Singular value analysis and reconstruction of photon correlation data equidistant in time. J Chem Phys 91:7374–7383. doi:10.1063/1.457260
    • (1989) J Chem Phys , vol.91 , pp. 7374-7383
    • Finsy, R.1    Degroen, P.2    Deriemaeker, L.3    Vanlaethem, M.4
  • 26
    • 0014954128 scopus 로고
    • Determination of diffusion coefficients of haemocyanin at low concentration by intensity fluctuation spectroscopy of scattered laser light
    • COI: 1:CAS:528:DyaE3cXltFOjtrY%3D, PID: 5428189
    • Foord R, Jakeman E, Oliver CJ, Pike ER, Blagrove RJ, Wood E, Peacocke AR (1970) Determination of diffusion coefficients of haemocyanin at low concentration by intensity fluctuation spectroscopy of scattered laser light. Nature 227:242. doi:10.1038/227242a0
    • (1970) Nature , vol.227 , pp. 242
    • Foord, R.1    Jakeman, E.2    Oliver, C.J.3    Pike, E.R.4    Blagrove, R.J.5    Wood, E.6    Peacocke, A.R.7
  • 27
    • 0015452844 scopus 로고
    • Quasi-elastic scattering of laser light. A new tool for the dynamic study of biological macromolecules
    • COI: 1:CAS:528:DyaE3sXhs1Khtr8%3D, PID: 4578839
    • Fujime S (1972) Quasi-elastic scattering of laser light. A new tool for the dynamic study of biological macromolecules. Adv Biophys 3:1–43
    • (1972) Adv Biophys , vol.3 , pp. 1-43
    • Fujime, S.1
  • 28
    • 85000520454 scopus 로고
    • Asymmetry of gas molecules — an article to determine the molecular form
    • COI: 1:CAS:528:DyaB3MXhsVyksg%3D%3D
    • Gans R (1921) Asymmetry of gas molecules — an article to determine the molecular form. Annalen Der Physik 65:97–123
    • (1921) Annalen Der Physik , vol.65 , pp. 97-123
    • Gans, R.1
  • 29
    • 0042473397 scopus 로고
    • The Tyndall effect in liquids
    • COI: 1:CAS:528:DyaB2cXhtlw%3D
    • Gans R (1923) The Tyndall effect in liquids. Z Phys 17:353–397. doi:10.1007/bf01328695
    • (1923) Z Phys , vol.17 , pp. 353-397
    • Gans, R.1
  • 30
    • 33845627785 scopus 로고    scopus 로고
    • Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action
    • COI: 1:CAS:528:DC%2BD2sXmslOisQ%3D%3D, PID: 17158706
    • Garcia MA, Gil J, Ventoso I, Guerra S, Domingo E, Rivas C, Esteban M (2006) Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol Mol Biol Rev 70:1032–1060. doi:10.1128/MMBR.00027-06
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 1032-1060
    • Garcia, M.A.1    Gil, J.2    Ventoso, I.3    Guerra, S.4    Domingo, E.5    Rivas, C.6    Esteban, M.7
  • 31
    • 0025950577 scopus 로고
    • Localization of a major nidogen-binding site to domain III of laminin B2 chain
    • COI: 1:CAS:528:DyaK38XisFSi, PID: 1935973
    • Gerl M, Mann K, Aumailley M, Timpl R (1991) Localization of a major nidogen-binding site to domain III of laminin B2 chain. Eur J Biochem 202:167–174
    • (1991) Eur J Biochem , vol.202 , pp. 167-174
    • Gerl, M.1    Mann, K.2    Aumailley, M.3    Timpl, R.4
  • 32
    • 0010707005 scopus 로고
    • Change of wave-length of light due to elastic heat waves at scattering in liquids
    • Gross E (1930) Change of wave-length of light due to elastic heat waves at scattering in liquids. Nature 126:201–202. doi:10.1038/126201a0
    • (1930) Nature , vol.126 , pp. 201-202
    • Gross, E.1
  • 33
    • 12244312857 scopus 로고    scopus 로고
    • Protein hydrodynamics
    • Allen G, (ed), JAI Press, Greenwich, CT
    • Harding SE (1999) Protein hydrodynamics. In: Allen G (ed) Protein: a comprehensive treatise, vol 2. JAI Press, Greenwich, CT, pp 271–305
    • (1999) Protein: a comprehensive treatise, vol 2 , pp. 271-305
    • Harding, S.E.1
  • 34
    • 77956361888 scopus 로고    scopus 로고
    • Light scattering
    • Coligan JE, Dunn BM, Ploegh HL, Speicher DW, Wingfield PT, (eds), John Wiley & Sons, Inc., New York
    • Harding SE, Jumel K (1998) Light scattering. In: Coligan JE, Dunn BM, Ploegh HL, Speicher DW, Wingfield PT (eds) Current protocols in protein science. John Wiley & Sons, Inc., New York. 10.1002/0471140864.ps0708s11
    • (1998) Current protocols in protein science
    • Harding, S.E.1    Jumel, K.2
