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Volumn 112, Issue 21, 2015, Pages E2775-E2784

A hypothesis to reconcile the physical and chemical unfolding of proteins

Author keywords

Hydrostatic; NMR; Protein folding; SAXS; Urea

Indexed keywords

PROTEIN; UREA; WATER; ABELSON KINASE; FUNGAL PROTEIN;

EID: 84930227070     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1500352112     Document Type: Article
Times cited : (76)

References (77)
  • 1
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C (1968) Are there pathways for protein folding? J Chim Phys 65(1):44-45.
    • (1968) J Chim Phys , vol.65 , Issue.1 , pp. 44-45
    • Levinthal, C.1
  • 4
    • 0042666825 scopus 로고    scopus 로고
    • Fibrillar aggregates of the tumor suppressor p53 core domain
    • Ishimaru D, et al. (2003) Fibrillar aggregates of the tumor suppressor p53 core domain. Biochemistry 42(30):9022-9027.
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 9022-9027
    • Ishimaru, D.1
  • 5
    • 84864999268 scopus 로고    scopus 로고
    • Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: Implications for cancer
    • Ano Bom APD, et al. (2012) Mutant p53 aggregates into prion-like amyloid oligomers and fibrils: Implications for cancer. J Biol Chem 287(33):28152-28162.
    • (2012) J Biol Chem , vol.287 , Issue.33 , pp. 28152-28162
    • Ano Bom, A.P.D.1
  • 7
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 8
    • 77249149930 scopus 로고    scopus 로고
    • Ligand binding and hydration in protein misfolding: Insights from studies of prion and p53 tumor suppressor proteins
    • Silva JL, et al. (2010) Ligand binding and hydration in protein misfolding: Insights from studies of prion and p53 tumor suppressor proteins. Acc Chem Res 43(2):271-279.
    • (2010) Acc Chem Res , vol.43 , Issue.2 , pp. 271-279
    • Silva, J.L.1
  • 9
    • 0001435569 scopus 로고
    • The coagulation of albumen by pressure
    • Bridgman PW (1914) The coagulation of albumen by pressure. J Biol Chem 19:511-512.
    • (1914) J Biol Chem , vol.19 , pp. 511-512
    • Bridgman, P.W.1
  • 10
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva JL, Weber G (1993) Pressure stability of proteins. Annu Rev Phys Chem 44:89-113.
    • (1993) Annu Rev Phys Chem , vol.44 , pp. 89-113
    • Silva, J.L.1    Weber, G.2
  • 11
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva JL, Foguel D, Royer CA (2001) Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem Sci 26(10):612-618.
    • (2001) Trends Biochem Sci , vol.26 , Issue.10 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 12
    • 84921998460 scopus 로고    scopus 로고
    • High-pressure chemical biology and biotechnology
    • Silva JL, et al. (2014) High-pressure chemical biology and biotechnology. Chem Rev 114(14):7239-7267.
    • (2014) Chem Rev , vol.114 , Issue.14 , pp. 7239-7267
    • Silva, J.L.1
  • 13
    • 84876518318 scopus 로고    scopus 로고
    • Exploring the folding energy landscape with pressure
    • Akasaka K, Kitahara R, Kamatari YO (2013) Exploring the folding energy landscape with pressure. Arch Biochem Biophys 531(1-2):110-115.
    • (2013) Arch Biochem Biophys , vol.531 , Issue.1-2 , pp. 110-115
    • Akasaka, K.1    Kitahara, R.2    Kamatari, Y.O.3
  • 14
    • 84860829715 scopus 로고    scopus 로고
    • Cavities determine the pressure unfolding of proteins
    • Roche J, et al. (2012) Cavities determine the pressure unfolding of proteins. Proc Natl Acad Sci USA 109(18):6945-6950.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.18 , pp. 6945-6950
    • Roche, J.1
  • 15
    • 0037154268 scopus 로고    scopus 로고
    • Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse
    • Cheung MS, García AE, Onuchic JN (2002) Protein folding mediated by solvation: Water expulsion and formation of the hydrophobic core occur after the structural collapse. Proc Natl Acad Sci USA 99(2):685-690.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.2 , pp. 685-690
    • Cheung, M.S.1    García, A.E.2    Onuchic, J.N.3
  • 16
    • 33646918845 scopus 로고    scopus 로고
    • Probing protein folding and conformational transitions with fluorescence
    • Royer CA (2006) Probing protein folding and conformational transitions with fluorescence. Chem Rev 106(5):1769-1784.
