메뉴 건너뛰기




Volumn 29, Issue 6, 2018, Pages 1950-1960

Influence of PEGylation on Domain Dynamics of Phosphoglycerate Kinase: PEG Acts Like Entropic Spring for the Protein

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; BROWNIAN MOVEMENT; DYNAMICS; ENZYMES; FUNCTIONAL POLYMERS; LIGANDS; NEUTRON SCATTERING;

EID: 85047966377     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/acs.bioconjchem.8b00203     Document Type: Article
Times cited : (16)

References (65)
  • 1
    • 84968857097 scopus 로고    scopus 로고
    • Site-specific pegylation of therapeutic proteins
    • Dozier, J. K. and Distefano, M. D. (2015) Site-specific pegylation of therapeutic proteins. Int. J. Mol. Sci. 16, 25831-25864, 10.3390/ijms161025831
    • (2015) Int. J. Mol. Sci. , vol.16 , pp. 25831-25864
    • Dozier, J.K.1    Distefano, M.D.2
  • 2
    • 34548482374 scopus 로고    scopus 로고
    • Stealth liposomes: Review of the basic science, rationale, and clinical applications, existing and potential
    • Immordino, M. L., Dosio, F., and Cattel, L. (2006) Stealth liposomes: Review of the basic science, rationale, and clinical applications, existing and potential. International Journal of Nanomedicine 1, 297-315
    • (2006) International Journal of Nanomedicine , vol.1 , pp. 297-315
    • Immordino, M.L.1    Dosio, F.2    Cattel, L.3
  • 4
    • 0036668565 scopus 로고    scopus 로고
    • Pegvisomant: Structure and function
    • Pradhananga, S., Wilkinson, I., and Ross, R. J. M. (2002) Pegvisomant: Structure and function. J. Mol. Endocrinol. 29 (1), 11-14, 10.1677/jme.0.0290011
    • (2002) J. Mol. Endocrinol. , vol.29 , Issue.1 , pp. 11-14
    • Pradhananga, S.1    Wilkinson, I.2    Ross, R.J.M.3
  • 5
    • 34548224598 scopus 로고    scopus 로고
    • PEG-asparaginase
    • Fu, C. H. and Sakamoto, K. M. (2007) PEG-asparaginase. Expert Opin. Pharmacother. 8 (12), 1977-1984, 10.1517/14656566.8.12.1977
    • (2007) Expert Opin. Pharmacother. , vol.8 , Issue.12 , pp. 1977-1984
    • Fu, C.H.1    Sakamoto, K.M.2
  • 6
    • 84994417460 scopus 로고    scopus 로고
    • Emerging therapies for neuropathic lysosomal storage disorders
    • Kelly, J. M., Bradbury, A., Martin, D. R., and Byrne, M. E. (2017) Emerging therapies for neuropathic lysosomal storage disorders. Prog. Neurobiol. 152, 166-180, 10.1016/j.pneurobio.2016.10.002
    • (2017) Prog. Neurobiol. , vol.152 , pp. 166-180
    • Kelly, J.M.1    Bradbury, A.2    Martin, D.R.3    Byrne, M.E.4
  • 7
    • 67349107534 scopus 로고    scopus 로고
    • Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates
    • Rodríguez-Martínez, J. A., Rivera-Rivera, I., Solá, R. J., and Griebenow, K. (2009) Enzymatic activity and thermal stability of PEG-α-chymotrypsin conjugates. Biotechnol. Lett. 31 (6), 883-887, 10.1007/s10529-009-9947-y
    • (2009) Biotechnol. Lett. , vol.31 , Issue.6 , pp. 883-887
    • Rodríguez-Martínez, J.A.1    Rivera-Rivera, I.2    Solá, R.J.3    Griebenow, K.4
  • 9
    • 79951580612 scopus 로고    scopus 로고
    • Biophysical characterisation of GlycoPEGylated recombinant human factor VIIa
    • Plesner, B., Westh, P., and Nielsen, A. D. (2011) Biophysical characterisation of GlycoPEGylated recombinant human factor VIIa. Int. J. Pharm. 406 (1-2), 62-68, 10.1016/j.ijpharm.2010.12.034
    • (2011) Int. J. Pharm. , vol.406 , Issue.12 , pp. 62-68
    • Plesner, B.1    Westh, P.2    Nielsen, A.D.3
  • 10
    • 79956205484 scopus 로고    scopus 로고
    • Prevention of benzyl alcohol- induced aggregation of chymotrypsinogen by PEGylation
