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Volumn 1, Issue 6, 2007, Pages 2527-2535

Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CIRCULAR DICHROISM; MATHEMATICS; METHODOLOGY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; TEMPERATURE; THERMODYNAMICS;

EID: 34548819311     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2006.204     Document Type: Article
Times cited : (665)

References (47)
  • 2
    • 0014009972 scopus 로고
    • Circular dichroism of biological macromolecules
    • Beychok, S. Circular dichroism of biological macromolecules. Science 154, 1288-1299 (1966).
    • (1966) Science , vol.154 , pp. 1288-1299
    • Beychok, S.1
  • 3
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler, A.J., Greenfield, N.J. & Fasman, G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27, 675-735 (1973).
    • (1973) Methods Enzymol , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 4
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W.C., Jr. Protein secondary structure and circular dichroism: A practical guide. Proteins 7, 205-214 (1990).
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 5
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R.W. Circular dichroism. Methods Enzymol. 246, 34-71 (1995).
    • (1995) Methods Enzymol , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 6
  • 7
    • 33644873189 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics
    • Miles, A.J. & Wallace, B.A. Synchrotron radiation circular dichroism spectroscopy of proteins and applications in structural and functional genomics. Chem. Soc. Rev. 35, 39-51 (2006).
    • (2006) Chem. Soc. Rev , vol.35 , pp. 39-51
    • Miles, A.J.1    Wallace, B.A.2
  • 8
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • doi: 10.1038/ nprot.2006.202
    • Greenfield, N.J. Using circular dichroism spectra to estimate protein secondary structure. Nat. Protocols 1, 2006 doi: 10.1038/ nprot.2006.202.
    • Nat. Protocols , vol.1 , pp. 2006
    • Greenfield, N.J.1
  • 9
    • 0021114569 scopus 로고
    • Molten-globule state': A compact form of globular proteins with mobile side-chains
    • Ohgushi, M. & Wada, A. 'Molten-globule state': A compact form of globular proteins with mobile side-chains. FEBS Lett. 164, 21-24 (1983).
    • (1983) FEBS Lett , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 11
    • 0023440826 scopus 로고
    • Secondary structure of proteins from circular dichroism spectra. V. Secondary structure of proteins in a "molten globule" state]
    • Bolotina, I.A. [Secondary structure of proteins from circular dichroism spectra. V. Secondary structure of proteins in a "molten globule" state]. Mol. Biol. (Mosk.) 21, 1625-1635 (1987).
    • (1987) Mol. Biol. (Mosk.) , vol.21 , pp. 1625-1635
    • Bolotina, I.A.1
  • 12
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103 (1989).
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 14
    • 34548817291 scopus 로고    scopus 로고
    • Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism
    • doi: 10.1038/nprot.2006.229
    • Greenfield, N.J. Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism. Nat. Protocols 1, 2006 doi: 10.1038/nprot.2006.229.
    • Nat. Protocols , vol.1 , pp. 2006
    • Greenfield, N.J.1
  • 15
    • 34548041437 scopus 로고    scopus 로고
    • Analysis of the kinetics of folding of proteins and peptides using circular dichroism
    • doi: 10.1038/nprot.2006.244
    • Greenfield, N.J. Analysis of the kinetics of folding of proteins and peptides using circular dichroism. Nat. Protocols 1, 2006 doi: 10.1038/nprot.2006.244.
    • Nat. Protocols , vol.1 , pp. 2006
    • Greenfield, N.J.1
  • 16
    • 3242713435 scopus 로고    scopus 로고
    • Circular dichroism analysis for protein-protein interactions
    • Greenfield, N.J. Circular dichroism analysis for protein-protein interactions. Methods Mol. Biol. 261, 55-78 (2004).
    • (2004) Methods Mol. Biol , vol.261 , pp. 55-78
    • Greenfield, N.J.1
  • 17
    • 1642486696 scopus 로고    scopus 로고
    • Analysis of circular dichroism data
    • Greenfield, N.J. Analysis of circular dichroism data. Methods Enzymol. 383, 282-317 (2004).
    • (2004) Methods Enzymol , vol.383 , pp. 282-317
    • Greenfield, N.J.1
  • 18
    • 0019321060 scopus 로고
    • Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation
    • Pace, C.N. & McGrath, T. Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation. J. Biol. Chem. 255 3862-3865 (1980).