    • (2006) Chem Rev , vol.106 , Issue.5 , pp. 1769-1784
    • Royer, C.A.1
  • 17
    • 0037171130 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in high-pressure studies on proteins
    • Dzwolak W, Kato M, Taniguchi Y (2002) Fourier transform infrared spectroscopy in high-pressure studies on proteins. Biochim Biophys Acta 1595(1-2):131-144.
    • (2002) Biochim Biophys Acta , vol.1595 , Issue.1-2 , pp. 131-144
    • Dzwolak, W.1    Kato, M.2    Taniguchi, Y.3
  • 18
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • Akasaka K (2006) Probing conformational fluctuation of proteins by pressure perturbation. Chem Rev 106(5):1814-1835.
    • (2006) Chem Rev , vol.106 , Issue.5 , pp. 1814-1835
    • Akasaka, K.1
  • 19
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104(8):3607-3622.
    • (2004) Chem Rev , vol.104 , Issue.8 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 20
    • 0037171184 scopus 로고    scopus 로고
    • Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure
    • Winter R (2002) Synchrotron X-ray and neutron small-angle scattering of lyotropic lipid mesophases, model biomembranes and proteins in solution at high pressure. Biochim Biophys Acta 1595(1-2):160-184.
    • (2002) Biochim Biophys Acta , vol.1595 , Issue.1-2 , pp. 160-184
    • Winter, R.1
  • 21
    • 78649241433 scopus 로고    scopus 로고
    • High-pressure SAXS study of folded and unfolded ensembles of proteins
    • Schroer MA, et al. (2010) High-pressure SAXS study of folded and unfolded ensembles of proteins. Biophys J 99(10):3430-3437.
    • (2010) Biophys J , vol.99 , Issue.10 , pp. 3430-3437
    • Schroer, M.A.1
  • 22
    • 84896541599 scopus 로고    scopus 로고
    • Observation of complete pressure-jump protein refolding in molecular dynamics simulation and experiment
    • Liu Y, Prigozhin MB, Schulten K, Gruebele M (2014) Observation of complete pressure-jump protein refolding in molecular dynamics simulation and experiment. JAm Chem Soc 136(11):4265-4272.
    • (2014) J Am Chem Soc , vol.136 , Issue.11 , pp. 4265-4272
    • Liu, Y.1    Prigozhin, M.B.2    Schulten, K.3    Gruebele, M.4
  • 23
    • 84889671229 scopus 로고    scopus 로고
    • Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin
    • Lerch MT, Horwitz J, McCoy J, Hubbell WL (2013) Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin. Proc Natl Acad Sci USA 110(49):E4714-E4722.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.49 , pp. E4714-E4722
    • Lerch, M.T.1    Horwitz, J.2    McCoy, J.3    Hubbell, W.L.4
  • 24
    • 84872109999 scopus 로고    scopus 로고
    • Insights into the intramolecular coupling between the N- and C-domains of troponin C derived from high-pressure, fluorescence, nuclear magnetic resonance, and small-angle X-ray scattering studies
    • de Oliveira GAP, et al. (2013) Insights into the intramolecular coupling between the N- and C-domains of troponin C derived from high-pressure, fluorescence, nuclear magnetic resonance, and small-angle X-ray scattering studies. Biochemistry 52(1):28-40.
    • (2013) Biochemistry , vol.52 , Issue.1 , pp. 28-40
    • De Oliveira, G.A.P.1
  • 25
    • 84884760040 scopus 로고    scopus 로고
    • Intramolecular dynamics within the N-Cap-SH3-SH2 regulatory unit of the c-Abl tyrosine kinase reveal targeting to the cellular membrane
    • de Oliveira GAP, et al. (2013) Intramolecular dynamics within the N-Cap-SH3-SH2 regulatory unit of the c-Abl tyrosine kinase reveal targeting to the cellular membrane. J Biol Chem 288(39):28331-28345.
