메뉴 건너뛰기




Volumn 110, Issue 48, 2013, Pages 19342-19347

Impact of reconstituted cytosol on protein stability

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN INHIBITOR; GLOBULAR PROTEIN; PROTON;

EID: 84888376873     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1312678110     Document Type: Article
Times cited : (160)

References (67)
  • 1
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman SB, Trach SO (1991) Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J Mol Biol 222(3): 599-620.
    • (1991) J Mol Biol , vol.222 , Issue.3 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2
  • 2
    • 84877014249 scopus 로고    scopus 로고
    • Soft interactions and crowding
    • Sarkar M, Li C, Pielak GJ (2013) Soft interactions and crowding. Biophys Rev 5(2): 187-194.
    • (2013) Biophys Rev , vol.5 , Issue.2 , pp. 187-194
    • Sarkar, M.1    Li, C.2    Pielak, G.J.3
  • 3
    • 84872904773 scopus 로고    scopus 로고
    • Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding
    • Minton AP (2013) Quantitative assessment of the relative contributions of steric repulsion and chemical interactions to macromolecular crowding. Biopolymers 99(4): 239-244.
    • (2013) Biopolymers , vol.99 , Issue.4 , pp. 239-244
    • Minton, A.P.1
  • 4
    • 79961215482 scopus 로고    scopus 로고
    • Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability
    • Knowles DB, LaCroix AS, Deines NF, Shkel I, Record MT, Jr. (2011) Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability. Proc Natl Acad Sci USA 108(31): 12699-12704.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.31 , pp. 12699-12704
    • Knowles, D.B.1    Lacroix, A.S.2    Deines, N.F.3    Shkel, I.4    Record Jr., M.T.5
  • 5
    • 80053106066 scopus 로고    scopus 로고
    • Quantitative characterization of temperatureindependent and temperature-dependent protein-protein interactions in highly nonideal solutions
    • Fodeke AA, Minton AP (2011) Quantitative characterization of temperatureindependent and temperature-dependent protein-protein interactions in highly nonideal solutions. J Phys Chem B 115(38): 11261-11268.
    • (2011) J Phys Chem B , vol.115 , Issue.38 , pp. 11261-11268
    • Fodeke, A.A.1    Minton, A.P.2
  • 6
    • 84876034428 scopus 로고    scopus 로고
    • Influence of crowded cellular environments on protein folding, binding, and oligomerization: Biological consequences and potentials of atomistic modeling
    • Zhou HX (2013) Influence of crowded cellular environments on protein folding, binding, and oligomerization: biological consequences and potentials of atomistic modeling. FEBS Lett 587(8): 1053-1061.
    • (2013) FEBS Lett , vol.587 , Issue.8 , pp. 1053-1061
    • Zhou, H.X.1
  • 7
    • 84876062242 scopus 로고    scopus 로고
    • Formation of protein complexes in crowded environments - From in vitro to in vivo
    • Phillip Y, Schreiber G (2013) Formation of protein complexes in crowded environments - from in vitro to in vivo. FEBS Lett 587(8): 1046-1052.
    • (2013) FEBS Lett , vol.587 , Issue.8 , pp. 1046-1052
    • Phillip, Y.1    Schreiber, G.2
  • 8
    • 79955698252 scopus 로고    scopus 로고
    • Protein crowding tunes protein stability
    • Miklos AC, Sarkar M, Wang Y, Pielak GJ (2011) Protein crowding tunes protein stability. J Am Chem Soc 133(18): 7116-7120.
    • (2011) J Am Chem Soc , vol.133 , Issue.18 , pp. 7116-7120
    • Miklos, A.C.1    Sarkar, M.2    Wang, Y.3    Pielak, G.J.4
  • 10
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181(4096): 223-230.
    • (1973) Science , vol.181 , Issue.4096 , pp. 223-230
    • Anfinsen, C.B.1
  • 12
    • 0019890347 scopus 로고
    • Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins
    • Wilf J, Minton AP (1981) Evidence for protein self-association induced by excluded volume. Myoglobin in the presence of globular proteins. Biochim Biophys Acta 670(3): 316-322.
