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Volumn 6, Issue , 2015, Pages

Biomimetic mineralization of metal-organic frameworks as protective coatings for biomacromolecules

Author keywords

[No Author keywords available]

Indexed keywords

2 METHYLIMIDAZOLE; BOVINE SERUM ALBUMIN; DNA; ENZYME; HORSERADISH PEROXIDASE; IMIDAZOLE DERIVATIVE; METAL ORGANIC FRAMEWORK; N,N DIMETHYLFORMAMIDE; PROTECTIVE AGENT; PROTEIN; UNCLASSIFIED DRUG; UREASE; ZEOLITIC IMIDAZOLATE FRAMEWORK 8; ZINC ION; 2-METHYLIMIDAZOLE; BIOMIMETIC MATERIAL; ORGANOMETALLIC COMPOUND; ZINC;

EID: 84930637209     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms8240     Document Type: Article
Times cited : (1145)

References (60)
  • 1
    • 57349141462 scopus 로고    scopus 로고
    • Introduction biomineralization
    • Estroff L. A. Introduction: biomineralization. Chem. Rev. 108, 4329-4331 (2008
    • (2008) Chem. Rev , vol.108 , pp. 4329-4331
    • Estroff, L.A.1
  • 2
    • 57349119498 scopus 로고    scopus 로고
    • Controlling mineral morphologies and structures in biological and synthetic systems
    • Meldrum F. C. & Cölfen H. Controlling mineral morphologies and structures in biological and synthetic systems. Chem. Rev. 108, 4332-4432 (2008
    • (2008) Chem. Rev , vol.108 , pp. 4332-4432
    • Meldrum, F.C.1    Cölfen, H.2
  • 3
    • 84874970384 scopus 로고    scopus 로고
    • Flexible minerals: Self-assembled calcite spicules with extreme bending strength
    • Natalio F., et al. Flexible minerals: self-assembled calcite spicules with extreme bending strength. Science 339, 1298-1302 (2013
    • (2013) Science , vol.339 , pp. 1298-1302
    • Natalio, F.1
  • 5
    • 77952274806 scopus 로고    scopus 로고
    • New nanofabrication strategies: Inspired by biomineralization
    • Aizenberg J. New nanofabrication strategies: inspired by biomineralization. MRS Bull. 35, 323-330 (2010
    • (2010) MRS Bull , vol.35 , pp. 323-330
    • Aizenberg, J.1
  • 6
    • 84863207403 scopus 로고    scopus 로고
    • Biomineralization as an inspiration for materials chemistry
    • Nudelman F. & Sommerdijk N. A. J. M. Biomineralization as an inspiration for materials chemistry. Angew. Chem. Int. Ed. 51, 6582-6596 (2012
    • (2012) Angew. Chem. Int. Ed , vol.51 , pp. 6582-6596
    • Nudelman, F.1    Sommerdijk, N.A.J.M.2
  • 7
    • 12044256704 scopus 로고
    • Molecular tectonics in biomineralization and biomimetic materials chemistry
    • Mann S. Molecular tectonics in biomineralization and biomimetic materials chemistry. Nature 365, 499-505 (1993
    • (1993) Nature , vol.365 , pp. 499-505
    • Mann, S.1
  • 8
    • 16244401140 scopus 로고    scopus 로고
    • Biomimetism and bioinspiration as tools for the design of innovative materials and systems
    • Sanchez C., Arribart H. & Giraud Guille M. M. Biomimetism and bioinspiration as tools for the design of innovative materials and systems. Nat. Mater. 4, 277-288 (2005
    • (2005) Nat. Mater , vol.4 , pp. 277-288
    • Sanchez, C.1    Arribart, H.2    Giraud Guille, M.M.3
  • 9
    • 84877316692 scopus 로고    scopus 로고
    • Rational design of thermostable vaccines by engineered peptideinduced virus self-biomineralization under physiological conditions
    • Wang G., et al. Rational design of thermostable vaccines by engineered peptideinduced virus self-biomineralization under physiological conditions. Proc. Natl Acad. Sci. USA 110, 7619-7624 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 7619-7624
    • Wang, G.1
  • 10
    • 84908299353 scopus 로고    scopus 로고