    • (2013) J Biol Chem , vol.288 , Issue.39 , pp. 28331-28345
    • De Oliveira, G.A.P.1
  • 26
    • 77956190770 scopus 로고    scopus 로고
    • Structural characterization of proteins and complexes using small-angle X-ray solution scattering
    • Mertens HDT, Svergun DI (2010) Structural characterization of proteins and complexes using small-angle X-ray solution scattering. J Struct Biol 172(1):128-141.
    • (2010) J Struct Biol , vol.172 , Issue.1 , pp. 128-141
    • Mertens, H.D.T.1    Svergun, D.I.2
  • 27
    • 70349289438 scopus 로고    scopus 로고
    • Urea-mediated protein denaturation: A consensus view
    • Das A, Mukhopadhyay C (2009) Urea-mediated protein denaturation: A consensus view. J Phys Chem B 113(38):12816-12824.
    • (2009) J Phys Chem B , vol.113 , Issue.38 , pp. 12816-12824
    • Das, A.1    Mukhopadhyay, C.2
  • 28
    • 79952860125 scopus 로고    scopus 로고
    • Comment on "urea-mediated protein denaturation: A consensus view."
    • discussion 1327-1328
    • Zhou R, Li J, Hua L, Yang Z, Berne BJ (2011) Comment on "urea-mediated protein denaturation: A consensus view." J Phys Chem B 115(5):1323-1326, discussion 1327-1328.
    • (2011) J Phys Chem B , vol.115 , Issue.5 , pp. 1323-1326
    • Zhou, R.1    Li, J.2    Hua, L.3    Yang, Z.4    Berne, B.J.5
  • 29
    • 55949131241 scopus 로고    scopus 로고
    • Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
    • Hua L, Zhou R, Thirumalai D, Berne BJ (2008) Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding. Proc Natl Acad Sci USA 105(44):16928-16933.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.44 , pp. 16928-16933
    • Hua, L.1    Zhou, R.2    Thirumalai, D.3    Berne, B.J.4
  • 30
    • 77749285768 scopus 로고    scopus 로고
    • Equilibrium study of protein denaturation by urea
    • Canchi DR, Paschek D, García AE (2010) Equilibrium study of protein denaturation by urea. J Am Chem Soc 132(7):2338-2344.
    • (2010) J Am Chem Soc , vol.132 , Issue.7 , pp. 2338-2344
    • Canchi, D.R.1    Paschek, D.2    García, A.E.3
  • 31
    • 80054717093 scopus 로고    scopus 로고
    • Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer
    • Guinn EJ, Pegram LM, Capp MW, Pollock MN, Record MT, Jr (2011) Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer. Proc Natl Acad Sci USA 108(41):16932-16937.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.41 , pp. 16932-16937
    • Guinn, E.J.1    Pegram, L.M.2    Capp, M.W.3    Pollock, M.N.4    Record, M.T.5
  • 32
    • 27244437952 scopus 로고    scopus 로고
    • Predicting the energetics of osmolyte-induced protein folding/unfolding
    • Auton M, Bolen DW (2005) Predicting the energetics of osmolyte-induced protein folding/unfolding. Proc Natl Acad Sci USA 102(42):15065-15068.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.42 , pp. 15065-15068
    • Auton, M.1    Bolen, D.W.2
  • 33
    • 34848916114 scopus 로고    scopus 로고
    • Anatomy of energetic changes accompanying urea-induced protein denaturation
    • Auton M, Holthauzen LMF, Bolen DW (2007) Anatomy of energetic changes accompanying urea-induced protein denaturation. Proc Natl Acad Sci USA 104(39):15317-15322.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.39 , pp. 15317-15322
    • Auton, M.1    Holthauzen, L.M.F.2    Bolen, D.W.3
  • 34
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion BJ, Daggett V (2003) The molecular basis for the chemical denaturation of proteins by urea. Proc Natl Acad Sci USA 100(9):5142-5147.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.9 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 35
    • 63149153986 scopus 로고    scopus 로고
    • Urea's action on hydrophobic interactions
    • Zangi R, Zhou R, Berne BJ (2009) Urea's action on hydrophobic interactions. J Am Chem Soc 131(4):1535-1541.