    • (1981) Biochim Biophys Acta , vol.670 , Issue.3 , pp. 316-322
    • Wilf, J.1    Minton, A.P.2
  • 13
    • 0019883893 scopus 로고
    • Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase
    • Minton AP, Wilf J (1981) Effect of macromolecular crowding upon the structure and function of an enzyme: Glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 20(17): 4821-4826.
    • (1981) Biochemistry , vol.20 , Issue.17 , pp. 4821-4826
    • Minton, A.P.1    Wilf, J.2
  • 14
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou HX, Rivas G, Minton AP (2008) Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys 37: 375-397.
    • (2008) Annu Rev Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 15
    • 77951298407 scopus 로고    scopus 로고
    • Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
    • Elcock AH (2010) Models of macromolecular crowding effects and the need for quantitative comparisons with experiment. Curr Opin Struct Biol 20(2): 196-206.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.2 , pp. 196-206
    • Elcock, A.H.1
  • 16
    • 77955686807 scopus 로고    scopus 로고
    • Effects of proteins on protein diffusion
    • Wang Y, Li C, Pielak GJ (2010) Effects of proteins on protein diffusion. J Am Chem Soc 132(27): 9392-9397.
    • (2010) J Am Chem Soc , vol.132 , Issue.27 , pp. 9392-9397
    • Wang, Y.1    Li, C.2    Pielak, G.J.3
  • 17
    • 84855848788 scopus 로고    scopus 로고
    • Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding
    • Feig M, Sugita Y (2012) Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding. J Phys Chem B 116(1): 599-605.
    • (2012) J Phys Chem B , vol.116 , Issue.1 , pp. 599-605
    • Feig, M.1    Sugita, Y.2
  • 18
    • 33644858247 scopus 로고
    • Escherichia coli and Salmonella typhimurium (Am Soc Microbiol, Washington, DC)
    • Neidhardt FC (1987) Chemical Composition of Escherichia coli. Escherichia coli and Salmonella typhimurium (Am Soc Microbiol, Washington, DC), Vol 1.
    • (1987) Chemical Composition of Escherichia Coli , pp. 1
    • Neidhardt, F.C.1
  • 19
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner FR, et al. (1997) The complete genome sequence of Escherichia coli K-12. Science 277(5331): 1453-1462.
    • (1997) Science , vol.277 , Issue.5331 , pp. 1453-1462
    • Blattner, F.R.1
  • 20
    • 70350292376 scopus 로고    scopus 로고
    • Post-reductionist protein science, or putting Humpty Dumpty back together again
    • Gierasch LM, Gershenson A (2009) Post-reductionist protein science, or putting Humpty Dumpty back together again. Nat Chem Biol 5(11): 774-777.
    • (2009) Nat Chem Biol , vol.5 , Issue.11 , pp. 774-777
    • Gierasch, L.M.1    Gershenson, A.2
  • 21
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • Ghaemmaghami S, Oas TG (2001) Quantitative protein stability measurement in vivo. Nat Struct Biol 8(10): 879-882.
    • (2001) Nat Struct Biol , vol.8 , Issue.10 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 22
    • 0347004717 scopus 로고    scopus 로고
    • Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling
    • Ignatova Z, Gierasch LM (2004) Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. Proc Natl Acad Sci USA 101(2): 523-528.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.2 , pp. 523-528
    • Ignatova, Z.1    Gierasch, L.M.2
  • 23
    • 77950792003 scopus 로고    scopus 로고
    • Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm
    • McGuffee SR, Elcock AH (2010) Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm. PLOS Comput Biol 6(3):e1000694.
    • (2010) PLOS Comput Biol , vol.6 , Issue.3
    • McGuffee, S.R.1    Elcock, A.H.2
  • 24
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander SW, Kallenbach NR (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys 16(4): 521-655.