  • 35
    • 0015810530 scopus 로고
    • Diffusion coefficients and hydrodynamic radii of three spherical RNA viruses by laser light scattering
    • COI: 1:STN:280:DyaE2c%2FhtFKntg%3D%3D, PID: 4355532
    • Harvey JD (1973) Diffusion coefficients and hydrodynamic radii of three spherical RNA viruses by laser light scattering. Virology 56:365–368. doi:10.1016/0042-6822(73)90313-9
    • (1973) Virology , vol.56 , pp. 365-368
    • Harvey, J.D.1
  • 36
    • 33745822430 scopus 로고    scopus 로고
    • Modification to the cumulant analysis of polydispersity in quasielastic light scattering data
    • COI: 1:CAS:528:DC%2BD28XmvFKmsbY%3D
    • Hassan PA, Kulshreshtha SK (2006) Modification to the cumulant analysis of polydispersity in quasielastic light scattering data. J Colloid Interf Sci 300:744–748. doi:10.1016/j.jcis.2006.04.013
    • (2006) J Colloid Interf Sci , vol.300 , pp. 744-748
    • Hassan, P.A.1    Kulshreshtha, S.K.2
  • 37
    • 33646026385 scopus 로고    scopus 로고
    • Alpha3Na+/K+−ATPase is a neuronal receptor for agrin
    • COI: 1:CAS:528:DC%2BD28Xkt1Oqur0%3D, PID: 16630822
    • Hilgenberg LG, Su H, Gu H, O’Dowd DK, Smith MA (2006) Alpha3Na+/K+−ATPase is a neuronal receptor for agrin. Cell 125:359–369. doi:10.1016/j.cell.2006.01.052
    • (2006) Cell , vol.125 , pp. 359-369
    • Hilgenberg, L.G.1    Su, H.2    Gu, H.3    O’Dowd, D.K.4    Smith, M.A.5
  • 38
    • 0037780911 scopus 로고    scopus 로고
    • The COOH-terminal domain of agrin signals via a synaptic receptor in central nervous system neurons
    • COI: 1:CAS:528:DC%2BD3sXks1Glsro%3D, PID: 12796478
    • Hoover CL, Hilgenberg LG, Smith MA (2003) The COOH-terminal domain of agrin signals via a synaptic receptor in central nervous system neurons. J Cell Biol 161:923–932. doi:10.1083/jcb.200301013
    • (2003) J Cell Biol , vol.161 , pp. 923-932
    • Hoover, C.L.1    Hilgenberg, L.G.2    Smith, M.A.3
  • 39
    • 34347206680 scopus 로고    scopus 로고
    • The human 2′-5′oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation
    • COI: 1:CAS:528:DC%2BD2sXnsFKrtbk%3D, PID: 17408844
    • Hovanessian AG, Justesen J (2007) The human 2′-5′oligoadenylate synthetase family: unique interferon-inducible enzymes catalyzing 2′-5′ instead of 3′-5′ phosphodiester bond formation. Biochimie 89:779–788. doi:10.1016/j.biochi.2007.02.003
    • (2007) Biochimie , vol.89 , pp. 779-788
    • Hovanessian, A.G.1    Justesen, J.2
  • 40
    • 0028277497 scopus 로고
    • The binding of fibronectin to entactin is mediated through the 29 kDa amino terminal fragment of fibronectin and the G2 domain of entactin
    • COI: 1:CAS:528:DyaK2cXksFamt70%3D, PID: 8147897
    • Hsieh JC, Wu C, Chung AE (1994) The binding of fibronectin to entactin is mediated through the 29 kDa amino terminal fragment of fibronectin and the G2 domain of entactin. Biochem Biophys Res Commun 199:1509–1517. doi:10.1006/bbrc.1994.1402
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 1509-1517
    • Hsieh, J.C.1    Wu, C.2    Chung, A.E.3
  • 41
    • 85000656068 scopus 로고    scopus 로고
    • ISO (2008) Particle size analysis — dynamic light scattering (DLS), 22412 International Standards Organization. - iso:std:iso:22412:en. Accessed July 2016
    • ISO (2008) Particle size analysis — dynamic light scattering (DLS), 22412 International Standards Organization. https://www.iso.org/obp/ui/ - iso:std:iso:22412:en. Accessed July 2016
  • 42
    • 0042452653 scopus 로고
    • Spectrum of clipped photon-counting fluctuations of gaussian light
    • Jakeman E, Pike ER (1969) Spectrum of clipped photon-counting fluctuations of gaussian light. J Phys Part Gen 2:411. doi:10.1088/0305-4470/2/3/021
    • (1969) J Phys Part Gen , vol.2 , pp. 411
    • Jakeman, E.1    Pike, E.R.2
  • 43
    • 0015519839 scopus 로고
    • Studies of elastin coacervation by quasielastic light scattering
    • COI: 1:CAS:528:DyaE38XksFOrurg%3D, PID: 5064583
    • Jamieson AM, Downs CE, Walton AG (1972) Studies of elastin coacervation by quasielastic light scattering. Biochim Biophys Acta 271:34–47. doi:10.1016/0005-2795(72)90130-4