    • (2009) J Am Chem Soc , vol.131 , Issue.4 , pp. 1535-1541
    • Zangi, R.1    Zhou, R.2    Berne, B.J.3
  • 36
    • 0032080534 scopus 로고    scopus 로고
    • Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect
    • Zou Q, Habermann-Rottinghaus SM, Murphy KP (1998) Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect. Proteins 31(2):107-115.
    • (1998) Proteins , vol.31 , Issue.2 , pp. 107-115
    • Zou, Q.1    Habermann-Rottinghaus, S.M.2    Murphy, K.P.3
  • 37
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride. A calorimetric study
    • Makhatadze GI, Privalov PL (1992) Protein interactions with urea and guanidinium chloride. A calorimetric study. J Mol Biol 226(2):491-505.
    • (1992) J Mol Biol , vol.226 , Issue.2 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 38
    • 62449341938 scopus 로고    scopus 로고
    • Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
    • Lim WK, Rösgen J, Englander SW (2009) Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group. Proc Natl Acad Sci USA 106(8):2595-2600.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.8 , pp. 2595-2600
    • Lim, W.K.1    Rösgen, J.2    Englander, S.W.3
  • 39
    • 78651119214 scopus 로고
    • The solubility of amino acids and related compounds in aqueous urea solutions
    • Nozaki Y, Tanford C (1963) The solubility of amino acids and related compounds in aqueous urea solutions. J Biol Chem 238(12):4074-4081.
    • (1963) J Biol Chem , vol.238 , Issue.12 , pp. 4074-4081
    • Nozaki, Y.1    Tanford, C.2
  • 40
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang A, Bolen DW (1997) A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry 36(30):9101-9108.
    • (1997) Biochemistry , vol.36 , Issue.30 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 41
    • 33947488954 scopus 로고
    • Isothermal unfolding of globular proteins in aqueous urea solutions
    • Tanford C (1964) Isothermal unfolding of globular proteins in aqueous urea solutions. J Am Chem Soc 86(10):2050-2059.
    • (1964) J Am Chem Soc , vol.86 , Issue.10 , pp. 2050-2059
    • Tanford, C.1
  • 42
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C (1970) Protein denaturation. C. Theoretical models for the mechanism of denaturation. Adv Protein Chem 24:1-95.
    • (1970) Adv Protein Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 43
    • 33845287229 scopus 로고    scopus 로고
    • Implications of protein conformational diversity for binding and development of new biological active compounds
    • Valente AP, Miyamoto CA, Almeida FCL (2006) Implications of protein conformational diversity for binding and development of new biological active compounds. Curr Med Chem 13(30):3697-3703.
    • (2006) Curr Med Chem , vol.13 , Issue.30 , pp. 3697-3703
    • Valente, A.P.1    Miyamoto, C.A.2    Almeida, F.C.L.3
  • 44
    • 84866664462 scopus 로고    scopus 로고
    • Moniliophthora perniciosa necrosis- and ethyleneinducing protein 2 (MpNep2) as a metastable dimer in solution: Structural and functional implications
    • de Oliveira GA, et al. (2012) Moniliophthora perniciosa necrosis- and ethyleneinducing protein 2 (MpNep2) as a metastable dimer in solution: Structural and functional implications. PLoS One 7(9):e45620.
    • (2012) PLoS One , vol.7 , Issue.9 , pp. e45620
    • De Oliveira, G.A.1
  • 45
    • 0034824155 scopus 로고    scopus 로고
    • Response of native and denatured hen lysozyme to high pressure studied by15 N/1 H NMR spectroscopy
    • Kamatari YO, et al. (2001) Response of native and denatured hen lysozyme to high pressure studied by15 N/1 H NMR spectroscopy. Eur J Biochem 268(6):1782-1793.
    • (2001) Eur J Biochem , vol.268 , Issue.6 , pp. 1782-1793
    • Kamatari, Y.O.1
  • 46
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
    • Li H, Yamada H, Akasaka K (1998) Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 37(5):1167-1173.