    • Rodríguez-Martínez, J. A., Rivera-Rivera, I., and Griebenow, K. (2011) Prevention of benzyl alcohol- induced aggregation of chymotrypsinogen by PEGylation. J. Pharm. Pharmacol. 63 (6), 800-805, 10.1111/j.2042-7158.2011.01288.x
    • (2011) J. Pharm. Pharmacol. , vol.63 , Issue.6 , pp. 800-805
    • Rodríguez-Martínez, J.A.1    Rivera-Rivera, I.2    Griebenow, K.3
  • 11
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics
    • Simone Fishburn, C. (2008) The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics. J. Pharm. Sci. 97, 4167-4183, 10.1002/jps.21278
    • (2008) J. Pharm. Sci. , vol.97 , pp. 4167-4183
    • Simone Fishburn, C.1
  • 12
    • 85012300513 scopus 로고    scopus 로고
    • Effect of PEG molecular weight and PEGylation degree on the physical stability of PEGylated lysozyme
    • Morgenstern, J., Baumann, P., Brunner, C., and Hubbuch, J. (2017) Effect of PEG molecular weight and PEGylation degree on the physical stability of PEGylated lysozyme. Int. J. Pharm. 519, 408-417, 10.1016/j.ijpharm.2017.01.040
    • (2017) Int. J. Pharm. , vol.519 , pp. 408-417
    • Morgenstern, J.1    Baumann, P.2    Brunner, C.3    Hubbuch, J.4
  • 13
    • 0036852102 scopus 로고    scopus 로고
    • Enhanced activity by poly(ethylene glycol) modification of Coriolopsis gallica laccase
    • Vandertol-Vanier, H. A., Vazquez-Duhalt, R., Tinoco, R., and Pickard, M. A. (2002) Enhanced activity by poly(ethylene glycol) modification of Coriolopsis gallica laccase. J. Ind. Microbiol. Biotechnol. 29 (5), 214-220, 10.1038/sj.jim.7000308
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.29 , Issue.5 , pp. 214-220
    • Vandertol-Vanier, H.A.1    Vazquez-Duhalt, R.2    Tinoco, R.3    Pickard, M.A.4
  • 14
    • 0026816560 scopus 로고
    • Increased activity and stability of poly(ethylene glycol)-modified trypsin
    • Gaertner, H. F. and Puigserver, A. J. (1992) Increased activity and stability of poly(ethylene glycol)-modified trypsin. Enzyme Microb. Technol. 14 (2), 150-155, 10.1016/0141-0229(92)90174-M
    • (1992) Enzyme Microb. Technol. , vol.14 , Issue.2 , pp. 150-155
    • Gaertner, H.F.1    Puigserver, A.J.2
  • 15
    • 78049291945 scopus 로고    scopus 로고
    • Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding
    • Dhar, A., Samiotakis, A., Ebbinghaus, S., Nienhaus, L., Homouz, D., Gruebele, M., and Cheung, M. S. (2010) Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding. Proc. Natl. Acad. Sci. U. S. A. 107 (41), 17586-17591, 10.1073/pnas.1006760107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.41 , pp. 17586-17591
    • Dhar, A.1    Samiotakis, A.2    Ebbinghaus, S.3    Nienhaus, L.4    Homouz, D.5    Gruebele, M.6    Cheung, M.S.7
  • 16
    • 81255189103 scopus 로고    scopus 로고
    • The conformation of the poly(ethylene glycol) chain in mono- PEGylated Lysozyme and mono-PEGylated human growth hormone
    • Pai, S. S., Hammouda, B., Hong, K., Pozzo, D. C., Przybycien, T. M., and Tilton, R. D. (2011) The conformation of the poly(ethylene glycol) chain in mono- PEGylated Lysozyme and mono-PEGylated human growth hormone. Bioconjugate Chem. 22 (11), 2317-2323, 10.1021/bc2003583
    • (2011) Bioconjugate Chem. , vol.22 , Issue.11 , pp. 2317-2323
    • Pai, S.S.1    Hammouda, B.2    Hong, K.3    Pozzo, D.C.4    Przybycien, T.M.5    Tilton, R.D.6
  • 17
    • 84938629639 scopus 로고    scopus 로고
    • Conformation of the Poly(ethylene Glycol) Chains in DiPEGylated Hemoglobin Specifically Probed by SANS: Correlation with PEG Length and in Vivo Efficiency