    • (1972) Biochim Biophys Acta , vol.271 , pp. 34-47
    • Jamieson, A.M.1    Downs, C.E.2    Walton, A.G.3
  • 44
    • 0035369125 scopus 로고    scopus 로고
    • Physiological regulation of the immunological synapse by agrin
    • COI: 1:CAS:528:DC%2BD3MXkt1Smurg%3D, PID: 11349136
    • Khan AA, Bose C, Yam LS, Soloski MJ, Rupp F (2001) Physiological regulation of the immunological synapse by agrin. Science 292:1681–1686. doi:10.1126/science.1056594
    • (2001) Science , vol.292 , pp. 1681-1686
    • Khan, A.A.1    Bose, C.2    Yam, L.S.3    Soloski, M.J.4    Rupp, F.5
  • 45
    • 33846446409 scopus 로고    scopus 로고
    • Rapid purification of RNAs using fast performance liquid chromatography (FPLC)
    • COI: 1:CAS:528:DC%2BD2sXksVKms7o%3D, PID: 17179067
    • Kim I, McKenna SA, Viani Puglisi E, Puglisi JD (2007) Rapid purification of RNAs using fast performance liquid chromatography (FPLC). RNA 13:289–294. doi:10.1261/rna.342607
    • (2007) RNA , vol.13 , pp. 289-294
    • Kim, I.1    McKenna, S.A.2    Viani Puglisi, E.3    Puglisi, J.D.4
  • 46
    • 36849103950 scopus 로고
    • Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants
    • COI: 1:CAS:528:DyaE3sXitFyqtQ%3D%3D
    • Koppel DE (1972) Analysis of macromolecular polydispersity in intensity correlation spectroscopy: the method of cumulants. J Chem Phys 57:4814. doi:10.1063/1.1678153
    • (1972) J Chem Phys , vol.57 , pp. 4814
    • Koppel, D.E.1
  • 47
    • 85047699539 scopus 로고    scopus 로고
    • Laminin gamma 1 chain peptide, C-16 (KAFDITYVRLKF), promotes migration, MMP-9 secretion, and pulmonary metastasis of B16-F10 mouse melanoma cells
    • COI: 1:CAS:528:DC%2BD38XjvFGisLk%3D, PID: 11953867
    • Kuratomi Y, Nomizu M, Tanaka K, Ponce ML, Komiyama S, Kleinman HK, Yamada Y (2002) Laminin gamma 1 chain peptide, C-16 (KAFDITYVRLKF), promotes migration, MMP-9 secretion, and pulmonary metastasis of B16-F10 mouse melanoma cells. Br J Cancer 86:1169–1173. doi:10.1038/sj.bjc.6600187
    • (2002) Br J Cancer , vol.86 , pp. 1169-1173
    • Kuratomi, Y.1    Nomizu, M.2    Tanaka, K.3    Ponce, M.L.4    Komiyama, S.5    Kleinman, H.K.6    Yamada, Y.7
  • 48
    • 0000726453 scopus 로고
    • Struktur der unverschobenen Streulinie
    • COI: 1:CAS:528:DyaA2cXislygtg%3D%3D
    • Landau LD, Placzek G (1934).Struktur der unverschobenen Streulinie. Z Phys Sowjetunion 5:172–173
    • (1934) Z Phys Sowjetunion , vol.5 , pp. 172-173
    • Landau, L.D.1    Placzek, G.2
  • 49
    • 0001002661 scopus 로고
    • Maximum entropy analysis of quasielastic light scattering from colloidal dispersions
    • COI: 1:CAS:528:DyaL28XhvFGkurw%3D
    • Livesey AK, Licinio P, Delaye M (1986) Maximum entropy analysis of quasielastic light scattering from colloidal dispersions. J Chem Phys 84:5102–5107. doi:10.1063/1.450663
    • (1986) J Chem Phys , vol.84 , pp. 5102-5107
    • Livesey, A.K.1    Licinio, P.2    Delaye, M.3
  • 50
    • 84869789038 scopus 로고    scopus 로고
    • Protein analysis by dynamic light scattering: methods and techniques for students
    • COI: 1:CAS:528:DC%2BC38XhsVyktrnI, PID: 23166025
    • Lorber B, Fischer F, Bailly M, Roy H, Kern D (2012) Protein analysis by dynamic light scattering: methods and techniques for students. Biochem Mol Biol Educ 40:372–382. doi:10.1002/bmb.20644
    • (2012) Biochem Mol Biol Educ , vol.40 , pp. 372-382
    • Lorber, B.1    Fischer, F.2    Bailly, M.3    Roy, H.4    Kern, D.5
  • 51
    • 85000620240 scopus 로고    scopus 로고
    • Malvern Instruments (2014) TN101104 Intensity Volume Number. Malvern Instruments Limited. Accessed July 2016
    • Malvern Instruments (2014) TN101104 Intensity Volume Number. Malvern Instruments Limited. http://www.malvern.com/en/pdf/secure/TN101104IntensityVolumeNumber.pdf. Accessed July 2016
  • 52
    • 0037415723 scopus 로고    scopus 로고
    • Mapping of the laminin-binding site of the N-terminal agrin domain (NtA)
    • COI: 1:CAS:528:DC%2BD3sXitlKksrk%3D, PID: 12554653