    • (1998) Biochemistry , vol.37 , Issue.5 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 47
    • 84880167453 scopus 로고    scopus 로고
    • Using chemical shift perturbation to characterise ligand binding
    • Williamson MP (2013) Using chemical shift perturbation to characterise ligand binding. Prog Nucl Magn Reson Spectrosc 73:1-16.
    • (2013) Prog Nucl Magn Reson Spectrosc , vol.73 , pp. 1-16
    • Williamson, M.P.1
  • 48
    • 77951214658 scopus 로고    scopus 로고
    • McVol - A program for calculating protein volumes and identifying cavities by a Monte Carlo algorithm
    • Till MS, Ullmann GM (2010) McVol - a program for calculating protein volumes and identifying cavities by a Monte Carlo algorithm. J Mol Model 16(3):419-429.
    • (2010) J Mol Model , vol.16 , Issue.3 , pp. 419-429
    • Till, M.S.1    Ullmann, G.M.2
  • 49
    • 80755156284 scopus 로고    scopus 로고
    • The crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of cacao's Witches' Broom disease reveals key elements for its activity
    • Zaparoli G, et al. (2011) The crystal structure of necrosis- and ethylene-inducing protein 2 from the causal agent of cacao's Witches' Broom disease reveals key elements for its activity. Biochemistry 50(45):9901-9910.
    • (2011) Biochemistry , vol.50 , Issue.45 , pp. 9901-9910
    • Zaparoli, G.1
  • 50
    • 0026541905 scopus 로고
    • Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor
    • Silva JL, Silveira CF, Correia Júnior A, Pontes L (1992) Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor. J Mol Biol 223(2):545-555.
    • (1992) J Mol Biol , vol.223 , Issue.2 , pp. 545-555
    • Silva, J.L.1    Silveira, C.F.2    Correia, A.3    Pontes, L.4
  • 51
    • 0027405350 scopus 로고
    • Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy
    • Peng X, Jonas J, Silva JL (1993) Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy. Proc Natl Acad Sci USA 90(5):1776-1780.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.5 , pp. 1776-1780
    • Peng, X.1    Jonas, J.2    Silva, J.L.3
  • 52
    • 84870222249 scopus 로고    scopus 로고
    • Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations
    • Roche J, et al. (2012) Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations. Biochemistry 51(47):9535-9546.
    • (2012) Biochemistry , vol.51 , Issue.47 , pp. 9535-9546
    • Roche, J.1
  • 53
    • 84885120689 scopus 로고    scopus 로고
    • Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy
    • Roche J, et al. (2013) Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy. J Am Chem Soc 135(39):14610-14618.
    • (2013) J Am Chem Soc , vol.135 , Issue.39 , pp. 14610-14618
    • Roche, J.1
  • 54
    • 0027268092 scopus 로고
    • Reversible pressure dissociation of R17 bacteriophage. The physical individuality of virus particles
    • Da Poian AT, Oliveira AC, Gaspar LP, Silva JL, Weber G (1993) Reversible pressure dissociation of R17 bacteriophage. The physical individuality of virus particles. J Mol Biol 231(4):999-1008.
    • (1993) J Mol Biol , vol.231 , Issue.4 , pp. 999-1008
    • Da Poian, A.T.1    Oliveira, A.C.2    Gaspar, L.P.3    Silva, J.L.4    Weber, G.5
  • 55
    • 0030031616 scopus 로고    scopus 로고
    • Concentration dependence of the subunit association of oligomers and viruses and the modification of the latter by urea binding
    • Weber G, Da Poian AT, Silva JL (1996) Concentration dependence of the subunit association of oligomers and viruses and the modification of the latter by urea binding. Biophys J 70(1):167-173.
    • (1996) Biophys J , vol.70 , Issue.1 , pp. 167-173
    • Weber, G.1    Da Poian, A.T.2    Silva, J.L.3
  • 56
    • 0036291143 scopus 로고    scopus 로고
    • High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded
    • Kitahara R, Yamada H, Akasaka K, Wright PE (2002) High pressure NMR reveals that apomyoglobin is an equilibrium mixture from the native to the unfolded. J Mol Biol 320(2):311-319.