    • Le Cœur, C., Combet, S., Carrot, G., Busch, P., Teixeira, J., and Longeville, S. (2015) Conformation of the Poly(ethylene Glycol) Chains in DiPEGylated Hemoglobin Specifically Probed by SANS: Correlation with PEG Length and in Vivo Efficiency. Langmuir 31 (30), 8402-8410, 10.1021/acs.langmuir.5b01121
    • (2015) Langmuir , vol.31 , Issue.30 , pp. 8402-8410
    • Le Cœur, C.1    Combet, S.2    Carrot, G.3    Busch, P.4    Teixeira, J.5    Longeville, S.6
  • 18
    • 0018803381 scopus 로고
    • Sequence, structure and activity of phosphoglycerate kinase: A possible hinge-bending enzyme
    • Banks, R. D., Blake, C. C. F., Evans, P. R., Haser, R., Rice, D. W., Hardy, G. W., Merrett, M., and Phillips, A. W. (1979) Sequence, structure and activity of phosphoglycerate kinase: a possible hinge-bending enzyme. Nature 279 (5716), 773-777, 10.1038/279773a0
    • (1979) Nature , vol.279 , Issue.5716 , pp. 773-777
    • Banks, R.D.1    Blake, C.C.F.2    Evans, P.R.3    Haser, R.4    Rice, D.W.5    Hardy, G.W.6    Merrett, M.7    Phillips, A.W.8
  • 19
    • 0025239322 scopus 로고
    • Functional identity of a primer recognition protein as phosphoglycerate kinase
    • Jindal, H. K. and Vishwanatha, J. K. (1990) Functional identity of a primer recognition protein as phosphoglycerate kinase. J. Biol. Chem. 265 (12), 6540-6543
    • (1990) J. Biol. Chem. , vol.265 , Issue.12 , pp. 6540-6543
    • Jindal, H.K.1    Vishwanatha, J.K.2
  • 20
    • 0034649626 scopus 로고    scopus 로고
    • Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase
    • Lay, A. J., Jiang, X. M., Kisker, O., Flynn, E., Underwood, A., Condron, R., and Hogg, P. J. (2000) Phosphoglycerate kinase acts in tumour angiogenesis as a disulphide reductase. Nature 408 (6814), 869-873, 10.1038/35048596
    • (2000) Nature , vol.408 , Issue.6814 , pp. 869-873
    • Lay, A.J.1    Jiang, X.M.2    Kisker, O.3    Flynn, E.4    Underwood, A.5    Condron, R.6    Hogg, P.J.7
  • 21
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, a M., and Chothia, C. (1994) Structural mechanisms for domain movements in proteins. Biochemistry 33 (22), 6739-6749, 10.1021/bi00188a001
    • (1994) Biochemistry , vol.33 , Issue.22 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 22
    • 0031030765 scopus 로고    scopus 로고
    • Phosphotransfer hinges in PGK
    • Blake, C. (1997) Phosphotransfer hinges in PGK. Nature 385 (6613), 204-205, 10.1038/385204a0
    • (1997) Nature , vol.385 , Issue.6613 , pp. 204-205
    • Blake, C.1
  • 23
    • 0027074883 scopus 로고
    • Domain motions in phosphoglycerate kinase: Determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer
    • Haran, G., Haas, E., Szpikowska, B. K., and Mas, M. T. (1992) Domain motions in phosphoglycerate kinase: determination of interdomain distance distributions by site-specific labeling and time-resolved fluorescence energy transfer. Proc. Natl. Acad. Sci. U. S. A. 89 (24), 11764-11768, 10.1073/pnas.89.24.11764
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , Issue.24 , pp. 11764-11768
    • Haran, G.1    Haas, E.2    Szpikowska, B.K.3    Mas, M.T.4
  • 24
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
    • Bernstein, B. E., Michels, P. A., and Hol, W. G. (1997) Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 385 (6613), 275-278, 10.1038/385275a0
    • (1997) Nature , vol.385 , Issue.6613 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.2    Hol, W.G.3
  • 25
    • 0026536746 scopus 로고
    • Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3- phospho-D-glycerate
    • Harlos, K., Vas, M., and Blake, C. F. (1992) Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3- phospho-D-glycerate. Proteins: Struct., Funct., Genet. 12 (2), 133-144, 10.1002/prot.340120207
    • (1992) Proteins: Struct., Funct., Genet. , vol.12 , Issue.2 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.F.3
  • 26
    • 77958157527 scopus 로고    scopus 로고
    • Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase
    • Inoue, R., Biehl, R., Rosenkranz, T., Fitter, J., Monkenbusch, M., Radulescu, A., Farago, B., and Richter, D. (2010) Large domain fluctuations on 50-ns timescale enable catalytic activity in phosphoglycerate kinase. Biophys. J. 99 (7), 2309-2317, 10.1016/j.bpj.2010.08.017
    • (2010) Biophys. J. , vol.99 , Issue.7 , pp. 2309-2317
    • Inoue, R.1    Biehl, R.2    Rosenkranz, T.3    Fitter, J.4    Monkenbusch, M.5    Radulescu, A.6    Farago, B.7    Richter, D.8
  • 27
    • 0026352256 scopus 로고
    • On-line characterization of polyethylene glycol- modified proteins
    • Kunitani, M., Dollinger, G., Johnson, D., and Kresin, L. (1991) On-line characterization of polyethylene glycol- modified proteins. J. Chromatogr. A 588, 125-137, 10.1016/0021-9673(91)85014-7
    • (1991) J. Chromatogr. A , vol.588 , pp. 125-137
    • Kunitani, M.1    Dollinger, G.2    Johnson, D.3    Kresin, L.4
  • 28
    • 34548288653 scopus 로고    scopus 로고
    • Native PAGE eliminates the problem of PEG-SDS interaction in SDS-PAGE and provides an alternative to HPLC in characterization of protein PEGylation
    • Zheng, C. Y., Ma, G., and Su, Z. (2007) Native PAGE eliminates the problem of PEG-SDS interaction in SDS-PAGE and provides an alternative to HPLC in characterization of protein PEGylation. Electrophoresis 28 (16), 2801-2807, 10.1002/elps.200600807
    • (2007) Electrophoresis , vol.28 , Issue.16 , pp. 2801-2807
    • Zheng, C.Y.1    Ma, G.2    Su, Z.3
  • 29
    • 85012300513 scopus 로고    scopus 로고
    • Effect of PEG molecular weight and PEGylation degree on the physical stability of PEGylated lysozyme
    • Morgenstern, J., Baumann, P., Brunner, C., and Hubbuch, J. (2017) Effect of PEG molecular weight and PEGylation degree on the physical stability of PEGylated lysozyme. Int. J. Pharm. 519 (1-2), 408-417, 10.1016/j.ijpharm.2017.01.040
    • (2017) Int. J. Pharm. , vol.519 , Issue.12 , pp. 408-417
    • Morgenstern, J.1    Baumann, P.2    Brunner, C.3    Hubbuch, J.4
  • 30
    • 84973468673 scopus 로고    scopus 로고
    • Light Scattering Analysis of Mono- and Multi-PEGylated Bovine Serum Albumin in Solution: Role of Composition on Structure and Interactions
    • Ferebee, R., Hakem, I. F., Koch, A., Chen, M., Wu, Y., Loh, D., Wilson, D. C., Poole, J. L., Walker, J. P., Fytas, G. et al. (2016) Light Scattering Analysis of Mono- and Multi-PEGylated Bovine Serum Albumin in Solution: Role of Composition on Structure and Interactions. J. Phys. Chem. B 120 (20), 4591-4599, 10.1021/acs.jpcb.6b03097
    • (2016) J. Phys. Chem. B , vol.120 , Issue.20 , pp. 4591-4599
    • Ferebee, R.1    Hakem, I.F.2    Koch, A.3    Chen, M.4    Wu, Y.5    Loh, D.6    Wilson, D.C.7    Poole, J.L.8    Walker, J.P.9    Fytas, G.10
  • 31
    • 70350674559 scopus 로고    scopus 로고
    • Protein Fluorescence
    • Springer US, Boston, MA
    • Lakowicz, J. R. (2006) Protein Fluorescence. In Principles of Fluorescence Spectroscopy, pp 529-575, Vol. 30, Springer US, Boston, MA.