    • Mascarenhas JB, Ruegg MA, Winzen U, Halfter W, Engel J, Stetefeld J (2003) Mapping of the laminin-binding site of the N-terminal agrin domain (NtA). EMBO J 22:529–536. doi:10.1093/emboj/cdg041
    • (2003) EMBO J , vol.22 , pp. 529-536
    • Mascarenhas, J.B.1    Ruegg, M.A.2    Winzen, U.3    Halfter, W.4    Engel, J.5    Stetefeld, J.6
  • 53
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • COI: 1:CAS:528:DyaK3sXksVeltLk%3D, PID: 8491180
    • Mayer U et al (1993) A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J 12:1879–1885
    • (1993) EMBO J , vol.12 , pp. 1879-1885
    • Mayer, U.1
  • 54
    • 38449103279 scopus 로고    scopus 로고
    • Biophysical and biochemical investigations of dsRNA-activated kinase PKR
    • COI: 1:CAS:528:DC%2BD1cXhsVeqtbY%3D, PID: 17913645
    • McKenna SA, Lindhout DA, Shimoike T, Puglisi JD (2007) Biophysical and biochemical investigations of dsRNA-activated kinase PKR. Methods Enzymol 430:373–396. doi:10.1016/S0076-6879(07)30014-1
    • (2007) Methods Enzymol , vol.430 , pp. 373-396
    • McKenna, S.A.1    Lindhout, D.A.2    Shimoike, T.3    Puglisi, J.D.4
  • 55
    • 84890288582 scopus 로고    scopus 로고
    • Binding of G-quadruplexes to the N-terminal recognition domain of the RNA helicase associated with AU-rich element (RHAU)
    • COI: 1:CAS:528:DC%2BC3sXhvFWktbfO, PID: 24151078
    • Meier M et al (2013) Binding of G-quadruplexes to the N-terminal recognition domain of the RNA helicase associated with AU-rich element (RHAU). J Biol Chem 288:35014–35027. doi:10.1074/jbc.M113.512970
    • (2013) J Biol Chem , vol.288 , pp. 35014-35027
    • Meier, M.1
  • 56
    • 84865675957 scopus 로고    scopus 로고
    • Regulation of the interferon-inducible 2′-5′-oligoadenylate synthetases by adenovirus VA(I) RNA
    • COI: 1:CAS:528:DC%2BC38XpvVOrtb8%3D, PID: 22709583
    • Meng H, Deo S, Xiong S, Dzananovic E, Donald LJ, van Dijk CW, McKenna SA (2012) Regulation of the interferon-inducible 2′-5′-oligoadenylate synthetases by adenovirus VA(I) RNA. J Mol Biol 422:635–649. doi:10.1016/j.jmb.2012.06.017
    • (2012) J Mol Biol , vol.422 , pp. 635-649
    • Meng, H.1    Deo, S.2    Xiong, S.3    Dzananovic, E.4    Donald, L.J.5    van Dijk, C.W.6    McKenna, S.A.7
  • 57
    • 84974687151 scopus 로고
    • Beiträge zur Optik trüber Medien, speziell kolloidaler Metallösungen
    • Mie G (1908) Beiträge zur Optik trüber Medien, speziell kolloidaler Metallösungen. Ann Phys 330:377–445. doi:10.1002/andp.19083300302
    • (1908) Ann Phys , vol.330 , pp. 377-445
    • Mie, G.1
  • 58
    • 0022092648 scopus 로고
    • Improved techniques for particle size determination by quasi-elastic light scattering
    • COI: 1:CAS:528:DyaL2MXksVehtr8%3D
    • Morrison ID, Grabowski EF, Herb CA (1985). Improved techniques for particle size determination by quasi-elastic light scattering. Langmuir 1:496–501 doi:10.1021/la00064a016
    • (1985) Langmuir , vol.1 , pp. 496-501
    • Morrison, I.D.1    Grabowski, E.F.2    Herb, C.A.3
  • 59
    • 0019754573 scopus 로고
    • Quasi-elastic light scattering of Artemia ribosomes sedimented in a CsCl density gradient
    • COI: 1:CAS:528:DyaL38Xhtl2hs7k%3D, PID: 7334175
    • Nieuwenhuysen P, Clauwaert J (1981) Quasi-elastic light scattering of Artemia ribosomes sedimented in a CsCl density gradient. J Biochem Biophys Methods 5:279–286
    • (1981) J Biochem Biophys Methods , vol.5 , pp. 279-286
    • Nieuwenhuysen, P.1    Clauwaert, J.2
  • 60
    • 0023461553 scopus 로고
    • Identification of agrin, a synaptic organizing protein from Torpedo electric organ
    • COI: 1:CAS:528:DyaL1cXhtVygt7g%3D, PID: 2826489
    • Nitkin RM, Smith MA, Magill C, Fallon JR, Yao YM, Wallace BG, McMahan UJ (1987) Identification of agrin, a synaptic organizing protein from Torpedo electric organ. J Cell Biol 105:2471–2478
    • (1987) J Cell Biol , vol.105 , pp. 2471-2478
    • Nitkin, R.M.1    Smith, M.A.2    Magill, C.3    Fallon, J.R.4    Yao, Y.M.5    Wallace, B.G.6    McMahan, U.J.7
  • 61
    • 35648978159 scopus 로고    scopus 로고
    • Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies
    • COI: 1:CAS:528:DC%2BD2sXhtlKiurjI, PID: 18059629
    • Nobbmann U et al (2007) Dynamic light scattering as a relative tool for assessing the molecular integrity and stability of monoclonal antibodies. Biotechnol Genet Eng Rev 24:117–128. doi:10.1080/02648725.2007.10648095
    • (2007) Biotechnol Genet Eng Rev , vol.24 , pp. 117-128
    • Nobbmann, U.1
  • 62
    • 0024749520 scopus 로고
    • Maximum-entropy analysis of photon correlation spectroscopy data
    • COI: 1:CAS:528:DyaL1MXlslGjtLg%3D
    • Nyeo SL, Chu B (1989). Maximum-entropy analysis of photon correlation spectroscopy data. Macromolecules 22:3998–4009 doi:10.1021/ma00200a031
    • (1989) Macromolecules , vol.22 , pp. 3998-4009
    • Nyeo, S.L.1    Chu, B.2
  • 63
    • 79955573066 scopus 로고    scopus 로고
    • Global fit and structure optimization of flexible and rigid macromolecules and nanoparticles from analytical ultracentrifugation and other dilute solution properties
    • COI: 1:CAS:528:DC%2BC3MXlvVChtrk%3D, PID: 21163355
    • Ortega A, Amoros D, Garcia de la Torre J (2011). Global fit and structure optimization of flexible and rigid macromolecules and nanoparticles from analytical ultracentrifugation and other dilute solution properties. Methods 54:115–123. doi:10.1016/j.ymeth.2010.12.004
    • (2011) Methods , vol.54 , pp. 115-123
    • Ortega, A.1    Amoros, D.2    Garcia de la Torre, J.3
  • 64
    • 80052470762 scopus 로고    scopus 로고
    • Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models
    • COI: 1:CAS:528:DC%2BC3MXhtVajtLbE, PID: 21843480
    • Ortega A, Amoros D, Garcia de la Torre J (2011a) Prediction of hydrodynamic and other solution properties of rigid proteins from atomic- and residue-level models. Biophys J 101:892–898. doi:10.1016/j.bpj.2011.06.046
    • (2011) Biophys J , vol.101 , pp. 892-898
    • Ortega, A.1    Amoros, D.2    Garcia de la Torre, J.3
  • 65
    • 34548224816 scopus 로고    scopus 로고
    • Equivalent radii and ratios of radii from solution properties as indicators of macromolecular conformation, shape, and flexibility
    • COI: 1:CAS:528:DC%2BD2sXotVKhsLc%3D, PID: 17645309
    • Ortega A, Garcia de la Torre J (2007) Equivalent radii and ratios of radii from solution properties as indicators of macromolecular conformation, shape, and flexibility. Biomacromolecules 8:2464–2475. doi:10.1021/bm700473f
    • (2007) Biomacromolecules , vol.8 , pp. 2464-2475
    • Ortega, A.1    Garcia de la Torre, J.2
  • 66
    • 58249134654 scopus 로고
    • Exponential sampling method for light scattering polydispersity analysis
    • Ostrowsky N, Sornette D, Parker P, Pike ER (1981) Exponential sampling method for light scattering polydispersity analysis. Opt Acta 28:1059–1070
    • (1981) Opt Acta , vol.28 , pp. 1059-1070
    • Ostrowsky, N.1    Sornette, D.2    Parker, P.3    Pike, E.R.4
  • 67
    • 84894273331 scopus 로고    scopus 로고
    • Structural elucidation of full-length nidogen and the laminin–nidogen complex in solution
    • COI: 1:CAS:528:DC%2BC3sXhtlKqs77I, PID: 23948589
    • Patel TR, Bernards C, Meier M, McEleney K, Winzor DJ, Koch M, Stetefeld J (2014) Structural elucidation of full-length nidogen and the laminin–nidogen complex in solution. Matrix Biol 33:60–67. doi:10.1016/j.matbio.2013.07.009
    • (2014) Matrix Biol , vol.33 , pp. 60-67
    • Patel, T.R.1    Bernards, C.2    Meier, M.3    McEleney, K.4    Winzor, D.J.5    Koch, M.6    Stetefeld, J.7
  • 68
    • 79956200486 scopus 로고    scopus 로고
    • T-shaped arrangement of the recombinant agrin G3-IgG Fc protein
    • COI: 1:CAS:528:DC%2BC3MXmtFSnurk%3D, PID: 21448912
    • Patel TR, Meier M, Li J, Morris G, Rowe AJ, Stetefeld J (2011) T-shaped arrangement of the recombinant agrin G3-IgG Fc protein. Protein Sci 20:931–940. doi:10.1002/pro.628
    • (2011) Protein Sci , vol.20 , pp. 931-940
    • Patel, T.R.1    Meier, M.2    Li, J.3    Morris, G.4    Rowe, A.J.5    Stetefeld, J.6
  • 69
    • 77957754110 scopus 로고    scopus 로고
    • Nano-structure of the laminin gamma-1 short arm reveals an extended and curved multidomain assembly