    • Overcoming the challenges in administering biopharmaceuticals: Formulation and delivery strategies
    • Mitragotri S., Burke P. A. & Langer R. Overcoming the challenges in administering biopharmaceuticals: formulation and delivery strategies. Nat. Rev. Drug Discov. 13, 655-672 (2014
    • (2014) Nat. Rev. Drug Discov , vol.13 , pp. 655-672
    • Mitragotri, S.1    Burke, P.A.2    Langer, R.3
  • 11
    • 84860741240 scopus 로고    scopus 로고
    • Engineering the third wave of biocatalysis
    • Bornscheuer U. T., et al. Engineering the third wave of biocatalysis. Nature 485, 185-194 (2012
    • (2012) Nature , vol.485 , pp. 185-194
    • Bornscheuer, U.T.1
  • 12
    • 84896276136 scopus 로고    scopus 로고
    • Logistics: Keeping cool
    • Savage N. Logistics: keeping cool. Nature 507, S8-S9 (2014
    • (2014) Nature , vol.507 , pp. S8-S9
    • Savage, N.1
  • 13
    • 57349101729 scopus 로고    scopus 로고
    • Computational techniques at the organic-inorganic interface in biomineralization
    • Harding J. H., et al. Computational techniques at the organic-inorganic interface in biomineralization. Chem. Rev. 108, 4823-4854 (2008
    • (2008) Chem. Rev , vol.108 , pp. 4823-4854
    • Harding, J.H.1
  • 14
    • 84930624515 scopus 로고    scopus 로고
    • eds Vanden Heuvel J. P., Perdew G. H., Mattes W. B. & Greenlee W. F. Elsevier Science B.V
    • Vanden Heuvel J. P. in Cellular and Molecular Toxicology Vol. 14 (eds Vanden Heuvel J. P., Perdew G. H., Mattes W. B. & Greenlee W. F.) 29-56 (Elsevier Science B.V., 2002
    • (2002) Cellular and Molecular Toxicology , vol.14 , pp. 29-56
    • Vanden Heuvel, J.P.1
  • 15
    • 0038128307 scopus 로고    scopus 로고
    • Reticular synthesis and the design of new materials
    • Yaghi O. M., et al. Reticular synthesis and the design of new materials. Nature 423, 705-714 (2003
    • (2003) Nature , vol.423 , pp. 705-714
    • Yaghi, O.M.1
  • 16
    • 84883066942 scopus 로고    scopus 로고
    • The chemistry and applications of metal-organic frameworks
    • Furukawa H., Cordova K. E., OKeeffe M. & Yaghi O. M. The chemistry and applications of metal-organic frameworks. Science 341, 1230444 (2013
    • (2013) Science , vol.341 , pp. 1230444
    • Furukawa, H.1    Cordova, K.E.2    Okeeffe, M.3    Yaghi, O.M.4
  • 17
    • 84892563052 scopus 로고    scopus 로고
    • Functional hybrid porous coordination polymers
    • Foo M. L., Matsuda R. & Kitagawa S. Functional hybrid porous coordination polymers. Chem. Mater. 26, 310-322 (2014
    • (2014) Chem. Mater , vol.26 , pp. 310-322
    • Foo, M.L.1    Matsuda, R.2    Kitagawa, S.3
  • 18
    • 77956018113 scopus 로고    scopus 로고
    • Carbon dioxide capture: Prospects for new materials
    • DAlessandro D. M., Smit B. & Long J. R. Carbon dioxide capture: prospects for new materials. Angew. Chem. Int. Ed. 49, 6058-6082 (2010
    • (2010) Angew. Chem. Int. Ed , vol.49 , pp. 6058-6082
    • Dalessandro, D.M.1    Smit, B.2    Long, J.R.3
  • 19
    • 84856956939 scopus 로고    scopus 로고
    • Metal-organic frameworks in biomedicine
    • Horcajada P., et al. Metal-organic frameworks in biomedicine. Chem. Rev. 112, 1232-1268 (2012
    • (2012) Chem. Rev , vol.112 , pp. 1232-1268
    • Horcajada, P.1
  • 20
    • 84856968657 scopus 로고    scopus 로고
    • Metal-organic framework thin films: From fundamentals to applications
    • Bétard A. & Fischer R. A. Metal-organic framework thin films: from fundamentals to applications. Chem. Rev. 112, 1055-1083 (2012
    • (2012) Chem. Rev , vol.112 , pp. 1055-1083
    • Bétard, A.1    Fischer, R.A.2