    • (1980) J. Biol. Chem , vol.255 , pp. 3862-3865
    • Pace, C.N.1    McGrath, T.2
  • 19
    • 0034255443 scopus 로고    scopus 로고
    • A new method for the determination of stability parameters of proteins from their heat-induced denaturation curves
    • Yadav, S. & Ahmad, F. A new method for the determination of stability parameters of proteins from their heat-induced denaturation curves. Anal. Biochem. 283, 207-213 (2000).
    • (2000) Anal. Biochem , vol.283 , pp. 207-213
    • Yadav, S.1    Ahmad, F.2
  • 20
    • 0029130877 scopus 로고
    • Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins
    • Eftink, M.R. Use of multiple spectroscopic methods to monitor equilibrium unfolding of proteins. Methods Enzymol. 259, 487-512 (1995).
    • (1995) Methods Enzymol , vol.259 , pp. 487-512
    • Eftink, M.R.1
  • 21
    • 0029000171 scopus 로고
    • Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor
    • Johnson, C.R., Morin, P.E., Arrowsmith, C.H. & Freire, E. Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor. Biochemistry 34, 5309-5316 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5309-5316
    • Johnson, C.R.1    Morin, P.E.2    Arrowsmith, C.H.3    Freire, E.4
  • 22
    • 0030008556 scopus 로고    scopus 로고
    • Thermodynamics of the unfolding and spectroscopic properties of the V66W mutant of staphylococcal nuclease and its 1-136 fragment
    • Eftink, M.R. et al. Thermodynamics of the unfolding and spectroscopic properties of the V66W mutant of staphylococcal nuclease and its 1-136 fragment. Biochemistry 35, 8084-8094 (1996).
    • (1996) Biochemistry , vol.35 , pp. 8084-8094
    • Eftink, M.R.1
  • 23
    • 0030445131 scopus 로고    scopus 로고
    • Thermodynamic analysis of a designed three-stranded coiled coil
    • Boice, J.A., Dieckmann, G.R., DeGrado, W.F. & Fairman, R. Thermodynamic analysis of a designed three-stranded coiled coil. Biochemistry 35, 14480-14485 (1996).
    • (1996) Biochemistry , vol.35 , pp. 14480-14485
    • Boice, J.A.1    Dieckmann, G.R.2    DeGrado, W.F.3    Fairman, R.4
  • 24
    • 0037470575 scopus 로고    scopus 로고
    • Rapid cooperative two-state folding of a miniature α-β protein and design of a thermostable variant
    • Horng, J.C., Moroz, V. & Raleigh, D.P. Rapid cooperative two-state folding of a miniature α-β protein and design of a thermostable variant. J. Mol. Biol. 326, 1261-1270 (2003).
    • (2003) J. Mol. Biol , vol.326 , pp. 1261-1270
    • Horng, J.C.1    Moroz, V.2    Raleigh, D.P.3
  • 25
    • 0025861478 scopus 로고
    • Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins
    • Perczel, A., Hollósi, M., Tusnády, G. & Fasman, G.D. Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins. Protein Eng. 4, 669-679 (1991).
    • (1991) Protein Eng , vol.4 , pp. 669-679
    • Perczel, A.1    Hollósi, M.2    Tusnády, G.3    Fasman, G.D.4
  • 26
    • 0027265825 scopus 로고
    • Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and α α-tropomyosin
    • Greenfield, N.J. & Hitchcock-DeGregori, S.E. Conformational intermediates in the folding of a coiled-coil model peptide of the N-terminus of tropomyosin and α α-tropomyosin. Protein Sci. 2 1263-1273 (1993).
    • (1993) Protein Sci , vol.2 , pp. 1263-1273
    • Greenfield, N.J.1    Hitchcock-DeGregori, S.E.2
  • 27
    • 0027363495 scopus 로고
    • Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity
    • Safar, J., Roller, P.P., Gajdusek, D.C. & Gibbs, C.J., Jr. Thermal stability and conformational transitions of scrapie amyloid (prion) protein correlate with infectivity. Protein Sci. 2, 2206-2216 (1993).
