메뉴 건너뛰기




Volumn 111, Issue 31, 2014, Pages 11335-11340

Erratum: Residue level quantification of protein stability in living cells (Proceedings of the National Academy of Sciences of the United States of America (2014) 111 (11335-11340) DOI 10.1073/pnas.1406845111);Residue level quantification of protein stability in living cells

Author keywords

H D exchange; Macromolecular crowding; Protein NMR; Protein thermodynamics

Indexed keywords

GLOBULAR PROTEIN; PROTEIN G;

EID: 84905652881     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1521913112     Document Type: Erratum
Times cited : (102)

References (73)
  • 1
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis RJ (2001) Macromolecular crowding: An important but neglected aspect of the intracellular environment. Curr Opin Struct Biol 11(1):114-119.
    • (2001) Curr Opin Struct Biol , vol.11 , Issue.1 , pp. 114-119
    • Ellis, R.J.1
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • Ellis RJ (2001) Macromolecular crowding: Obvious but underappreciated. Trends Biochem Sci 26(10):597-604.
    • (2001) Trends Biochem Sci , vol.26 , Issue.10 , pp. 597-604
    • Ellis, R.J.1
  • 5
    • 80052479046 scopus 로고    scopus 로고
    • Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells
    • Dhar A, et al. (2011) Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells. Biophys J 101(2):421-430.
    • (2011) Biophys J , vol.101 , Issue.2 , pp. 421-430
    • Dhar, A.1
  • 6
    • 77951643591 scopus 로고    scopus 로고
    • Protein folding stability and dynamics imaged in a living cell
    • Ebbinghaus S, Dhar A, McDonald JD, Gruebele M (2010) Protein folding stability and dynamics imaged in a living cell. Nat Methods 7(4):319-323.
    • (2010) Nat Methods , vol.7 , Issue.4 , pp. 319-323
    • Ebbinghaus, S.1    Dhar, A.2    McDonald, J.D.3    Gruebele, M.4
  • 7
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • DOI 10.1038/nsb1001-879
    • Ghaemmaghami S, Oas TG (2001) Quantitative protein stability measurement in vivo. Nat Struct Biol 8(10):879-882. (Pubitemid 32923608)
    • (2001) Nature Structural Biology , vol.8 , Issue.10 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 9
    • 84890856805 scopus 로고    scopus 로고
    • The extracellular protein VlsE is destabilized inside cells
    • Guzman I, Gelman H, Tai J, Gruebele M (2014) The extracellular protein VlsE is destabilized inside cells. J Mol Biol 426(1):11-20.
    • (2014) J Mol Biol , vol.426 , Issue.1 , pp. 11-20
    • Guzman, I.1    Gelman, H.2    Tai, J.3    Gruebele, M.4
  • 10
    • 78651138927 scopus 로고
    • The interaction between polysaccharides and other macromolecules. 5. The solubility of proteins in the presence of dextran
    • Laurent TC (1963) The interaction between polysaccharides and other macromolecules. 5. The solubility of proteins in the presence of dextran. Biochem J 89:253-257.
    • (1963) Biochem J , vol.89 , pp. 253-257
    • Laurent, T.C.1
  • 11
    • 0020668187 scopus 로고
    • The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences
    • Minton AP (1983) The effect of volume occupancy upon the thermodynamic activity of proteins: Some biochemical consequences. Mol Cell Biochem 55(2):119-140.
    • (1983) Mol Cell Biochem , vol.55 , Issue.2 , pp. 119-140
    • Minton, A.P.1
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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
  • 17
    • 84877926338 scopus 로고    scopus 로고
    • 2+-calmodulin in E. Coli lysate
    • 2+-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
  • 18
    • 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 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
  • 23
    • 84890860233 scopus 로고    scopus 로고
    • Deciphering protein stability in cells
    • Gershenson A (2014) Deciphering protein stability in cells. J Mol Biol 426(1):4-6.
    • (2014) J Mol Biol , vol.426 , Issue.1 , pp. 4-6
    • Gershenson, A.1
  • 24
  • 25
    • 84874843784 scopus 로고    scopus 로고
    • Reduced native state stability in crowded cellular environment due to protein-protein interactions
    • Harada R, Tochio N, Kigawa T, Sugita Y, Feig M (2013) Reduced native state stability in crowded cellular environment due to protein-protein interactions. J Am Chem Soc 135(9):3696-3701.