    • (1983) Q Rev Biophys , vol.16 , Issue.4 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 25
    • 77955676884 scopus 로고    scopus 로고
    • Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability
    • Miklos AC, Li C, Pielak GJ (2009) Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability. Methods Enzymol 466: 1-18.
    • (2009) Methods Enzymol , vol.466 , pp. 1-18
    • Miklos, A.C.1    Li, C.2    Pielak, G.J.3
  • 26
    • 79551565926 scopus 로고    scopus 로고
    • Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy
    • Barnes CO, Monteith WB, Pielak GJ (2011) Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy. ChemBioChem 12(3): 390-391.
    • (2011) ChemBioChem , vol.12 , Issue.3 , pp. 390-391
    • Barnes, C.O.1    Monteith, W.B.2    Pielak, G.J.3
  • 27
    • 79955024130 scopus 로고    scopus 로고
    • Protein interactions in the Escherichia coli cytosol: An impediment to in-cell NMR spectroscopy
    • Crowley PB, Chow E, Papkovskaia T (2011) Protein interactions in the Escherichia coli cytosol: An impediment to in-cell NMR spectroscopy. ChemBioChem 12(7): 1043-1048.
    • (2011) ChemBioChem , vol.12 , Issue.7 , pp. 1043-1048
    • Crowley, P.B.1    Chow, E.2    Papkovskaia, T.3
  • 28
    • 80055013471 scopus 로고    scopus 로고
    • Exploring weak, transient protein - Protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy
    • Wang Q, Zhuravleva A, Gierasch LM (2011) Exploring weak, transient protein - protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy. Biochemistry 50(43): 9225-9236.
    • (2011) Biochemistry , vol.50 , Issue.43 , pp. 9225-9236
    • Wang, Q.1    Zhuravleva, A.2    Gierasch, L.M.3
  • 29
    • 59849113286 scopus 로고    scopus 로고
    • Protein nuclear magnetic resonance under physiological conditions
    • Pielak GJ, et al. (2009) Protein nuclear magnetic resonance under physiological conditions. Biochemistry 48(2): 226-234.
    • (2009) Biochemistry , vol.48 , Issue.2 , pp. 226-234
    • Pielak, G.J.1
  • 30
    • 84888327393 scopus 로고    scopus 로고
    • Amide proton exchange of a dynamic loop in cell extracts
    • Smith AE, Sarkar M, Young GB, Pielak GJ (2013) Amide proton exchange of a dynamic loop in cell extracts. Protein Sci 22(10): 1313-1319.
    • (2013) Protein Sci , vol.22 , Issue.10 , pp. 1313-1319
    • Smith, A.E.1    Sarkar, M.2    Young, G.B.3    Pielak, G.J.4
  • 31
    • 84877926338 scopus 로고    scopus 로고
    • Probing non-specific interactions of Ca2+-calmodulin in E coli lysate
    • Latham MP, Kay LE (2013) Probing non-specific interactions of Ca2+-calmodulin in E. coli lysate. J Biomol NMR 55(3): 239-247.
    • (2013) J Biomol NMR , vol.55 , Issue.3 , pp. 239-247
    • Latham, M.P.1    Kay, L.E.2
  • 32
    • 84868122319 scopus 로고    scopus 로고
    • Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E coli lysate
    • Latham MP, Kay LE (2012) Is buffer a good proxy for a crowded cell-like environment? A comparative NMR study of calmodulin side-chain dynamics in buffer and E. coli lysate. PLoS ONE 7(10):e48226.
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Latham, M.P.1    Kay, L.E.2
  • 33
    • 0031552590 scopus 로고    scopus 로고
    • Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature
    • Itzhaki LS, Neira JL, Fersht AR (1997) Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature. J Mol Biol 270(1): 89-98.
    • (1997) J Mol Biol , vol.270 , Issue.1 , pp. 89-98
    • Itzhaki, L.S.1    Neira, J.L.2    Fersht, A.R.3
  • 34
    • 0031552596 scopus 로고    scopus 로고
    • Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis
    • Neira JL, Itzhaki LS, Otzen DE, Davis B, Fersht AR (1997) Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis. J Mol Biol 270(1): 99-110.