  • 21
    • 84894236745 scopus 로고    scopus 로고
    • Using functional nano- and microparticles for the preparation of metal-organic framework composites with novel properties
    • Doherty C. M., et al. Using functional nano- and microparticles for the preparation of metal-organic framework composites with novel properties. Acc. Chem. Res. 47, 396-405 (2014
    • (2014) Acc. Chem. Res , vol.47 , pp. 396-405
    • Doherty, C.M.1
  • 22
    • 84880130091 scopus 로고    scopus 로고
    • Biomineral-inspired growth of metal-organic frameworks in gelatin hydrogel matrices
    • Garai A., Shepherd W., Huo J. & Bradshaw D. Biomineral-inspired growth of metal-organic frameworks in gelatin hydrogel matrices. J. Mater. Chem. B 1, 3678-3684 (2013
    • (2013) J. Mater. Chem. B , vol.1 , pp. 3678-3684
    • Garai, A.1    Shepherd, W.2    Huo, J.3    Bradshaw, D.4
  • 23
    • 84897006308 scopus 로고    scopus 로고
    • Optimized metal-organic-framework nanospheres for drug delivery: Evaluation of small-molecule encapsulation
    • Zhuang J., et al. Optimized metal-organic-framework nanospheres for drug delivery: evaluation of small-molecule encapsulation. ACS Nano 8, 2812-2819 (2014
    • (2014) ACS Nano , vol.8 , pp. 2812-2819
    • Zhuang, J.1
  • 24
    • 84856690588 scopus 로고    scopus 로고
    • Metal-adeninate vertices for the construction of an exceptionally porous metal-organic framework
    • An J., et al. Metal-adeninate vertices for the construction of an exceptionally porous metal-organic framework. Nat. Commun. 3, 604 (2012
    • (2012) Nat. Commun , vol.3 , pp. 604
    • An, J.1
  • 25
    • 79955114926 scopus 로고    scopus 로고
    • Interfacial synthesis of hollow metal-organic framework capsules demonstrating selective permeability
    • Ameloot R., et al. Interfacial synthesis of hollow metal-organic framework capsules demonstrating selective permeability. Nat. Chem. 3, 382-387 (2011
    • (2011) Nat. Chem , vol.3 , pp. 382-387
    • Ameloot, R.1
  • 26
    • 79952727900 scopus 로고    scopus 로고
    • A new method to position and functionalize metal-organic framework crystals
    • Falcaro P., et al. A new method to position and functionalize metal-organic framework crystals. Nat. Commun. 2, 237 (2011
    • (2011) Nat. Commun , vol.2 , pp. 237
    • Falcaro, P.1
  • 27
    • 84861452693 scopus 로고    scopus 로고
    • Large-pore apertures in a series of metal-organic frameworks
    • Deng H., et al. Large-pore apertures in a series of metal-organic frameworks. Science 336, 1018-1023 (2012
    • (2012) Science , vol.336 , pp. 1018-1023
    • Deng, H.1
  • 28
    • 79960053751 scopus 로고    scopus 로고
    • Immobilization of mp-11 into a mesoporous metal-organic framework mp-11@mesomof: A new platform for enzymatic catalysis
    • Lykourinou V., et al. Immobilization of MP-11 into a mesoporous metal-organic framework, MP-11@mesoMOF: a new platform for enzymatic catalysis. J. Am. Chem. Soc. 133, 10382-10385 (2011
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 10382-10385
    • Lykourinou, V.1
  • 29
    • 84865145315 scopus 로고    scopus 로고
    • How can proteins enter the interior of a MOF? Investigation of cytochrome c translocation into a mof consisting of mesoporous cages with microporous windows
    • Chen Y., et al. How can proteins enter the interior of a MOF?. investigation of Cytochrome c translocation into a MOF consisting of mesoporous cages with microporous windows. J. Am. Chem. Soc. 134, 13188-13191 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 13188-13191