    • (2013) J Am Chem Soc , vol.135 , Issue.9 , pp. 3696-3701
    • Harada, R.1    Tochio, N.2    Kigawa, T.3    Sugita, Y.4    Feig, M.5
  • 26
    • 84888376873 scopus 로고    scopus 로고
    • Impact of reconstituted cytosol on protein stability
    • Sarkar M, Smith AE, Pielak GJ (2013) Impact of reconstituted cytosol on protein stability. Proc Natl Acad Sci USA 110(48):19342-19347.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.48 , pp. 19342-19347
    • Sarkar, M.1    Smith, A.E.2    Pielak, G.J.3
  • 27
    • 0022545967 scopus 로고
    • Gene for an immunoglobulin-binding protein from a group G streptococcus
    • Fahnestock SR, Alexander P, Nagle J, Filpula D (1986) Gene for an immunoglobulinbinding protein from a group G streptococcus. J Bacteriol 167(3):870-880. (Pubitemid 16045020)
    • (1986) Journal of Bacteriology , vol.167 , Issue.3 , pp. 870-880
    • Fahnestock, S.R.1    Alexander, P.2    Nagle, J.3    Filpula, D.4
  • 29
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures
    • Alexander P, Fahnestock S, Lee T, Orban J, Bryan P (1992) Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures. Biochemistry 31(14):3597-3603.
    • (1992) Biochemistry , vol.31 , Issue.14 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 30
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G
    • Alexander P, Orban J, Bryan P (1992) Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G. Biochemistry 31(32): 7243-7248.
    • (1992) Biochemistry , vol.31 , Issue.32 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 32
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher T, Alexander P, Bryan P, Gilliland GL (1994) Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33(15):4721-4729. (Pubitemid 24145123)
    • (1994) Biochemistry , vol.33 , Issue.15 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 33
    • 0028810974 scopus 로고
    • Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: Comparison with calorimetric data
    • Orban J, Alexander P, Bryan P, Khare D (1995) Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: Comparison with calorimetric data. Biochemistry 34(46):15291-15300.
    • (1995) Biochemistry , vol.34 , Issue.46 , pp. 15291-15300
    • Orban, J.1    Alexander, P.2    Bryan, P.3    Khare, D.4
  • 34
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L (1994) A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry 33(18):5510-5517.
    • (1994) Biochemistry , vol.33 , Issue.18 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 35
    • 0028578686 scopus 로고
    • Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G
    • Kuszewski J, Clore GM, Gronenborn AM (1994) Fast folding of a prototypic polypeptide: The immunoglobulin binding domain of streptococcal protein G. Protein Sci 3(11):1945-1952.
    • (1994) Protein Sci , vol.3 , Issue.11 , pp. 1945-1952
    • Kuszewski, J.1    Clore, G.M.2    Gronenborn, A.M.3
  • 36
    • 0032867418 scopus 로고    scopus 로고
    • Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing
    • DOI 10.1038/13311
    • Park S-H, Shastry MCR, Roder H (1999) Folding dynamics of the B1 domain of protein G explored by ultrarapid mixing. Nat Struct Biol 6(10):943-947. (Pubitemid 29463308)
    • (1999) Nature Structural Biology , vol.6 , Issue.10 , pp. 943-947
    • Park, S.-H.1    Shastry, M.C.R.2    Roder, H.3
  • 37
    • 0036440985 scopus 로고    scopus 로고
    • Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
    • DOI 10.1016/S0022-2836(02)01029-X
    • Krantz BA, Mayne L, Rumbley J, Englander SW, Sosnick TR (2002) Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. J Mol Biol 324(2):359-371. (Pubitemid 35379034)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.2 , pp. 359-371
    • Krantz, B.A.1    Mayne, L.2    Rumbley, J.3    Englander, S.W.4    Sosnick, T.R.5
  • 38
    • 80054705419 scopus 로고    scopus 로고
    • GB1 is not a two-state folder: Identification and characterization of an on-pathway intermediate
    • Morrone A, et al. (2011) GB1 is not a two-state folder: Identification and characterization of an on-pathway intermediate. Biophys J 101(8):2053-2060.
    • (2011) Biophys J , vol.101 , Issue.8 , pp. 2053-2060
    • Morrone, A.1
  • 39
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • Pace CN (1990) Measuring and increasing protein stability. Trends Biotechnol 8(4):93-98.
