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Volumn 126, Issue 1-3, 2007, Pages 16-24

Microcalorimetry of biological macromolecules

Author keywords

Association; DNA; Hydration; Microcalorimetry; Proteins; Thermodynamics; Unfolding

Indexed keywords

DOUBLE STRANDED DNA;

EID: 33846637900     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.05.004     Document Type: Article
Times cited : (151)

References (57)
  • 3
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study
    • Privalov P.L., and Khechinashvili N.N. A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J. Mol. Biol. 86 (1974) 665-684
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 4
    • 0018588511 scopus 로고
    • Stability of proteins: small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33 (1979) 167-241
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 5
    • 33846639985 scopus 로고    scopus 로고
    • Protein stability
    • Creighton T. (Ed), Wiley, New York
    • Privalov P.L. Protein stability. In: Creighton T. (Ed). Encyclopedia of Molecular Biology (1999), Wiley, New York 2016-2020
    • (1999) Encyclopedia of Molecular Biology , pp. 2016-2020
    • Privalov, P.L.1
  • 6
    • 0028845120 scopus 로고
    • Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution
    • Privalov G., Kavina V., Freire E., and Privalov P.L. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Anal. Biochem. 232 (1995) 79-85
    • (1995) Anal. Biochem. , vol.232 , pp. 79-85
    • Privalov, G.1    Kavina, V.2    Freire, E.3    Privalov, P.L.4
  • 7
    • 45349109508 scopus 로고
    • Three generations of scanning microcalorimeters for liquids
    • Privalov P.L., and Plotnikov V.V. Three generations of scanning microcalorimeters for liquids. Thermochim. Acta 139 (1989) 257-277
    • (1989) Thermochim. Acta , vol.139 , pp. 257-277
    • Privalov, P.L.1    Plotnikov, V.V.2
  • 8
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov P.L., and Gill S.J. Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39 (1988) 191-234
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 9
    • 0014669266 scopus 로고
    • Heat capacities from 11 to 305 degrees K and entropies of hydrated and anhydrous bovine zinc insulin and bovine chymotrypsinogen A. Entropy change for formation of peptide bonds
    • Hutchens J.O., Cole A.G., and Stout J.W. Heat capacities from 11 to 305 degrees K and entropies of hydrated and anhydrous bovine zinc insulin and bovine chymotrypsinogen A. Entropy change for formation of peptide bonds. J. Biol. Chem. 244 (1969) 26-32
    • (1969) J. Biol. Chem. , vol.244 , pp. 26-32
    • Hutchens, J.O.1    Cole, A.G.2    Stout, J.W.3
  • 11
    • 33846616712 scopus 로고    scopus 로고
    • Heat capacity of polymers
    • Mark J.E. (Ed), American Institute of Physics, Woodbury, NY
    • Wen J. Heat capacity of polymers. In: Mark J.E. (Ed). Physical Properties of Polymers Handbook (1996), American Institute of Physics, Woodbury, NY
    • (1996) Physical Properties of Polymers Handbook
    • Wen, J.1
  • 13
    • 0032766705 scopus 로고    scopus 로고
    • Experimental study of the protein folding landscape: unfolding reactions in cytochrome c
    • Milne J.S., Xu Y., Mayne L.C., and Englander S.W. Experimental study of the protein folding landscape: unfolding reactions in cytochrome c. J. Mol. Biol. 290 (1999) 811-822
    • (1999) J. Mol. Biol. , vol.290 , pp. 811-822
    • Milne, J.S.1    Xu, Y.2    Mayne, L.C.3    Englander, S.W.4
  • 14
    • 0033544727 scopus 로고    scopus 로고
    • The energetics of HMG box interactions with DNA: thermodynamics of the DNA binding of the HMG box from mouse sox-5
    • Privalov P.L., Jelesarov I., Read C.M., Dragan A.I., and Crane-Robinson C. The energetics of HMG box interactions with DNA: thermodynamics of the DNA binding of the HMG box from mouse sox-5. J. Mol. Biol. 294 (1999) 997-1013
    • (1999) J. Mol. Biol. , vol.294 , pp. 997-1013
    • Privalov, P.L.1    Jelesarov, I.2    Read, C.M.3    Dragan, A.I.4    Crane-Robinson, C.5
  • 15