    • (2006) Principles of Fluorescence Spectroscopy , vol.30 , pp. 529-575
    • Lakowicz, J.R.1
  • 32
    • 0029905519 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in yeast 3- phosphoglycerate kinase monitored by fluorescence of single tryptophan probes
    • Cheung, C. W. and Mas, M. T. (1996) Substrate-induced conformational changes in yeast 3- phosphoglycerate kinase monitored by fluorescence of single tryptophan probes. Protein Sci. 5 (6), 1144-1149, 10.1002/pro.5560050616
    • (1996) Protein Sci. , vol.5 , Issue.6 , pp. 1144-1149
    • Cheung, C.W.1    Mas, M.T.2
  • 33
    • 0018606116 scopus 로고
    • Substrate Binding Closes the Cleft between the Domains of Yeast Phosphoglycerate Kinase
    • Pickover, C. A., McKay, D. B., Engelman, D. M., and Steitz, T. A. (1979) Substrate Binding Closes the Cleft between the Domains of Yeast Phosphoglycerate Kinase. J. Biol. Chem. 254 (22), 11323-11329
    • (1979) J. Biol. Chem. , vol.254 , Issue.22 , pp. 11323-11329
    • Pickover, C.A.1    McKay, D.B.2    Engelman, D.M.3    Steitz, T.A.4
  • 34
    • 33646174431 scopus 로고    scopus 로고
    • Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase
    • Varga, A., Flachner, B., Konarev, P., Gráczer, é., Szabó, J., Svergun, D., Závodszky, P., and Vas, M. (2006) Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase. FEBS Lett. 580 (11), 2698-2706, 10.1016/j.febslet.2006.04.024
    • (2006) FEBS Lett. , vol.580 , Issue.11 , pp. 2698-2706
    • Varga, A.1    Flachner, B.2    Konarev, P.3    Gráczer, A.4    Szabó, J.5    Svergun, D.6    Závodszky, P.7    Vas, M.8
  • 35
    • 79951472288 scopus 로고    scopus 로고
    • Exploring internal protein dynamics by neutron spin echo spectroscopy
    • Biehl, R., Monkenbusch, M., and Richter, D. (2011) Exploring internal protein dynamics by neutron spin echo spectroscopy. Soft Matter 7 (4), 1299-1307, 10.1039/C0SM00683A
    • (2011) Soft Matter , vol.7 , Issue.4 , pp. 1299-1307
    • Biehl, R.1    Monkenbusch, M.2    Richter, D.3
  • 36
    • 36149052898 scopus 로고
    • The dynamics of interacting Brownian particles
    • Pusey, P. N. (1975) The dynamics of interacting Brownian particles. J. Phys. A: Math. Gen. 8 (9), 1433-1440, 10.1088/0305-4470/8/9/012
    • (1975) J. Phys. A: Math. Gen. , vol.8 , Issue.9 , pp. 1433-1440
    • Pusey, P.N.1
  • 37
    • 0001526976 scopus 로고
    • Correlations for interacting Brownian particles. II
    • Ackerson, B. J. (1978) Correlations for interacting Brownian particles. II. J. Chem. Phys. 69 (2), 684-690, 10.1063/1.436634
    • (1978) J. Chem. Phys. , vol.69 , Issue.2 , pp. 684-690
    • Ackerson, B.J.1
  • 38
    • 5544266284 scopus 로고
    • Interpretation of the intermediate scattering function at short times
    • Ackerson, B. J., Pusey, P. N., and Tough, R. J. A. (1982) Interpretation of the intermediate scattering function at short times. J. Chem. Phys. 76 (3), 1279, 10.1063/1.443146
    • (1982) J. Chem. Phys. , vol.76 , Issue.3 , pp. 1279
    • Ackerson, B.J.1    Pusey, P.N.2    Tough, R.J.A.3
  • 39
    • 40849119960 scopus 로고    scopus 로고
    • Short-time transport properties in dense suspensions: From neutral to charge-stabilized colloidal spheres