    • Chen, Y.1
  • 30
    • 84907879493 scopus 로고    scopus 로고
    • One-pot synthesis of proteinembedded metal-organic frameworks with enhanced biological activities
    • Lyu F., Zhang Y., Zare R. N., Ge J. & Liu Z. One-pot synthesis of proteinembedded metal-organic frameworks with enhanced biological activities. Nano Lett. 14, 5761-5765 (2014
    • (2014) Nano Lett , vol.14 , pp. 5761-5765
    • Lyu, F.1    Zhang, Y.2    Zare, R.N.3    Ge, J.4    Liu, Z.5
  • 31
    • 84903784157 scopus 로고    scopus 로고
    • MOF positioning technology and device fabrication
    • Falcaro P., et al. MOF positioning technology and device fabrication. Chem. Soc. Rev. 43, 5513-5560 (2014
    • (2014) Chem. Soc. Rev , vol.43 , pp. 5513-5560
    • Falcaro, P.1
  • 32
    • 33745900775 scopus 로고    scopus 로고
    • Exceptional chemical and thermal stability of zeolitic imidazolate frameworks
    • Park K. S., et al. Exceptional chemical and thermal stability of zeolitic imidazolate frameworks. Proc. Natl Acad. Sci. USA 103, 10186-10191 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10186-10191
    • Park, K.S.1
  • 33
    • 84862162170 scopus 로고    scopus 로고
    • Zeolitic imidazolate framework-8 as efficient pH-sensitive drug delivery vehicle
    • Sun C.-Y., et al. Zeolitic imidazolate framework-8 as efficient pH-sensitive drug delivery vehicle. Dalton Trans. 41, 6906-6909 (2012
    • (2012) Dalton Trans , vol.41 , pp. 6906-6909
    • Sun, C.-Y.1
  • 34
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A. & Zscherp C. What vibrations tell us about proteins. Q. Rev. Biophys. 35, 369-430 (2002
    • (2002) Q. Rev. Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 35
    • 84962385185 scopus 로고    scopus 로고
    • A theoretical study of zinc(II) interactions with amino acid models and peptide fragments
    • Trzaskowski B., Adamowicz L. & Deymier P. A. A theoretical study of zinc(II) interactions with amino acid models and peptide fragments. J. Biol. Inorg. Chem. 13, 133-137 (2008
    • (2008) J. Biol. Inorg. Chem , vol.13 , pp. 133-137
    • Trzaskowski, B.1    Adamowicz, L.2    Deymier, P.A.3
  • 36
    • 84873630814 scopus 로고    scopus 로고
    • New functional amorphous calcium phosphate nanocomposites by enzyme-assisted biomineralization
    • Hwang E. T., Tatavarty R., Chung J. & Gu M. B. New functional amorphous calcium phosphate nanocomposites by enzyme-assisted biomineralization. Appl. Mater. Interfaces 5, 532-537 (2013
    • (2013) Appl. Mater. Interfaces , vol.5 , pp. 532-537
    • Hwang, E.T.1    Tatavarty, R.2    Chung, J.3    Gu, M.B.4
  • 37
    • 36949087112 scopus 로고
    • Participation of imidazole in intramolecular hydrogen bonding
    • Lukton A. Participation of imidazole in intramolecular hydrogen bonding. Nature 192, 422-424 (1961
    • (1961) Nature , vol.192 , pp. 422-424
    • Lukton, A.1
  • 38
    • 31444450716 scopus 로고    scopus 로고
    • Histidine aromatic interactions in proteins and protein-ligand complexes: Quantum chemical study of X-ray and model structures
    • Cauët, E., Rooman M., Wintjens R., Liévin J. & Biot C. Histidine aromatic interactions in proteins and protein-ligand complexes: quantum chemical study of X-ray and model structures. J. Chem. Theory Comput. 1, 472-483 (2005
    • (2005) J. Chem. Theory Comput , vol.1 , pp. 472-483
    • Cauët, E.1    Rooman, M.2    Wintjens, R.3    Liévin, J.4    Biot, C.5
  • 39
    • 80051766035 scopus 로고    scopus 로고
    • Fast nucleation and growth of ZIF-8 nanocrystals monitored by time-resolved in situ small-angle and wide-angle X-Ray scattering