    • (1990) Trends Biotechnol , vol.8 , Issue.4 , pp. 93-98
    • Pace, C.N.1
  • 41
    • 0035928606 scopus 로고    scopus 로고
    • Hydrogen exchange in peptides and proteins using NMR spectroscopy
    • Dempsey CE (2001) Hydrogen exchange in peptides and proteins using NMR spectroscopy. Prog Nucl Magn Reson Spectrosc 39:135-170.
    • (2001) Prog Nucl Magn Reson Spectrosc , vol.39 , pp. 135-170
    • Dempsey, C.E.1
  • 42
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt A, Nielsen SO (1966) Hydrogen exchange in proteins. Adv Protein Chem 21:287-386.
    • (1966) Adv Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 44
    • 0003776016 scopus 로고
    • PhD thesis (Structural Biology and Molecular Biophysics, University of Pennsylvania, Philadelphia). Available at Accessed July 7, 2014
    • Zhang Y-Z (1995) Protein and peptide structure and interactions studied by hydrogen exchange and NMR. PhD thesis (Structural Biology and Molecular Biophysics, University of Pennsylvania, Philadelphia). Available at www.fccc.edu/research/labs/roder/sphere/. Accessed July 7, 2014.
    • (1995) Protein and Peptide Structure and Interactions Studied by Hydrogen Exchange and NMR
    • Zhang, Y.-Z.1
  • 45
    • 1642535628 scopus 로고    scopus 로고
    • EX1 Hydrogen Exchange and Protein Folding
    • DOI 10.1021/bi035943y
    • Ferraro DM, Lazo N, Robertson AD (2004) EX1 hydrogen exchange and protein folding. Biochemistry 43(3):587-594. (Pubitemid 38114045)
    • (2004) Biochemistry , vol.43 , Issue.3 , pp. 587-594
    • Ferraro, D.M.1    Robertson, A.D.2
  • 46
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander SW, Mayne L (1992) Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21:243-265.
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 47
    • 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
  • 48
    • 0031908874 scopus 로고    scopus 로고
    • Hydrogen exchange studies of protein structure
    • DOI 10.1016/S0958-1669(98)80088-8
    • Raschke TM, Marqusee S (1998) Hydrogen exchange studies of protein structure. Curr Opin Biotechnol 9(1):80-86. (Pubitemid 28098319)
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.1 , pp. 80-86
    • Raschke, T.M.1    Marqusee, S.2
  • 50
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW (1995) Protein folding intermediates: Native-state hydrogen exchange. Science 269(5221):192-197.
    • (1995) Science , vol.269 , Issue.5221 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 51
    • 61949243261 scopus 로고    scopus 로고
    • High-resolution multi-dimensional NMR spectroscopy of proteins in human cells
    • Inomata K, et al. (2009) High-resolution multi-dimensional NMR spectroscopy of proteins in human cells. Nature 458(7234):106-109.
    • (2009) Nature , vol.458 , Issue.7234 , pp. 106-109
    • Inomata, K.1
  • 53
    • 77955676884 scopus 로고    scopus 로고
    • 1H exchange to assess macromolecular crowding effects on globular-protein stability
    • 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
  • 54
    • 23744476746 scopus 로고    scopus 로고
    • Multidimensional NMR spectroscopy for protein characterization and assignment inside cells
    • DOI 10.1021/ja053145k
    • Reardon PN, Spicer LD (2005) Multidimensional NMR spectroscopy for protein characterization and assignment inside cells. J Am Chem Soc 127(31):10848-10849. (Pubitemid 41129858)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.31 , pp. 10848-10849
    • Reardon, P.N.1    Spicer, L.D.2
  • 55
    • 84898071694 scopus 로고    scopus 로고
    • Strategies for protein NMR in Escherichia coli
    • Xu G, et al. (2014) Strategies for protein NMR in Escherichia coli. Biochemistry 53(12):1971-1981.
    • (2014) Biochemistry , vol.53 , Issue.12 , pp. 1971-1981
    • Xu, G.1
  • 57
    • 0030566807 scopus 로고    scopus 로고
    • Core mutants of the immunoglobulin binding domain of streptococcal protein G: Stability and structural integrity
    • DOI 10.1016/S0014-5793(96)01262-8, PII S0014579396012628
    • Gronenborn AM, Frank MK, Clore GM (1996) Core mutants of the immunoglobulin binding domain of streptococcal protein G: Stability and structural integrity. FEBS Lett 398(2-3):312-316. (Pubitemid 26414332)
    • (1996) FEBS Letters , vol.398 , Issue.2-3 , pp. 312-316
    • Gronenborn, A.M.1    Frank, M.K.2    Clore, G.M.3