    • (2002) J Mol Biol , vol.320 , Issue.2 , pp. 311-319
    • Kitahara, R.1    Yamada, H.2    Akasaka, K.3    Wright, P.E.4
  • 57
    • 3242789489 scopus 로고    scopus 로고
    • Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
    • Mohana-Borges R, Goto NK, Kroon GJ, Dyson HJ, Wright PE (2004) Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings. J Mol Biol 340(5):1131-1142.
    • (2004) J Mol Biol , vol.340 , Issue.5 , pp. 1131-1142
    • Mohana-Borges, R.1    Goto, N.K.2    Kroon, G.J.3    Dyson, H.J.4    Wright, P.E.5
  • 58
    • 0038219554 scopus 로고    scopus 로고
    • Role of hydration in the closed-to-open transition involved in Ca2+ binding by troponin C
    • Suarez MC, et al. (2003) Role of hydration in the closed-to-open transition involved in Ca2+ binding by troponin C. Biochemistry 42(18):5522-5530.
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5522-5530
    • Suarez, M.C.1
  • 59
    • 58149291948 scopus 로고    scopus 로고
    • Free-energy linkage between folding and calcium binding in EF-hand proteins
    • Suarez MC, Rocha CB, Sorenson MM, Silva JL, Foguel D (2008) Free-energy linkage between folding and calcium binding in EF-hand proteins. Biophys J 95(10):4820-4828.
    • (2008) Biophys J , vol.95 , Issue.10 , pp. 4820-4828
    • Suarez, M.C.1    Rocha, C.B.2    Sorenson, M.M.3    Silva, J.L.4    Foguel, D.5
  • 60
    • 42449141471 scopus 로고    scopus 로고
    • Volume and free energy of folding for troponin C C-domain: Linkage to ion binding and N-domain interaction
    • Rocha CB, et al. (2008) Volume and free energy of folding for troponin C C-domain: Linkage to ion binding and N-domain interaction. Biochemistry 47(17):5047-5058.
    • (2008) Biochemistry , vol.47 , Issue.17 , pp. 5047-5058
    • Rocha, C.B.1
  • 61
    • 84892576511 scopus 로고    scopus 로고
    • Unified description of urea denaturation: Backbone and side chains contribute equally in the transfer model
    • Moeser B, Horinek D (2014) Unified description of urea denaturation: Backbone and side chains contribute equally in the transfer model. J Phys Chem B 118(1):107-114.
    • (2014) J Phys Chem B , vol.118 , Issue.1 , pp. 107-114
    • Moeser, B.1    Horinek, D.2
  • 62
    • 33644904056 scopus 로고    scopus 로고
    • Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution - Experiments and theoretical interpretation
    • Mitra L, Smolin N, Ravindra R, Royer C, Winter R (2006) Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution - experiments and theoretical interpretation. Phys Chem Chem Phys 8(11):1249-1265.
    • (2006) Phys Chem Chem Phys , vol.8 , Issue.11 , pp. 1249-1265
    • Mitra, L.1    Smolin, N.2    Ravindra, R.3    Royer, C.4    Winter, R.5
  • 63
    • 72749109890 scopus 로고    scopus 로고
    • Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins
    • Schweiker KL, Makhatadze GI (2009) Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins. Methods Enzymol 466:527-547.
    • (2009) Methods Enzymol , vol.466 , pp. 527-547
    • Schweiker, K.L.1    Makhatadze, G.I.2
  • 64
    • 84925440964 scopus 로고    scopus 로고
    • Thermal expansivities of peptides, polypeptides and proteins as measured by pressure perturbation calorimetry
    • Pandharipande PP, Makhatadze GI (2015) Thermal expansivities of peptides, polypeptides and proteins as measured by pressure perturbation calorimetry. Methods 76:61-66.
    • (2015) Methods , vol.76 , pp. 61-66
    • Pandharipande, P.P.1    Makhatadze, G.I.2
  • 65
    • 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
  • 66
    • 0032516448 scopus 로고    scopus 로고
    • Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure
    • Fuentes EJ, Wand AJ (1998) Local stability and dynamics of apocytochrome b562 examined by the dependence of hydrogen exchange on hydrostatic pressure. Biochemistry 37(28):9877-9883.