    • (1993) Protein Sci , vol.2 , pp. 2206-2216
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 28
    • 0024281318 scopus 로고
    • Conformational transition of hyaluronic acid in aqueous-organic solvent monitored by vacuum ultraviolet circular dichroism
    • Staskus, P.W. & Johnson, W.C., Jr. Conformational transition of hyaluronic acid in aqueous-organic solvent monitored by vacuum ultraviolet circular dichroism. Biochemistry 27, 1522-1527 (1988).
    • (1988) Biochemistry , vol.27 , pp. 1522-1527
    • Staskus, P.W.1    Johnson Jr., W.C.2
  • 29
    • 0026551983 scopus 로고
    • An investigation of the thermal unfolding of swine pepsinogen using circular dichroism
    • McPhie, P. & Shrager, R.I. An investigation of the thermal unfolding of swine pepsinogen using circular dichroism. Arch. Biochem. Biophys. 293, 46-53 (1992).
    • (1992) Arch. Biochem. Biophys , vol.293 , pp. 46-53
    • McPhie, P.1    Shrager, R.I.2
  • 30
    • 0031976413 scopus 로고    scopus 로고
    • Conformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra
    • Konno, T. Conformational diversity of acid-denatured cytochrome c studied by a matrix analysis of far-UV CD spectra. Protein Sci. 7, 975-982 (1998).
    • (1998) Protein Sci , vol.7 , pp. 975-982
    • Konno, T.1
  • 31
    • 0034622508 scopus 로고    scopus 로고
    • Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles
    • Ionescu, R.M., Smith, V.F., O'Neill, J.C., Jr. & Matthews, C.R. Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles. Biochemistry 39, 9540-9550 (2000).
    • (2000) Biochemistry , vol.39 , pp. 9540-9550
    • Ionescu, R.M.1    Smith, V.F.2    O'Neill Jr., J.C.3    Matthews, C.R.4
  • 32
    • 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. & Freire, E. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry 32, 5491-5496 (1993).
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.S.1    Vinson, C.R.2    Freire, E.3
  • 33
    • 0033609809 scopus 로고    scopus 로고
    • A calorimetric study of the folding-unfolding of an α-helix with covalently closed N and C-terminal loops
    • Taylor, J.W., Greenfield, N.J., Wu, B. & Privalov, P.L. A calorimetric study of the folding-unfolding of an α-helix with covalently closed N and C-terminal loops. J. Mol. Biol. 291, 965-976 (1999).
    • (1999) J. Mol. Biol , vol.291 , pp. 965-976
    • Taylor, J.W.1    Greenfield, N.J.2    Wu, B.3    Privalov, P.L.4
  • 34
    • 0344198181 scopus 로고    scopus 로고
    • Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding
    • Singh, A. & Hitchcock-DeGregori, S.E. Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 42, 14114-14121 (2003).
    • (2003) Biochemistry , vol.42 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 35
    • 0028673096 scopus 로고
    • Analysis of multidimensional spectroscopic data to monitor unfolding of proteins
    • Ramsay, G.D. & Eftink, M.R. Analysis of multidimensional spectroscopic data to monitor unfolding of proteins. Methods Enzymol. 240, 615-645 (1994).
    • (1994) Methods Enzymol , vol.240 , pp. 615-645
    • Ramsay, G.D.1    Eftink, M.R.2
  • 36
    • 0016699207 scopus 로고
    • Macromolecular binding
    • Schellman, J.A. Macromolecular binding. Biopolymers 14, 999-1018 (1975).
    • (1975) Biopolymers , vol.14 , pp. 999-1018
    • Schellman, J.A.1
  • 37
    • 0017066152 scopus 로고
    • The effect of binding on the melting temperature of biopolymers
    • Schellman, J.A. The effect of binding on the melting temperature of biopolymers. Biopolymers 15, 999-1000 (1976).
    • (1976) Biopolymers , vol.15 , pp. 999-1000
    • Schellman, J.A.1
  • 38
    • 0000169232 scopus 로고
    • An algorithm for the estimation of non-linear parameters
    • Marquardt, D.W. An algorithm for the estimation of non-linear parameters. J. Soc. Indust. Appl. Math. 11, 431-441 (1963).