    • COI: 1:CAS:528:DC%2BC3cXht1Oms7rP, PID: 20688161
    • Patel TR et al (2010) Nano-structure of the laminin gamma-1 short arm reveals an extended and curved multidomain assembly. Matrix Biol 29:565–572. doi:10.1016/j.matbio.2010.07.004
    • (2010) Matrix Biol , vol.29 , pp. 565-572
    • Patel, T.R.1
  • 70
    • 84857029766 scopus 로고    scopus 로고
    • Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements
    • COI: 1:CAS:528:DC%2BC38XjtVyhtbk%3D, PID: 22210009
    • Patel TR, Reuten R, Xiong S, Meier M, Winzor DJ, Koch M, Stetefeld J (2012) Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements. Matrix Biol 31:135–140. doi:10.1016/j.matbio.2011.11.004
    • (2012) Matrix Biol , vol.31 , pp. 135-140
    • Patel, T.R.1    Reuten, R.2    Xiong, S.3    Meier, M.4    Winzor, D.J.5    Koch, M.6    Stetefeld, J.7
  • 71
    • 0000471758 scopus 로고
    • Doppler shifts in light scattering from pure liquids and polymer solutions
    • COI: 1:CAS:528:DyaF2cXls1emug%3D%3D
    • Pecora R (1964) Doppler shifts in light scattering from pure liquids and polymer solutions. J Chem Phys 40:1604. doi:10.1063/1.1725368
    • (1964) J Chem Phys , vol.40 , pp. 1604
    • Pecora, R.1
  • 72
    • 0015457756 scopus 로고
    • Quasi-elastic light scattering from macromolecules
    • COI: 1:CAS:528:DyaE3sXhtVKn, PID: 4567754
    • Pecora R (1972) Quasi-elastic light scattering from macromolecules. Annu Rev Biophys Bioeng 1:257–276. doi:10.1146/annurev.bb.01.060172.001353
    • (1972) Annu Rev Biophys Bioeng , vol.1 , pp. 257-276
    • Pecora, R.1
  • 73
    • 85038184664 scopus 로고
    • The accuracy of diffusion-constant measurements by digital autocorrelation of photon-counting fluctuations
    • Pike ER (1972) The accuracy of diffusion-constant measurements by digital autocorrelation of photon-counting fluctuations. Journal de Physique Colloques 33:C1-177–C171-180. doi:10.1051/jphyscol:1972132
    • (1972) Journal de Physique Colloques , vol.33 , pp. C1-177-C171-180
    • Pike, E.R.1
  • 74
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher SW (1982a) A constrained regularization method for inverting data represented by linear algebraic or integral equations. Comput Phys Commun 27:213–227. doi:10.1016/0010-4655(82)90173-4
    • (1982) Comput Phys Commun , vol.27 , pp. 213-227
    • Provencher, S.W.1
  • 75
    • 0020176708 scopus 로고
    • CONTIN: A general purpose constrained regularization programm for inverting noisy linear algebraic and integral equations
    • Provencher SW (1982b) CONTIN: A general purpose constrained regularization programm for inverting noisy linear algebraic and integral equations. Comput Phys Commun 27:229–242. doi:10.1016/0010-4655(82)90174-6
    • (1982) Comput Phys Commun , vol.27 , pp. 229-242
    • Provencher, S.W.1
  • 76
    • 0002005096 scopus 로고    scopus 로고
    • Global analysis of dynamic light scattering autocorrelation functions
    • COI: 1:CAS:528:DyaK2sXjs1ansg%3D%3D
    • Provencher SW, Stepanek P (1996) Global analysis of dynamic light scattering autocorrelation functions. Part Part Syst Char 13:291–294. doi:10.1002/ppsc.19960130507
    • (1996) Part Part Syst Char , vol.13 , pp. 291-294
    • Provencher, S.W.1    Stepanek, P.2
  • 77
    • 0003013271 scopus 로고
    • Correlation and light beating spectroscopy
    • Cummings HZ, Pike ER, (eds), Plenum, New York
    • Pusey PN (1972) Correlation and light beating spectroscopy. In: Cummings HZ, Pike ER (eds) Photon correlation and light beating spectroscopy, Plenum, New York, pp 387–428
    • (1972) Photon correlation and light beating spectroscopy , pp. 387-428
    • Pusey, P.N.1
  • 78
    • 84858074561 scopus 로고    scopus 로고
    • LAMC1 gene is associated with premature ovarian failure
    • COI: 1:CAS:528:DC%2BC38Xjt1ajur0%3D, PID: 22321639
    • Pyun JA, Cha DH, Kwack K (2012) LAMC1 gene is associated with premature ovarian failure. Maturitas 71:402–406. doi:10.1016/j.maturitas.2012.01.011
    • (2012) Maturitas , vol.71 , pp. 402-406