    • (1997) J Mol Biol , vol.270 , Issue.1 , pp. 99-110
    • Neira, J.L.1    Itzhaki, L.S.2    Otzen, D.E.3    Davis, B.4    Fersht, A.R.5
  • 35
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12
    • Link AJ, Robison K, Church GM (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18(8): 1259-1313.
    • (1997) Electrophoresis , vol.18 , Issue.8 , pp. 1259-1313
    • Link, A.J.1    Robison, K.2    Church, G.M.3
  • 36
    • 84876695491 scopus 로고    scopus 로고
    • NMR studies of weak protein-protein interactions
    • Lian L-Y (2013) NMR studies of weak protein-protein interactions. Prog Nucl Magn Reson Spectrosc 71: 59-72.
    • (2013) Prog Nucl Magn Reson Spectrosc , vol.71 , pp. 59-72
    • Lian, L.-Y.1
  • 37
    • 84888352385 scopus 로고    scopus 로고
    • PhD dissertation (Univ of North Carolina at Chapel Hill, Chapel Hill, NC)
    • Charlton LM (2008) Protein behavior in crowded environments. PhD dissertation (Univ of North Carolina at Chapel Hill, Chapel Hill, NC).
    • (2008) Protein Behavior in Crowded Environments
    • Charlton, L.M.1
  • 38
    • 77955707910 scopus 로고    scopus 로고
    • Volume exclusion and soft interaction effects on protein stability under crowded conditions
    • Miklos AC, Li C, Sharaf NG, Pielak GJ (2010) Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry 49(33): 6984-6991.
    • (2010) Biochemistry , vol.49 , Issue.33 , pp. 6984-6991
    • Miklos, A.C.1    Li, C.2    Sharaf, N.G.3    Pielak, G.J.4
  • 39
    • 84870899331 scopus 로고    scopus 로고
    • Unexpected effects of macromolecular crowding on protein stability
    • Benton LA, Smith AE, Young GB, Pielak GJ (2012) Unexpected effects of macromolecular crowding on protein stability. Biochemistry 51(49): 9773-9775.
    • (2012) Biochemistry , vol.51 , Issue.49 , pp. 9773-9775
    • Benton, L.A.1    Smith, A.E.2    Young, G.B.3    Pielak, G.J.4
  • 40
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y, Milne JS, Mayne L, Englander SW (1993) Primary structure effects on peptide group hydrogen exchange. Proteins 17(1): 75-86.
    • (1993) Proteins , vol.17 , Issue.1 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 41
    • 0031019924 scopus 로고    scopus 로고
    • The folding pathway of a protein at high resolution from microseconds to seconds
    • Nölting B, et al. (1997) The folding pathway of a protein at high resolution from microseconds to seconds. Proc Natl Acad Sci USA 94(3): 826-830.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.3 , pp. 826-830
    • Nölting, B.1
  • 42
    • 0019334807 scopus 로고
    • A novel application of nuclear Overhauser enhancement (NOE) in proteins: Analysis of correlated events in the exchange of internal labile protons
    • Wagner G (1980) A novel application of nuclear Overhauser enhancement (NOE) in proteins: Analysis of correlated events in the exchange of internal labile protons. Biochem Biophys Res Commun 97(2): 614-620.
    • (1980) Biochem Biophys Res Commun , vol.97 , Issue.2 , pp. 614-620
    • Wagner, G.1
  • 44
    • 44349088135 scopus 로고    scopus 로고
    • Residue-level interrogation of macromolecular crowding effects on protein stability
    • Charlton LM, et al. (2008) Residue-level interrogation of macromolecular crowding effects on protein stability. J Am Chem Soc 130(21): 6826-6830.
    • (2008) J Am Chem Soc , vol.130 , Issue.21 , pp. 6826-6830
    • Charlton, L.M.1
  • 45
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki LS, Otzen DE, Fersht AR (1995) The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol 254(2): 260-288.