    • 0036382925 scopus 로고    scopus 로고
    • Unfolding of a leucine zipper is not a simple two-state transition
    • Dragan A.I., and Privalov P.L. Unfolding of a leucine zipper is not a simple two-state transition. J. Mol. Biol. 321 (2002) 891-908
    • (2002) J. Mol. Biol. , vol.321 , pp. 891-908
    • Dragan, A.I.1    Privalov, P.L.2
  • 16
    • 0037943192 scopus 로고    scopus 로고
    • A new set of peptide-based group heat capacities for use in protein stability calculations
    • Hackel M., Hinz H.J., and Hedwig G.R. A new set of peptide-based group heat capacities for use in protein stability calculations. J. Mol. Biol. 291 (1999) 197-213
    • (1999) J. Mol. Biol. , vol.291 , pp. 197-213
    • Hackel, M.1    Hinz, H.J.2    Hedwig, G.R.3
  • 17
    • 0025360593 scopus 로고
    • Heat capacity of proteins: I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect
    • Makhatadze G.I., and Privalov P.L. Heat capacity of proteins: I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. J. Mol. Biol. 213 (1990) 375-384
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 18
    • 0025287103 scopus 로고
    • Heat capacity of proteins: II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects
    • Privalov P.L., and Makhatadze G.I. Heat capacity of proteins: II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects. J. Mol. Biol. 213 (1990) 385-391
    • (1990) J. Mol. Biol. , vol.213 , pp. 385-391
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 20
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics: I. The enthalpy of hydration
    • Makhatadze G.I., and Privalov P.L. Contribution of hydration to protein folding thermodynamics: I. The enthalpy of hydration. J. Mol. Biol. 232 (1993) 639-659
    • (1993) J. Mol. Biol. , vol.232 , pp. 639-659
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 21
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics: II. The entropy and Gibbs energy of hydration
    • Privalov P.L., and Makhatadze G.I. Contribution of hydration to protein folding thermodynamics: II. The entropy and Gibbs energy of hydration. J. Mol. Biol. 232 (1993) 660-679
    • (1993) J. Mol. Biol. , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 22
    • 0026344361 scopus 로고
    • Solid model compounds and the thermodynamics of protein unfolding
    • Murphy K.P., and Gill S.J. Solid model compounds and the thermodynamics of protein unfolding. J. Mol. Biol. 222 (1991) 699-709
    • (1991) J. Mol. Biol. , vol.222 , pp. 699-709
    • Murphy, K.P.1    Gill, S.J.2
  • 23
    • 0026511652 scopus 로고
    • Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding
    • Privalov P.L., and Makhatadze G.I. Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding. J. Mol. Biol. 224 (1992) 715-723
    • (1992) J. Mol. Biol. , vol.224 , pp. 715-723
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 24
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar R.S., Livingstone J.R., and Record Jr. M.T. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 31 (1992) 3947-3955
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record Jr., M.T.3
  • 25
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig A.J., and Sternberg M.J. Side-chain conformational entropy in protein folding. Protein Sci. 4 (1995) 2247-2251
    • (1995) Protein Sci. , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.2
  • 26
    • 0027991081 scopus 로고
    • Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation
    • Lee K.H., Xie D., Freire E., and Amzel L.M. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins 20 (1994) 68-84
    • (1994) Proteins , vol.20 , pp. 68-84
    • Lee, K.H.1    Xie, D.2    Freire, E.3    Amzel, L.M.4
  • 27
    • 0000181415 scopus 로고
    • The influence of amino acid side-chains on the free energy of helix-coil transitions
    • Nemethy G., Leach S.J., and Scheraga H.A. The influence of amino acid side-chains on the free energy of helix-coil transitions. J. Phys. Chem. 70 (1966) 998-1004
    • (1966) J. Phys. Chem. , vol.70 , pp. 998-1004