    • Banchio, A. J. and Nägele, G. (2008) Short-time transport properties in dense suspensions: From neutral to charge-stabilized colloidal spheres. J. Chem. Phys. 128 (10), 104903-104920, 10.1063/1.2868773
    • (2008) J. Chem. Phys. , vol.128 , Issue.10 , pp. 104903-104920
    • Banchio, A.J.1    Nägele, G.2
  • 40
    • 84912080934 scopus 로고    scopus 로고
    • Slow internal protein dynamics in solution
    • Biehl, R. and Richter, D. (2014) Slow internal protein dynamics in solution. J. Phys.: Condens. Matter 26 (50), 503103, 10.1088/0953-8984/26/50/503103
    • (2014) J. Phys.: Condens. Matter , vol.26 , Issue.50 , pp. 503103
    • Biehl, R.1    Richter, D.2
  • 41
    • 79951472288 scopus 로고    scopus 로고
    • Exploring internal protein dynamics by neutron spin echo spectroscopy
    • Biehl, R., Monkenbusch, M., and Richter, D. (2011) Exploring internal protein dynamics by neutron spin echo spectroscopy. Soft Matter 7 (4), 1299, 10.1039/C0SM00683A
    • (2011) Soft Matter , vol.7 , Issue.4 , pp. 1299
    • Biehl, R.1    Monkenbusch, M.2    Richter, D.3
  • 42
    • 84962374450 scopus 로고    scopus 로고
    • Fast antibody fragment motion: Flexible linkers act as entropic spring
    • Stingaciu, L. R., Ivanova, O., Ohl, M., Biehl, R., and Richter, D. (2016) Fast antibody fragment motion: flexible linkers act as entropic spring. Sci. Rep. 6, 22148, 10.1038/srep22148
    • (2016) Sci. Rep. , vol.6 , pp. 22148
    • Stingaciu, L.R.1    Ivanova, O.2    Ohl, M.3    Biehl, R.4    Richter, D.5
  • 43
    • 36149005118 scopus 로고
    • On the Theory of the Brownian Motion
    • Uhlenbeck, G. and Ornstein, L. (1930) On the Theory of the Brownian Motion. Phys. Rev. 36 (5), 823-841, 10.1103/PhysRev.36.823
    • (1930) Phys. Rev. , vol.36 , Issue.5 , pp. 823-841
    • Uhlenbeck, G.1    Ornstein, L.2
  • 44
    • 22344432186 scopus 로고    scopus 로고
    • Quasielastic neutron scattering and relaxation processes in proteins: Analytical and simulation-based models
    • Kneller, G. R. (2005) Quasielastic neutron scattering and relaxation processes in proteins: analytical and simulation-based models. Phys. Chem. Chem. Phys. 7 (13), 2641-2655, 10.1039/b502040a
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , Issue.13 , pp. 2641-2655
    • Kneller, G.R.1
  • 45
    • 0034333282 scopus 로고    scopus 로고
    • Inelastic neutron scattering from damped collective vibrations of macromolecules
    • Kneller, G. R. (2000) Inelastic neutron scattering from damped collective vibrations of macromolecules. Chem. Phys. 261 (1), 1-24, 10.1016/S0301-0104(00)00223-8
    • (2000) Chem. Phys. , vol.261 , Issue.1 , pp. 1-24
    • Kneller, G.R.1
  • 47
    • 77949793651 scopus 로고    scopus 로고
    • Polymer dynamics under soft confinement in a self-assembled system
    • Willner, L., Lund, R., Monkenbusch, M., Holderer, O., Colmenero, J., and Richter, D. (2010) Polymer dynamics under soft confinement in a self-assembled system. Soft Matter 6 (7), 1559-1570, 10.1039/b922649d
    • (2010) Soft Matter , vol.6 , Issue.7 , pp. 1559-1570
    • Willner, L.1    Lund, R.2    Monkenbusch, M.3    Holderer, O.4    Colmenero, J.5    Richter, D.6
  • 48
    • 0000054224 scopus 로고
    • The Configuration of the Polyoxyethylene Chain
    • Mark, J. E. and Flory, P. J. (1965) The Configuration of the Polyoxyethylene Chain. J. Am. Chem. Soc. 87 (7), 1415-1423, 10.1021/ja01085a001