  • 58
    • 33646186493 scopus 로고    scopus 로고
    • Salting the charged surface: PH and salt dependence of protein G B1 stability
    • Lindman S, et al. (2006) Salting the charged surface: pH and salt dependence of protein G B1 stability. Biophys J 90(8):2911-2921.
    • (2006) Biophys J , vol.90 , Issue.8 , pp. 2911-2921
    • Lindman, S.1
  • 59
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel WJ, Schellman JA (1987) Protein stability curves. Biopolymers 26(11): 1859 - 1877.
    • (1987) Biopolymers , vol.26 , Issue.11 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 60
    • 0032876680 scopus 로고    scopus 로고
    • Protein conformational stabilities can be determined from hydrogen exchange rates
    • DOI 10.1038/13273
    • Huyghues-Despointes BMP, Scholtz JM, Pace CN (1999) Protein conformational stabilities can be determined from hydrogen exchange rates. Nat Struct Biol 6(10):910-912. (Pubitemid 29463301)
    • (1999) Nature Structural Biology , vol.6 , Issue.10 , pp. 910-912
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Pace, C.N.3
  • 61
    • 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
  • 62
    • 0015514380 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Molday RS, Englander SW, Kallen RG (1972) Primary structure effects on peptide group hydrogen exchange. Biochemistry 11(2):150-158.
    • (1972) Biochemistry , vol.11 , Issue.2 , pp. 150-158
    • Molday, R.S.1    Englander, S.W.2    Kallen, R.G.3
  • 63
    • 84868130708 scopus 로고    scopus 로고
    • Temperature dependence of protein folding kinetics in living cells
    • Guo M, Xu Y, Gruebele M (2012) Temperature dependence of protein folding kinetics in living cells. Proc Natl Acad Sci USA 109(44):17863-17867.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.44 , pp. 17863-17867
    • Guo, M.1    Xu, Y.2    Gruebele, M.3
  • 64
    • 61949315876 scopus 로고    scopus 로고
    • Protein structure determination in living cells by in-cell NMR spectroscopy
    • Sakakibara D, et al. (2009) Protein structure determination in living cells by in-cell NMR spectroscopy. Nature 458(7234):102-105.
    • (2009) Nature , vol.458 , Issue.7234 , pp. 102-105
    • Sakakibara, D.1
  • 65
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards FM (1977) Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng 6:151-176.
    • (1977) Annu Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 66
    • 66749128608 scopus 로고    scopus 로고
    • The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence
    • Spitzer J, Poolman B (2009) The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence. Microbiol Mol Biol Rev 73(2):371-388.
    • (2009) Microbiol Mol Biol Rev , vol.73 , Issue.2 , pp. 371-388
    • Spitzer, J.1    Poolman, B.2
  • 68
    • 84876033838 scopus 로고    scopus 로고
    • Protein dynamics in living cells studied by in-cell NMR spectroscopy
    • Li C, Liu M (2013) Protein dynamics in living cells studied by in-cell NMR spectroscopy. FEBS Lett 587(8):1008-1011.
    • (2013) FEBS Lett , vol.587 , Issue.8 , pp. 1008-1011
    • Li, C.1    Liu, M.2
  • 70
    • 84899021008 scopus 로고    scopus 로고
    • Protein crowder charge and protein stability
    • Sarkar M, Lu J, Pielak GJ (2014) Protein crowder charge and protein stability. Biochemistry 53(10):1601-1606.
    • (2014) Biochemistry , vol.53 , Issue.10 , pp. 1601-1606
    • Sarkar, M.1    Lu, J.2    Pielak, G.J.3
  • 71
    • 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
  • 72
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe PK, Long FA (1960) Use of glass electrodes to measure acidities in deuterium oxide. J Phys Chem B 64(1):188-190.
    • (1960) J Phys Chem B , vol.64 , Issue.1 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 73
    • 0042121261 scopus 로고    scopus 로고
    • POPS: A fast algorithm for solvent accessible surface areas at atomic and residue level
    • DOI 10.1093/nar/gkg601
    • Cavallo L, Kleinjung J, Fraternali F (2003) POPS: A fast algorithm for solvent accessible surface areas at atomic and residue level. Nucleic Acids Research 31(13):3364-3366. (Pubitemid 37442160)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3364-3366
    • Cavallo, L.1    Kleinjung, J.2    Fraternali, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.