    • Nemethy, G.1    Leach, S.J.2    Scheraga, H.A.3
  • 28
    • 0027166270 scopus 로고
    • Empirical scale of side-chain conformational entropy in protein folding
    • Pickett S.D., and Sternberg M.J. Empirical scale of side-chain conformational entropy in protein folding. J. Mol. Biol. 231 (1993) 825-839
    • (1993) J. Mol. Biol. , vol.231 , pp. 825-839
    • Pickett, S.D.1    Sternberg, M.J.2
  • 29
    • 77049276418 scopus 로고
    • The stability of hydrogen bonded peptide structures in aqueous solution
    • Schellman J.A. The stability of hydrogen bonded peptide structures in aqueous solution. Trav. Lab. Carlsberg. Ser. Chim. 29 (1955) 230-259
    • (1955) Trav. Lab. Carlsberg. Ser. Chim. , vol.29 , pp. 230-259
    • Schellman, J.A.1
  • 30
    • 0028174101 scopus 로고
    • Protein side-chain conformational entropy derived from fusion data-comparison with other empirical scales
    • Sternberg M.J., and Chickos J.S. Protein side-chain conformational entropy derived from fusion data-comparison with other empirical scales. Protein Eng. 7 (1994) 149-155
    • (1994) Protein Eng. , vol.7 , pp. 149-155
    • Sternberg, M.J.1    Chickos, J.S.2
  • 31
    • 0028844980 scopus 로고
    • Calculation of relative binding free energies and configurational entropies: a structural and thermodynamic analysis of the nature of non-polar binding of thrombin inhibitors based on hirudin55-65
    • Wang J., Szewczuk Z., Yue S.Y., Tsuda Y., Konishi Y., and Purisima E.O. Calculation of relative binding free energies and configurational entropies: a structural and thermodynamic analysis of the nature of non-polar binding of thrombin inhibitors based on hirudin55-65. J. Mol. Biol. 253 (1995) 473-492
    • (1995) J. Mol. Biol. , vol.253 , pp. 473-492
    • Wang, J.1    Szewczuk, Z.2    Yue, S.Y.3    Tsuda, Y.4    Konishi, Y.5    Purisima, E.O.6
  • 32
    • 0029121068 scopus 로고
    • Free energy determinants of secondary structure formation: I. Alpha-helices
    • Yang A.S., and Honig B. Free energy determinants of secondary structure formation: I. Alpha-helices. J. Mol. Biol. 252 (1995) 351-365
    • (1995) J. Mol. Biol. , vol.252 , pp. 351-365
    • Yang, A.S.1    Honig, B.2
  • 33
    • 0032575767 scopus 로고    scopus 로고
    • The energetics of HMG box interactions with DNA. Thermodynamic description of the box from mouse Sox-5
    • Crane-Robinson C., Read C.M., Cary P.D., Driscoll P.C., Dragan A.I., and Privalov P.L. The energetics of HMG box interactions with DNA. Thermodynamic description of the box from mouse Sox-5. J. Mol. Biol. 281 (1998) 705-717
    • (1998) J. Mol. Biol. , vol.281 , pp. 705-717
    • Crane-Robinson, C.1    Read, C.M.2    Cary, P.D.3    Driscoll, P.C.4    Dragan, A.I.5    Privalov, P.L.6
  • 34
    • 0017836908 scopus 로고
    • Statistical mechanical deconvolution of thermal transitions in macromolecules: I. Theory and application to homogeneous systems
    • Freire E., and Biltonen R.L. Statistical mechanical deconvolution of thermal transitions in macromolecules: I. Theory and application to homogeneous systems. Biopolymers 17 (1978) 463-479
    • (1978) Biopolymers , vol.17 , pp. 463-479
    • Freire, E.1    Biltonen, R.L.2
  • 35
    • 0028674091 scopus 로고
    • Statistical thermodynamic analysis of differential scanning calorimetry data: structural deconvolution of heat capacity function of proteins
    • Freire E. Statistical thermodynamic analysis of differential scanning calorimetry data: structural deconvolution of heat capacity function of proteins. Methods Enzymol. 240 (1994) 502-530
    • (1994) Methods Enzymol. , vol.240 , pp. 502-530
    • Freire, E.1
  • 36
    • 0017826433 scopus 로고
    • Thermodynamic analysis of transfer RNA unfolding
    • Privalov P.L., and Filimonov V.V. Thermodynamic analysis of transfer RNA unfolding. J. Mol. Biol. 122 (1978) 447-464
    • (1978) J. Mol. Biol. , vol.122 , pp. 447-464
    • Privalov, P.L.1    Filimonov, V.V.2
  • 37