    • Pyun, J.A.1    Cha, D.H.2    Kwack, K.3
  • 80
    • 0014711311 scopus 로고
    • Quasi-elastic light scattering by diffusional fluctuations in RNase solutions
    • COI: 1:CAS:528:DyaE3cXnsFShtw%3D%3D, PID: 5409774
    • Rimai L, Hichmott JT Jr, Carew EB, Cole T (1970) Quasi-elastic light scattering by diffusional fluctuations in RNase solutions. Biophys J 10:20–37. doi:10.1016/S0006-3495(70)86283-X
    • (1970) Biophys J , vol.10 , pp. 20-37
    • Rimai, L.1    Hichmott, J.T.2    Carew, E.B.3    Cole, T.4
  • 81
    • 0029584361 scopus 로고
    • Binding of mouse and human fibulin-2 to extracellular matrix ligands
    • COI: 1:CAS:528:DyaK28XhtV2isQ%3D%3D, PID: 7500359
    • Sasaki T, Gohring W, Pan TC, Chu ML, Timpl R (1995a) Binding of mouse and human fibulin-2 to extracellular matrix ligands. J Mol Biol 254:892–899. doi:10.1006/jmbi.1995.0664
    • (1995) J Mol Biol , vol.254 , pp. 892-899
    • Sasaki, T.1    Gohring, W.2    Pan, T.C.3    Chu, M.L.4    Timpl, R.5
  • 82
    • 0028815977 scopus 로고
    • Structural characterization of two variants of fibulin-1 that differ in nidogen affinity
    • COI: 1:CAS:528:DyaK2MXjtFGjs7k%3D, PID: 7844816
    • Sasaki T, Kostka G, Gohring W, Wiedemann H, Mann K, Chu ML, Timpl R (1995b) Structural characterization of two variants of fibulin-1 that differ in nidogen affinity. J Mol Biol 245:241–250
    • (1995) J Mol Biol , vol.245 , pp. 241-250
    • Sasaki, T.1    Kostka, G.2    Gohring, W.3    Wiedemann, H.4    Mann, K.5    Chu, M.L.6    Timpl, R.7
  • 83
    • 34548205414 scopus 로고    scopus 로고
    • Binding of netrin-4 to laminin short arms regulates basement membrane assembly
    • COI: 1:CAS:528:DC%2BD2sXoslOnsbk%3D, PID: 17588941
    • Schneiders FI et al (2007) Binding of netrin-4 to laminin short arms regulates basement membrane assembly. J Biol Chem 282:23750–23758. doi:10.1074/jbc.M703137200
    • (2007) J Biol Chem , vol.282 , pp. 23750-23758
    • Schneiders, F.I.1
  • 84
    • 0017555826 scopus 로고
    • Dynamic light scattering of biopolymers and biocolloids
    • COI: 1:CAS:528:DyaE1cXlt1Ggur4%3D, PID: 336278
    • Schurr JM (1977) Dynamic light scattering of biopolymers and biocolloids. CRC Crit Rev Biochem 4:371–431. doi:10.3109/10409237709105461
    • (1977) CRC Crit Rev Biochem , vol.4 , pp. 371-431
    • Schurr, J.M.1
  • 85
    • 80052526015 scopus 로고    scopus 로고
    • Examination of the discrepancy between size estimates for ovalbumin from small-angle X-ray scattering and other physicochemical measurements
    • COI: 1:CAS:528:DC%2BC3MXhtVGnurfI, PID: 21793570
    • Scott DJ, Patel TR, Besong DMT, Stetefeld J, Winzor DJ (2011) Examination of the discrepancy between size estimates for ovalbumin from small-angle X-ray scattering and other physicochemical measurements. J Phys Chem B 115:10725–10729. doi:10.1021/jp2006149
    • (2011) J Phys Chem B , vol.115 , pp. 10725-10729
    • Scott, D.J.1    Patel, T.R.2    Besong, D.M.T.3    Stetefeld, J.4    Winzor, D.J.5
  • 88
    • 12144289844 scopus 로고    scopus 로고
    • Modulation of agrin function by alternative splicing and Ca2+ binding
    • COI: 1:CAS:528:DC%2BD2cXitFKksrw%3D, PID: 15016366
    • Stetefeld J et al (2004) Modulation of agrin function by alternative splicing and Ca2+ binding. Structure 12:503–515. doi:10.1016/j.str.2004.02.001
    • (2004) Structure , vol.12 , pp. 503-515
    • Stetefeld, J.1
  • 89
    • 0034889777 scopus 로고    scopus 로고
    • The laminin-binding domain of agrin is structurally related to N-TIMP-1
    • COI: 1:CAS:528:DC%2BD3MXls1Oms7k%3D, PID: 11473262
    • Stetefeld J et al (2001) The laminin-binding domain of agrin is structurally related to N-TIMP-1. Nat Struct Biol 8:705–709. doi:10.1038/90422
    • (2001) Nat Struct Biol , vol.8 , pp. 705-709
    • Stetefeld, J.1
  • 90
    • 0000119455 scopus 로고
    • On the theories of internal friction of fluids in motion
    • Stokes GG (1845) On the theories of internal friction of fluids in motion. Trans Cam Philos Soc 8:287–305
    • (1845) Trans Cam Philos Soc , vol.8 , pp. 287-305