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 9877-9883
    • Fuentes, E.J.1    Wand, A.J.2
  • 67
    • 84861389489 scopus 로고    scopus 로고
    • Coupled motion in proteins revealed by pressure perturbation
    • Fu Y, et al. (2012) Coupled motion in proteins revealed by pressure perturbation. JAm Chem Soc 134(20):8543-8550.
    • (2012) J Am Chem Soc , vol.134 , Issue.20 , pp. 8543-8550
    • Fu, Y.1
  • 68
    • 39749155117 scopus 로고    scopus 로고
    • Water penetration in the low and high pressure native states of ubiquitin
    • Day R, García AE (2008) Water penetration in the low and high pressure native states of ubiquitin. Proteins 70(4):1175-1184.
    • (2008) Proteins , vol.70 , Issue.4 , pp. 1175-1184
    • Day, R.1    García, A.E.2
  • 69
    • 77649105245 scopus 로고    scopus 로고
    • Dynamic correlation between pressure-induced protein structural transition and water penetration
    • Imai T, Sugita Y (2010) Dynamic correlation between pressure-induced protein structural transition and water penetration. J Phys Chem B 114(6):2281-2286.
    • (2010) J Phys Chem B , vol.114 , Issue.6 , pp. 2281-2286
    • Imai, T.1    Sugita, Y.2
  • 70
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • Kitahara R, Yokoyama S, Akasaka K (2005) NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar. J Mol Biol 347(2):277-285.
    • (2005) J Mol Biol , vol.347 , Issue.2 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 71
    • 77957970492 scopus 로고    scopus 로고
    • Dry molten globule intermediates and the mechanism of protein unfolding
    • Baldwin RL, Frieden C, Rose GD (2010) Dry molten globule intermediates and the mechanism of protein unfolding. Proteins 78(13):2725-2737.
    • (2010) Proteins , vol.78 , Issue.13 , pp. 2725-2737
    • Baldwin, R.L.1    Frieden, C.2    Rose, G.D.3
  • 72
    • 0029001090 scopus 로고
    • Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A
    • Kiefhaber T, Labhardt AM, Baldwin RL (1995) Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A. Nature 375(6531):513-515.
    • (1995) Nature , vol.375 , Issue.6531 , pp. 513-515
    • Kiefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 73
    • 0029079665 scopus 로고
    • Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase
    • Hoeltzli SD, Frieden C (1995) Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-19F-tryptophan-labeled Escherichia coli dihydrofolate reductase. Proc Natl Acad Sci USA 92(20):9318-9322.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.20 , pp. 9318-9322
    • Hoeltzli, S.D.1    Frieden, C.2
  • 74
    • 68149147539 scopus 로고    scopus 로고
    • Direct evidence for a dry molten globule intermediate during the unfolding of a small protein
    • Jha SK, Udgaonkar JB (2009) Direct evidence for a dry molten globule intermediate during the unfolding of a small protein. Proc Natl Acad Sci USA 106(30):12289-12294.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.30 , pp. 12289-12294
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 75
    • 77950388103 scopus 로고    scopus 로고
    • An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain
    • Reiner A, Henklein P, Kiefhaber T (2010) An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain. Proc Natl Acad Sci USA 107(11):4955-4960.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.11 , pp. 4955-4960
    • Reiner, A.1    Henklein, P.2    Kiefhaber, T.3
  • 76
    • 0027576642 scopus 로고
    • X-ray powder diffraction analysis of silver behenate, a possible low-angle diffraction standard
    • Huang TC, Toraya H, Blanton TN, Wu Y (1993) X-ray powder diffraction analysis of silver behenate, a possible low-angle diffraction standard. J Appl Cryst 26:180-184.
    • (1993) J Appl Cryst , vol.26 , pp. 180-184
    • Huang, T.C.1    Toraya, H.2    Blanton, T.N.3    Wu, Y.4
  • 77
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Cryst 25:495-503.
    • (1992) J Appl Cryst , vol.25 , pp. 495-503
    • Svergun, D.I.1


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