    • (1995) J Mol Biol , vol.254 , Issue.2 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 46
    • 77951667170 scopus 로고    scopus 로고
    • 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: Application to denatured drkN SH3
    • Chevelkov V, Xue Y, Rao DK, Forman-Kay JD, Skrynnikov NR (2010) 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: Application to denatured drkN SH3. J Biomol NMR 46(3): 227-244.
    • (2010) J Biomol NMR , vol.46 , Issue.3 , pp. 227-244
    • Chevelkov, V.1    Xue, Y.2    Rao, D.K.3    Forman-Kay, J.D.4    Skrynnikov, N.R.5
  • 47
    • 62649143879 scopus 로고    scopus 로고
    • NMR analysis of native-state protein conformational flexibility by hydrogen exchange
    • Hernández G, LeMaster DM (2009) NMR analysis of native-state protein conformational flexibility by hydrogen exchange. Methods Mol Biol 490: 285-310.
    • (2009) Methods Mol Biol , vol.490 , pp. 285-310
    • Hernández, G.1    Lemaster, D.M.2
  • 49
    • 0020483829 scopus 로고
    • Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance
    • Wagner G, Wüthrich K (1982) Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance. J Mol Biol 160(2): 343-361.
    • (1982) J Mol Biol , vol.160 , Issue.2 , pp. 343-361
    • Wagner, G.1    Wüthrich, K.2
  • 50
    • 44949164734 scopus 로고    scopus 로고
    • A billion-fold range in acidity for the solvent-exposed amides of Pyrococcus furiosus rubredoxin
    • Anderson JS, Hernández G, Lemaster DM (2008) A billion-fold range in acidity for the solvent-exposed amides of Pyrococcus furiosus rubredoxin. Biochemistry 47(23): 6178-6188.
    • (2008) Biochemistry , vol.47 , Issue.23 , pp. 6178-6188
    • Anderson, J.S.1    Hernández, G.2    Lemaster, D.M.3
  • 51
    • 63149177937 scopus 로고    scopus 로고
    • Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions
    • Li C, Pielak GJ (2009) Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions. J Am Chem Soc 131(4): 1368-1369.
    • (2009) J Am Chem Soc , vol.131 , Issue.4 , pp. 1368-1369
    • Li, C.1    Pielak, G.J.2
  • 52
    • 50349092811 scopus 로고    scopus 로고
    • Absolute quantitation of intracellular metabolite concentrations by an isotope ratio-based approach
    • Bennett BD, Yuan J, Kimball EH, Rabinowitz JD (2008) Absolute quantitation of intracellular metabolite concentrations by an isotope ratio-based approach. Nat Protoc 3(8): 1299-1311.
    • (2008) Nat Protoc , vol.3 , Issue.8 , pp. 1299-1311
    • Bennett, B.D.1    Yuan, J.2    Kimball, E.H.3    Rabinowitz, J.D.4
  • 53
    • 68049100110 scopus 로고    scopus 로고
    • Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli
    • Bennett BD, et al. (2009) Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli. Nat Chem Biol 5(8): 593-599.
    • (2009) Nat Chem Biol , vol.5 , Issue.8 , pp. 593-599
    • Bennett, B.D.1
  • 54
    • 0026409841 scopus 로고
    • Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo
    • Cayley S, Lewis BA, Guttman HJ, Record MT, Jr. (1991) Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo. J Mol Biol 222(2): 281-300.
    • (1991) J Mol Biol , vol.222 , Issue.2 , pp. 281-300
    • Cayley, S.1    Lewis, B.A.2    Guttman, H.J.3    Record Jr., M.T.4
  • 55
    • 43149110398 scopus 로고    scopus 로고
    • Intracellular organic osmolytes: Function and regulation
    • Burg MB, Ferraris JD (2008) Intracellular organic osmolytes: Function and regulation. J Biol Chem 283(12): 7309-7313.