    • (1965) J. Am. Chem. Soc. , vol.87 , Issue.7 , pp. 1415-1423
    • Mark, J.E.1    Flory, P.J.2
  • 49
    • 0035578763 scopus 로고    scopus 로고
    • Local entropic effects of polymers grafted to soft interfaces
    • Bickel, T., Jeppesen, C., and Marques, C. M. (2001) Local entropic effects of polymers grafted to soft interfaces. Eur. Phys. J. E: Soft Matter Biol. Phys. 4 (1), 33-43, 10.1007/s101890170140
    • (2001) Eur. Phys. J. E: Soft Matter Biol. Phys. , vol.4 , Issue.1 , pp. 33-43
    • Bickel, T.1    Jeppesen, C.2    Marques, C.M.3
  • 50
    • 79960189344 scopus 로고    scopus 로고
    • Dynamic allostery: Linkers are not merely flexible
    • Ma, B., Tsai, C. J., Haliloǧlu, T., and Nussinov, R. (2011) Dynamic allostery: Linkers are not merely flexible. Structure 19 (7), 907-917, 10.1016/j.str.2011.06.002
    • (2011) Structure , vol.19 , Issue.7 , pp. 907-917
    • Ma, B.1    Tsai, C.J.2    Haliloǧlu, T.3    Nussinov, R.4
  • 51
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh, H. N., Wrabl, J. O., Li, J., and Hilser, V. J. (2014) The ensemble nature of allostery. Nature 508 (7496), 331-339, 10.1038/nature13001
    • (2014) Nature , vol.508 , Issue.7496 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 52
    • 84940081777 scopus 로고    scopus 로고
    • A dynamically coupled allosteric network underlies binding cooperativity in Src kinase
    • Foda, Z. H., Shan, Y., Kim, E. T., Shaw, D. E., and Seeliger, M. A. (2015) A dynamically coupled allosteric network underlies binding cooperativity in Src kinase. Nat. Commun. 6 (1), 5939, 10.1038/ncomms6939
    • (2015) Nat. Commun. , vol.6 , Issue.1 , pp. 5939
    • Foda, Z.H.1    Shan, Y.2    Kim, E.T.3    Shaw, D.E.4    Seeliger, M.A.5
  • 53
    • 84989936696 scopus 로고    scopus 로고
    • Strain analysis of protein structures and low dimensionality of mechanical allosteric couplings
    • Mitchell, M. R., Tlusty, T., and Leibler, S. (2016) Strain analysis of protein structures and low dimensionality of mechanical allosteric couplings. Proc. Natl. Acad. Sci. U. S. A. 113 (40), E5847-E5855, 10.1073/pnas.1609462113
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , Issue.40 , pp. E5847-E5855
    • Mitchell, M.R.1    Tlusty, T.2    Leibler, S.3
  • 54
    • 73449144096 scopus 로고    scopus 로고
    • Dynamic Allostery in the Methionine Repressor Revealed by Force Distribution Analysis
    • Stacklies, W., Xia, F., and Gräter, F. (2009) Dynamic Allostery in the Methionine Repressor Revealed by Force Distribution Analysis. PLoS Comput. Biol. 5 (11), e1000574, 10.1371/journal.pcbi.1000574
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.11 , pp. e1000574
    • Stacklies, W.1    Xia, F.2    Gräter, F.3
  • 55
    • 79953671764 scopus 로고    scopus 로고
    • "fluctuograms" reveal the intermittent intra-protein communication in subtilisin carlsberg and correlate mechanical coupling with co-evolution
    • Silvestre-Ryan, J., Lin, Y., and Chu, J. W. (2011) "Fluctuograms" reveal the intermittent intra-protein communication in subtilisin carlsberg and correlate mechanical coupling with co-evolution. PLoS Comput. Biol. 7 (3), e1002023, 10.1371/journal.pcbi.1002023
    • (2011) PLoS Comput. Biol. , vol.7 , Issue.3 , pp. e1002023