    • (1963) J. Soc. Indust. Appl. Math , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 39
    • 0032568543 scopus 로고    scopus 로고
    • The structure of the N-terminus of striated muscle α-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies
    • Greenfield, N.J., Montelione, G.T., Farid, R.S. & Hitchcock-DeGregori, S.E. The structure of the N-terminus of striated muscle α-tropomyosin in a chimeric peptide: Nuclear magnetic resonance structure and circular dichroism studies. Biochemistry 37, 7834-7843 (1998).
    • (1998) Biochemistry , vol.37 , pp. 7834-7843
    • Greenfield, N.J.1    Montelione, G.T.2    Farid, R.S.3    Hitchcock-DeGregori, S.E.4
  • 40
    • 0036842026 scopus 로고    scopus 로고
    • Structure and interactions of the carboxyl terminus of striated muscle α-tropomyosin: It is important to be flexible
    • Greenfield, N.J., Palm, T. & Hitchcock-DeGregori, S.E. Structure and interactions of the carboxyl terminus of striated muscle α-tropomyosin: it is important to be flexible. Biophys. J. 83, 2754-2766 (2002).
    • (2002) Biophys. J , vol.83 , pp. 2754-2766
    • Greenfield, N.J.1    Palm, T.2    Hitchcock-DeGregori, S.E.3
  • 41
    • 0346034577 scopus 로고    scopus 로고
    • The structure of the carboxyl terminus of striated α-tropomyosin in solution reveals an unusual parallel arrangement of interacting α-helices
    • Greenfield, N.J. et al. The structure of the carboxyl terminus of striated α-tropomyosin in solution reveals an unusual parallel arrangement of interacting α-helices. Biochemistry 42, 614-619 (2003).
    • (2003) Biochemistry , vol.42 , pp. 614-619
    • Greenfield, N.J.1
  • 42
    • 0037961515 scopus 로고    scopus 로고
    • Tropomyosin ends determine the stability and functionality of overlap and troponin T complexes
    • Palm, T., Greenfield, N.J. & Hitchcock-DeGregori, S.E. Tropomyosin ends determine the stability and functionality of overlap and troponin T complexes. Biophys. J. 84, 3181-3189 (2003).
    • (2003) Biophys. J , vol.84 , pp. 3181-3189
    • Palm, T.1    Greenfield, N.J.2    Hitchcock-DeGregori, S.E.3
  • 43
    • 0034759429 scopus 로고    scopus 로고
    • Disease-causing mutations in cardiac troponin T: Identification of a critical tropomyosin-binding region
    • Palm, T., Graboski, S., Hitchcock-DeGregori, S.E. & Greenfield, N.J. Disease-causing mutations in cardiac troponin T: Identification of a critical tropomyosin-binding region. Biophys. J. 81, 2827-2837 (2001).
    • (2001) Biophys. J , vol.81 , pp. 2827-2837
    • Palm, T.1    Graboski, S.2    Hitchcock-DeGregori, S.E.3    Greenfield, N.J.4
  • 44
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. & Fasman, G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 4108-4116 (1969).
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 45
    • 0018256713 scopus 로고
    • Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helix
    • Bentz, H., Bächinger, H.P., Glanville, R. & Kühn, K. Physical evidence for the assembly of A and B chains of human placental collagen in a single triple helix. Eur. J. Biochem. 92, 563-567 (1978).
    • (1978) Eur. J. Biochem , vol.92 , pp. 563-567
    • Bentz, H.1    Bächinger, H.P.2    Glanville, R.3    Kühn, K.4
  • 46
    • 0015455860 scopus 로고
    • Effect of temperature on the circular dichroism spectra of polypeptides in the extended state
    • Tiffany, M.L. & Krimm, S. Effect of temperature on the circular dichroism spectra of polypeptides in the extended state. Biopolymers 11, 2309-2316 (1972).
    • (1972) Biopolymers , vol.11 , pp. 2309-2316
    • Tiffany, M.L.1    Krimm, S.2
  • 47
    • 0002251831 scopus 로고
    • Circular dichroism and conformation of unordered polypeptides
    • Woody, R.W. Circular dichroism and conformation of unordered polypeptides. Adv. Biophys. Chem. 2, 31-79 (1992).
    • (1992) Adv. Biophys. Chem , vol.2 , pp. 31-79
    • Woody, R.W.1


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