    • (2008) J Biol Chem , vol.283 , Issue.12 , pp. 7309-7313
    • Burg, M.B.1    Ferraris, J.D.2
  • 56
    • 34247521095 scopus 로고    scopus 로고
    • From the test tube to the cell: Exploring the folding and aggregation of a beta-clam protein
    • Ignatova Z, et al. (2007) From the test tube to the cell: Exploring the folding and aggregation of a beta-clam protein. Biopolymers 88(2): 157-163.
    • (2007) Biopolymers , vol.88 , Issue.2 , pp. 157-163
    • Ignatova, Z.1
  • 57
    • 84874194203 scopus 로고    scopus 로고
    • Polymer crowders and protein crowders act similarly on protein folding stability
    • Zhou HX (2013) Polymer crowders and protein crowders act similarly on protein folding stability. FEBS Lett 587(5): 394-397.
    • (2013) FEBS Lett , vol.587 , Issue.5 , pp. 394-397
    • Zhou, H.X.1
  • 58
    • 0020135896 scopus 로고
    • Molecular evolution, intracellular organization, and the quinary structure of proteins
    • McConkey EH (1982) Molecular evolution, intracellular organization, and the quinary structure of proteins. Proc Natl Acad Sci USA 79(10): 3236-3240.
    • (1982) Proc Natl Acad Sci USA , vol.79 , Issue.10 , pp. 3236-3240
    • McConkey, E.H.1
  • 59
    • 0034161474 scopus 로고    scopus 로고
    • Macromolecular interactions: Tracing the roots
    • Srere PA (2000) Macromolecular interactions: Tracing the roots. Trends Biochem Sci 25(3): 150-153.
    • (2000) Trends Biochem Sci , vol.25 , Issue.3 , pp. 150-153
    • Srere, P.A.1
  • 60
    • 67649922591 scopus 로고    scopus 로고
    • Self-organization of the Escherichia coli chemotaxis network imaged with super-resolution light microscopy
    • Greenfield D, et al. (2009) Self-organization of the Escherichia coli chemotaxis network imaged with super-resolution light microscopy. PLoS Biol 7(6):e1000137.
    • (2009) PLoS Biol , vol.7 , Issue.6
    • Greenfield, D.1
  • 61
    • 84879693202 scopus 로고    scopus 로고
    • How crowded is the prokaryotic cytoplasm?
    • Spitzer J, Poolman B (2013) How crowded is the prokaryotic cytoplasm? FEBS Lett 587(14): 2094-2098.
    • (2013) FEBS Lett , vol.587 , Issue.14 , pp. 2094-2098
    • Spitzer, J.1    Poolman, B.2
  • 62
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and betacarbon resonances in proteins
    • Wittekind M, Mueller L (1993) HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and betacarbon resonances in proteins. J Magn Reson B 101(2): 201-205.
    • (1993) J Magn Reson B , vol.101 , Issue.2 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 63
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S, Bax A (1992) Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114: 6291-6293.
    • (1992) J Am Chem Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 64
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, et al. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6(3): 277-293.
    • (1995) J Biomol NMR , vol.6 , Issue.3 , pp. 277-293
    • Delaglio, F.1
  • 65
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA (1994) NMR View: A computer program for the visualization and analysis of NMR data. J Biomol NMR 4(5): 603-614.
    • (1994) J Biomol NMR , vol.4 , Issue.5 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 66
    • 0020346954 scopus 로고
    • Solvent isotope effects of enzyme systems
    • Schowen KB, Schowen RL (1982) Solvent isotope effects of enzyme systems. Methods Enzymol 87: 551-606.
    • (1982) Methods Enzymol , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 67
    • 84860833500 scopus 로고    scopus 로고
    • Reorganizing the protein space at the Universal Protein Resource (UniProt)
    • The UniProt Consortium
    • The UniProt Consortium (2012) Reorganizing the protein space at the Universal Protein Resource (UniProt). Nucleic Acids Res 40 (Database issue):D71-D75.
    • (2012) Nucleic Acids Res , vol.40 , Issue.DATABASE ISSUE


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.