    • Stokes, G.G.1
  • 91
    • 0000792455 scopus 로고
    • LVIII. On the scattering of light by small particles
    • Strutt JW (1871a) LVIII. On the scattering of light by small particles. Philos Mag Ser 4(41):447–454. doi:10.1080/14786447108640507
    • (1871) Philos Mag Ser , vol.4 , Issue.41 , pp. 447-454
    • Strutt, J.W.1
  • 92
    • 0001123918 scopus 로고
    • XXXVI. On the light from the sky, its polarization and colour
    • Strutt JW (1871b) XXXVI. On the light from the sky, its polarization and colour. Philos Mag Ser 4(41):274–279. doi:10.1080/14786447108640479
    • (1871) Philos Mag Ser , vol.4 , Issue.41 , pp. 274-279
    • Strutt, J.W.1
  • 93
    • 0001472707 scopus 로고
    • LXXV. A dynamical theory of diffusion for non-electrolytes and the molecular mass of albumin
    • Sutherland W (1905) LXXV. A dynamical theory of diffusion for non-electrolytes and the molecular mass of albumin. Philos Mag Ser 6(9):781–785. doi:10.1080/14786440509463331
    • (1905) Philos Mag Ser , vol.6 , Issue.9 , pp. 781-785
    • Sutherland, W.1
  • 96
    • 0006792334 scopus 로고
    • On the Blue Colour of the Sky, the Polarization of Skylight, and on the Polarization of Light by Cloudy Matter Generally
    • Tyndall J (1868). On the Blue Colour of the Sky, the Polarization of Skylight, and on the Polarization of Light by Cloudy Matter Generally. Proceedings of the Royal Society of London 17:223–233 doi:10.1098/rspl.1868.0033
    • (1868) Proceedings of the Royal Society of London , vol.17 , pp. 223-233
    • Tyndall, J.1
  • 97
    • 84974626611 scopus 로고
    • Molekular-kinetische Theorie der Opaleszenz von Gasen im kritischen Zustande, sowie einiger verwandter Erscheinungen
    • v. Smoluchowski M (1908).Molekular-kinetische Theorie der Opaleszenz von Gasen im kritischen Zustande, sowie einiger verwandter Erscheinungen. Annalen der Physik 330:205–226 doi:10.1002/andp.19083300203
    • (1908) Annalen der Physik , vol.330 , pp. 205-226
    • v. Smoluchowski, M.1
  • 98
    • 84921883395 scopus 로고    scopus 로고
    • The beta-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide
    • COI: 1:CAS:528:DC%2BC2MXhvVers7Y%3D, PID: 25480792
    • Vadlamani G et al (2015) The beta-lactamase gene regulator AmpR is a tetramer that recognizes and binds the D-Ala-D-Ala motif of its repressor UDP-N-acetylmuramic acid (MurNAc)-pentapeptide. J Biol Chem 290:2630–2643. doi:10.1074/jbc.M114.618199
    • (2015) J Biol Chem , vol.290 , pp. 2630-2643
    • Vadlamani, G.1
  • 99
    • 0014895122 scopus 로고
    • Physical characterization of the protein molecule
    • PID: 4950193
    • Van Holde KE (1970) Physical characterization of the protein molecule. Mol Biol Biochem Biophys 8:2–24
    • (1970) Mol Biol Biochem Biophys , vol.8 , pp. 2-24
    • Van Holde, K.E.1
  • 100
    • 0027498262 scopus 로고
    • Light scattering and the absolute characterization of macromolecules
    • COI: 1:CAS:528:DyaK3sXotFKrtg%3D%3D
    • Wyatt PJ (1993) Light scattering and the absolute characterization of macromolecules. Anal Chim Acta 272:1–40. doi:10.1016/0003-2670(93)80373-S
    • (1993) Anal Chim Acta , vol.272 , pp. 1-40
    • Wyatt, P.J.1
  • 102
    • 19944425601 scopus 로고
    • Molecular theory of the scattering of light in fluids
    • COI: 1:CAS:528:DyaH2MXhsFOmuw%3D%3D
    • Zimm BH (1945) Molecular theory of the scattering of light in fluids. J Chem Phys 13:141–145. doi:10.1063/1.1724013
    • (1945) J Chem Phys , vol.13 , pp. 141-145
    • Zimm, B.H.1
  • 103
    • 0042849714 scopus 로고
    • Apparatus and methods for measurement and interpretation of the angular variation of light scattering; preliminary results on polystyrene solutions
    • COI: 1:CAS:528:DyaH1MXnslWk
    • Zimm BH (1948) Apparatus and methods for measurement and interpretation of the angular variation of light scattering; preliminary results on polystyrene solutions. J Chem Phys 16:1099–1116. doi:10.1063/1.1746740
    • (1948) J Chem Phys , vol.16 , pp. 1099-1116
    • Zimm, B.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.