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov P.L., and Potekhin S.A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131 (1986) 4-51
    • (1986) Methods Enzymol. , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 38
    • 0042166066 scopus 로고    scopus 로고
    • DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution
    • Dragan A.I., Klass J., Read C., Churchill M.E., Crane-Robinson C., and Privalov P.L. DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial non-electrostatic contribution. J. Mol. Biol. 331 (2003) 795-813
    • (2003) J. Mol. Biol. , vol.331 , pp. 795-813
    • Dragan, A.I.1    Klass, J.2    Read, C.3    Churchill, M.E.4    Crane-Robinson, C.5    Privalov, P.L.6
  • 40
    • 0020348367 scopus 로고
    • Stability of proteins. Proteins which do not present a single cooperative system
    • Privalov P.L. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35 (1982) 1-104
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 41
    • 0035957225 scopus 로고    scopus 로고
    • Energetics of coiled coil folding: the nature of the transition states
    • Bosshard H.R., Durr E., Hitz T., and Jelesarov I. Energetics of coiled coil folding: the nature of the transition states. Biochemistry 40 (2001) 3544-3552
    • (2001) Biochemistry , vol.40 , pp. 3544-3552
    • Bosshard, H.R.1    Durr, E.2    Hitz, T.3    Jelesarov, I.4
  • 42
    • 0029900846 scopus 로고    scopus 로고
    • The magnitude of the backbone conformational entropy change in protein folding
    • D'Aquino J.A., Gomez J., Hilser V.J., Lee K.H., Amzel L.M., and Freire E. The magnitude of the backbone conformational entropy change in protein folding. Proteins 25 (1996) 143-156
    • (1996) Proteins , vol.25 , pp. 143-156
    • D'Aquino, J.A.1    Gomez, J.2    Hilser, V.J.3    Lee, K.H.4    Amzel, L.M.5    Freire, E.6
  • 43
    • 0035936548 scopus 로고    scopus 로고
    • Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1
    • Ibarra-Molero B., Makhatadze G.I., and Matthews C.R. Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1. Biochemistry 40 (2001) 719-731
    • (2001) Biochemistry , vol.40 , pp. 719-731
    • Ibarra-Molero, B.1    Makhatadze, G.I.2    Matthews, C.R.3
  • 44
    • 0345676548 scopus 로고    scopus 로고
    • Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper)
    • Jelesarov I., Durr E., Thomas R.M., and Bosshard H.R. Salt effects on hydrophobic interaction and charge screening in the folding of a negatively charged peptide to a coiled coil (leucine zipper). Biochemistry 37 (1998) 7539-7550
    • (1998) Biochemistry , vol.37 , pp. 7539-7550
    • Jelesarov, I.1    Durr, E.2    Thomas, R.M.3    Bosshard, H.R.4
  • 45
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions
    • Krylov D., Mikhailenko I., and Vinson C. A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions. EMBO J. 13 (1994) 2849-2861
    • (1994) EMBO J. , vol.13 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 46
    • 0034711008 scopus 로고    scopus 로고
    • Interhelical ion pairing in coiled coils: solution structure of a heterodimeric leucine zipper and determination of pKa values of Glu side chains
    • Marti D.N., Jelesarov I., and Bosshard H.R. Interhelical ion pairing in coiled coils: solution structure of a heterodimeric leucine zipper and determination of pKa values of Glu side chains. Biochemistry 39 (2000) 12804-12818
    • (2000) Biochemistry , vol.39 , pp. 12804-12818
    • Marti, D.N.1    Jelesarov, I.2    Bosshard, H.R.3
  • 47
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson K.S., Vinson C.R., and Freire E. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry 32 (1993) 5491-5496
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 48
    • 5144227739 scopus 로고    scopus 로고
    • Thermodynamic signature of GCN4-bZIP binding to DNA indicates the role of water in discriminating between the AP-1 and ATF/CREB sites
    • Dragan A.I., Frank L., Liu Y., Makeyeva E.N., Crane-Robinson C., and Privalov P.L. Thermodynamic signature of GCN4-bZIP binding to DNA indicates the role of water in discriminating between the AP-1 and ATF/CREB sites. J. Mol. Biol. 343 (2004) 865-878