    • Cravillon J., et al. Fast nucleation and growth of ZIF-8 nanocrystals monitored by time-resolved in situ small-angle and wide-angle X-Ray scattering. Angew. Chem. Int. Ed. 50, 8067-8071 (2011
    • (2011) Angew. Chem. Int. Ed , vol.50 , pp. 8067-8071
    • Cravillon, J.1
  • 40
    • 4644233245 scopus 로고    scopus 로고
    • An overview of biomineralization processes and the problem of the vital effect
    • Weiner S. & Dove P. M. An overview of biomineralization processes and the problem of the vital effect. Rev. Mineral. Geochem. 54, 1-29 (2003
    • (2003) Rev. Mineral. Geochem , vol.54 , pp. 1-29
    • Weiner, S.1    Dove, P.M.2
  • 41
    • 0030142878 scopus 로고    scopus 로고
    • Compatibilization of polymer blends by complexation 1 spectroscopic characterization of ion amide interactions in ionomer/polyamide blends
    • Feng Y., Schmidt A. & Weiss R. A. Compatibilization of polymer blends by complexation. 1. spectroscopic characterization of ion amide interactions in ionomer/polyamide blends. Macromolecules 29, 3909-3917 (1996
    • (1996) Macromolecules , vol.29 , pp. 3909-3917
    • Feng, Y.1    Schmidt, A.2    Weiss, R.A.3
  • 42
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller K. M. & Wong C.-H. Enzymes for chemical synthesis. Nature 409, 232-240 (2001
    • (2001) Nature , vol.409 , pp. 232-240
    • Koeller, K.M.1    Wong, C.-H.2
  • 43
    • 0030662088 scopus 로고    scopus 로고
    • The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents
    • Toba S. & Merz K. M. The concept of solvent compatibility and its impact on protein stability and activity enhancement in nonaqueous solvents. J. Am. Chem. Soc. 119, 9939-9948 (1997
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 9939-9948
    • Toba, S.1    Merz, K.M.2
  • 44
    • 84880082972 scopus 로고    scopus 로고
    • Immobilization of enzymes on porous silicas - Benefits and challenges
    • Hartmann M. & Kostrov X. Immobilization of enzymes on porous silicas - benefits and challenges. Chem. Soc. Rev. 42, 6277-6289 (2013
    • (2013) Chem. Soc. Rev , vol.42 , pp. 6277-6289
    • Hartmann, M.1    Kostrov, X.2
  • 45
    • 84880113060 scopus 로고    scopus 로고
    • Conformational changes of enzymes upon immobilisation
    • Secundo F. Conformational changes of enzymes upon immobilisation. Chem. Soc. Rev. 42, 6250-6261 (2013
    • (2013) Chem. Soc. Rev , vol.42 , pp. 6250-6261
    • Secundo, F.1
  • 46
    • 81355149809 scopus 로고    scopus 로고
    • Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface
    • Su Y., et al. Improving the thermostability of a methyl parathion hydrolase by adding the ionic bond on protein surface. Appl. Biochem. Biotechnol. 165, 989-997 (2011
    • (2011) Appl. Biochem. Biotechnol , vol.165 , pp. 989-997
    • Su, Y.1
  • 48
    • 0037207018 scopus 로고    scopus 로고
    • Reversible immobilization of urease onto procion brown mx-5br-ni(ii) attached polyamide hollow-fibre membranes
    • Akgöl, S., Yalçinkaya Y., Bayramoʇlu G., Denizli A. & Arica M. Y. Reversible immobilization of urease onto Procion Brown MX-5BR-Ni(II) attached polyamide hollow-fibre membranes. Process Biochem. 38, 675-683 (2002
    • (2002) Process Biochem , vol.38 , pp. 675-683
    • Akgöl, S.1    Yalçinkaya, Y.2    Bayramoʇlu, G.3    Denizli, A.4    Arica, M.Y.5
  • 49
    • 64649100132 scopus 로고    scopus 로고
    • Functional, catalytic and kinetic properties: A review
    • Krajewska B. & Ureases I. Functional, catalytic and kinetic properties: a review. J. Mol. Catal. B: Enzym. 59, 9-21 (2009