    • Silvestre-Ryan, J.1    Lin, Y.2    Chu, J.W.3
  • 56
    • 0001060193 scopus 로고    scopus 로고
    • Site-directed mutagenesis of proline 204 in the "hinge" region of yeast phosphoglycerate kinase
    • McHarg, J., Kelly, S. M., Price, N. C., Cooper, a, and Littlechild, J. a. (1999) Site-directed mutagenesis of proline 204 in the "hinge" region of yeast phosphoglycerate kinase. Eur. J. Biochem. 259 (3), 939-945, 10.1046/j.1432-1327.1999.00133.x
    • (1999) Eur. J. Biochem. , vol.259 , Issue.3 , pp. 939-945
    • McHarg, J.1    Kelly, S.M.2    Price, N.C.3    Cooper, A.4    Littlechild, J.A.5
  • 58
    • 77956985151 scopus 로고
    • Phosphoglycerate kinase from Brewer's yeast. D-l,3-Diphosphoglycerate + ADP ⇄ d-3- Phosphoglycerate + ATP
    • Bücher, T. (1955) Phosphoglycerate kinase from Brewer's yeast. d-l,3-Diphosphoglycerate + ADP ⇄ d-3- Phosphoglycerate + ATP. Methods Enzymol. 1 (C), 415-422, 10.1016/0076-6879(55)01068-9
    • (1955) Methods Enzymol. , vol.1 , Issue.C , pp. 415-422
    • Bücher, T.1
  • 59
    • 0002388667 scopus 로고
    • Über die Abklingungszeit der Fluoreszenz
    • Stern, O. and Volmer, M. (1919) Über die Abklingungszeit der Fluoreszenz. Phys. Zeitschrift 20 (1), 183-188
    • (1919) Phys. Zeitschrift , vol.20 , Issue.1 , pp. 183-188
    • Stern, O.1    Volmer, M.2
  • 62
    • 0032533790 scopus 로고    scopus 로고
    • Analysis of domain motions by approximate normal mode calculations
    • Hinsen, K. (1998) Analysis of domain motions by approximate normal mode calculations. Proteins: Struct., Funct., Genet. 33 (3), 417-429, 10.1002/(SICI)1097-0134(19981115)33:3<417::AID-PROT10>3.0.CO;2-8
    • (1998) Proteins: Struct., Funct., Genet. , vol.33 , Issue.3 , pp. 417-429
    • Hinsen, K.1
  • 63
    • 0001339660 scopus 로고
    • The study of biological structures by neutron scattering from solution
    • Jacrot, B. (1976) The study of biological structures by neutron scattering from solution. Rep. Prog. Phys. 39 (10), 911-953, 10.1088/0034-4885/39/10/001
    • (1976) Rep. Prog. Phys. , vol.39 , Issue.10 , pp. 911-953
    • Jacrot, B.1
  • 64
    • 84977295671 scopus 로고
    • Dirac-Fock calculations of X-ray scattering factors and contributions to the mean inner potential for electron scattering
    • Rez, D., Rez, P., and Grant, I. (1994) Dirac-Fock calculations of X-ray scattering factors and contributions to the mean inner potential for electron scattering. Acta Crystallogr., Sect. A: Found. Crystallogr. 50 (4), 481-497, 10.1107/S0108767393013200
    • (1994) Acta Crystallogr., Sect. A: Found. Crystallogr. , vol.50 , Issue.4 , pp. 481-497
    • Rez, D.1    Rez, P.2    Grant, I.3
  • 65
    • 0032478214 scopus 로고    scopus 로고
    • Protein Hydration in Solution: Experimental Observation by X-Ray and Neutron Scattering
    • MARCH
    • Svergun, D. I., Richard, S., Koch, M. H. J., Sayers, Z., Kuprin, S., and Zaccai, G. (1998) Protein Hydration in Solution: Experimental Observation by X-Ray and Neutron Scattering. Proc. Natl. Acad. Sci. U. S. A. 95 (March), 2267-2272, 10.1073/pnas.95.5.2267
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 2267-2272
    • Svergun, D.I.1    Richard, S.2    Koch, M.H.J.3    Sayers, Z.4    Kuprin, S.5    Zaccai, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.