    • (2004) J. Mol. Biol. , vol.343 , pp. 865-878
    • Dragan, A.I.1    Frank, L.2    Liu, Y.3    Makeyeva, E.N.4    Crane-Robinson, C.5    Privalov, P.L.6
  • 49
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar R.S., and Record Jr. M.T. Coupling of local folding to site-specific binding of proteins to DNA. Science 263 (1994) 777-784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 51
    • 27444436325 scopus 로고    scopus 로고
    • Stability and DNA binding ability of the DNA binding domains of interferon regulatory factors 1 and 3
    • Hargreaves V.V., Makeyeva E.N., Dragan A.I., and Privalov P.L. Stability and DNA binding ability of the DNA binding domains of interferon regulatory factors 1 and 3. Biochemistry 44 (2005) 14202-14209
    • (2005) Biochemistry , vol.44 , pp. 14202-14209
    • Hargreaves, V.V.1    Makeyeva, E.N.2    Dragan, A.I.3    Privalov, P.L.4
  • 52
    • 0033656801 scopus 로고    scopus 로고
    • Energetics of the specific binding interaction of the first three zinc fingers of the transcription factor TFIIIA with its cognate DNA sequence
    • Liggins J.R., and Privalov P.L. Energetics of the specific binding interaction of the first three zinc fingers of the transcription factor TFIIIA with its cognate DNA sequence. Proteins, Suppl. 4 (2000) 50-62
    • (2000) Proteins, Suppl. , vol.4 , pp. 50-62
    • Liggins, J.R.1    Privalov, P.L.2
  • 53
    • 0034435652 scopus 로고    scopus 로고
    • Structural and thermodynamic strategies for site-specific DNA binding proteins
    • Jen-Jacobson L., Engler L.E., and Jacobson L.A. Structural and thermodynamic strategies for site-specific DNA binding proteins. Structure 8 (2000) 1015-1023
    • (2000) Structure , vol.8 , pp. 1015-1023
    • Jen-Jacobson, L.1    Engler, L.E.2    Jacobson, L.A.3
  • 54
    • 4644342209 scopus 로고    scopus 로고
    • Thermodynamics of DNA binding and distortion by the hyperthermophile chromatin protein Sac7d
    • Peters W.B., Edmondson S.P., and Shriver J.W. Thermodynamics of DNA binding and distortion by the hyperthermophile chromatin protein Sac7d. J. Mol. Biol. 343 (2004) 339-360
    • (2004) J. Mol. Biol. , vol.343 , pp. 339-360
    • Peters, W.B.1    Edmondson, S.P.2    Shriver, J.W.3
  • 55
    • 20144368902 scopus 로고    scopus 로고
    • Complicated water orientations in the minor groove of the B-DNA decamer d(CCATTAATGG)2 observed by neutron diffraction measurements
    • Arai S., Chatake T., Ohhara T., Kurihara K., Tanaka I., Suzuki N., Fujimoto Z., Mizuno H., and Niimura N. Complicated water orientations in the minor groove of the B-DNA decamer d(CCATTAATGG)2 observed by neutron diffraction measurements. Nucleic Acids Res. 33 (2005) 3017-3024
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3017-3024
    • Arai, S.1    Chatake, T.2    Ohhara, T.3    Kurihara, K.4    Tanaka, I.5    Suzuki, N.6    Fujimoto, Z.7    Mizuno, H.8    Niimura, N.9
  • 56
    • 0033600794 scopus 로고    scopus 로고
    • Absence of minor groove monovalent cations in the crosslinked dodecamer C-G-C-G-A-A-T-T-C-G-C-G
    • Chiu T.K., Kaczor-Grzeskowiak M., and Dickerson R.E. Absence of minor groove monovalent cations in the crosslinked dodecamer C-G-C-G-A-A-T-T-C-G-C-G. J. Mol. Biol. 292 (1999) 589-608
    • (1999) J. Mol. Biol. , vol.292 , pp. 589-608
    • Chiu, T.K.1    Kaczor-Grzeskowiak, M.2    Dickerson, R.E.3
  • 57
    • 0032387836 scopus 로고    scopus 로고
    • Structure of the potassium form of CGCGAATTCGCG: DNA deformation by electrostatic collapse around inorganic cations
    • Shui X., Sines C.C., McFail-Isom L., VanDerveer D., and Williams L.D. Structure of the potassium form of CGCGAATTCGCG: DNA deformation by electrostatic collapse around inorganic cations. Biochemistry 37 (1998) 16877-16887
    • (1998) Biochemistry , vol.37 , pp. 16877-16887
    • Shui, X.1    Sines, C.C.2    McFail-Isom, L.3    VanDerveer, D.4    Williams, L.D.5


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