    • (2009) J. Mol. Catal. B: Enzym , vol.59 , pp. 9-21
    • Krajewska, B.1    Ureases, I.2
  • 50
    • 33646429780 scopus 로고    scopus 로고
    • Immobilization imparts stability to watermelon urease to work in water miscible organic media
    • Prakash O. & Upadhyay L. S. B. Immobilization imparts stability to watermelon urease to work in water miscible organic media. Biotechnol. Bioprocess Eng. 11, 140-145 (2006
    • (2006) Biotechnol. Bioprocess Eng , vol.11 , pp. 140-145
    • Prakash, O.1    Upadhyay, L.S.B.2
  • 51
    • 44149086370 scopus 로고    scopus 로고
    • Structural and luminescent properties of micro- and nanosized particles of lanthanide terephthalate coordination polymers
    • Daiguebonne C., et al. Structural and luminescent properties of micro- and nanosized particles of lanthanide terephthalate coordination polymers. Inorg. Chem. 47, 3700-3708 (2008
    • (2008) Inorg. Chem , vol.47 , pp. 3700-3708
    • Daiguebonne, C.1
  • 52
    • 0014940352 scopus 로고
    • Gel chromatography of proteins in denaturing solvents comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants
    • Fish W. W., Reynolds J. A. & Tanford C. Gel chromatography of proteins in denaturing solvents comparison between sodium dodecyl sulfate and guanidine hydrochloride as denaturants. J. Biol. Chem. 245, 5166-5168 (1970
    • (1970) J. Biol. Chem , vol.245 , pp. 5166-5168
    • Fish, W.W.1    Reynolds, J.A.2    Tanford, C.3
  • 53
    • 33744465233 scopus 로고    scopus 로고
    • Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS
    • Gudiksen K. L., Gitlin I. & Whitesides G. M. Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS. Proc. Natl Acad. Sci. USA 103, 7968-7972 (2006
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 7968-7972
    • Gudiksen, K.L.1    Gitlin, I.2    Whitesides, G.M.3
  • 55
    • 1642578975 scopus 로고    scopus 로고
    • Pqq glucose dehydrogenase with novel electron transfer ability
    • Okuda J. & Sode K. PQQ glucose dehydrogenase with novel electron transfer ability. Biochem. Biophys. Res. Commun. 314, 793-797 (2004
    • (2004) Biochem. Biophys. Res. Commun , vol.314 , pp. 793-797
    • Okuda, J.1    Sode, K.2
  • 56
    • 0028587627 scopus 로고
    • Over expression of pqq glucose dehydrogenase in escherichia coli under holo enzyme forming condition
    • Sode K., et al. Over expression of PQQ glucose dehydrogenase in Escherichia coli under holo enzyme forming condition. Biotechnol. Lett. 16, 1265-1268 (1994
    • (1994) Biotechnol. Lett , vol.16 , pp. 1265-1268
    • Sode, K.1
  • 58
    • 0000876929 scopus 로고    scopus 로고
    • Small-angle scattering from polymeric mass fractals of arbitrary mass-fractal dimension
    • Beaucage G. Small-angle scattering from polymeric mass fractals of arbitrary mass-fractal dimension. J. Appl. Crystallogr. 29, 134-146 (1996
    • (1996) J. Appl. Crystallogr , vol.29 , pp. 134-146
    • Beaucage, G.1
  • 59
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins D. K., et al. Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38, 16424-16431 (1999
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1
  • 60
    • 34248397195 scopus 로고    scopus 로고
    • Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering
    • Mylonas E. & Svergun D. I. Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering. J. Appl. Crystallogr. 40, 95-106 (2007
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 95-106
    • Mylonas, E.1    Svergun, D.I.2


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