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Volumn 327, Issue 2, 2003, Pages 537-548

Thermodynamics of a designed protein catenane

Author keywords

Chemical ligation; Protein design; Protein stability; Thermodynamics; Topological chemistry

Indexed keywords

CATENANE; OLIGOMER; PROTEIN P53;

EID: 0037459237     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00115-3     Document Type: Article
Times cited : (46)

References (48)
  • 1
    • 33947466111 scopus 로고
    • Theory of elastic mechanisms in fibrous proteins
    • Flory P. Theory of elastic mechanisms in fibrous proteins. J. Am. Chem. Soc. 78:1956;5222-5235.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 5222-5235
    • Flory, P.1
  • 2
    • 84984087977 scopus 로고
    • Statistical mechanics of noncovalent bonds in polyamino acids
    • Poland D.C., Scheraga H.A. Statistical mechanics of noncovalent bonds in polyamino acids. Biopolymers. 3:1965;379-399.
    • (1965) Biopolymers , vol.3 , pp. 379-399
    • Poland, D.C.1    Scheraga, H.A.2
  • 3
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews B.W., Nicholson H., Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl Acad. Sci. USA. 84:1987;6663-6667.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 4
    • 0033611958 scopus 로고    scopus 로고
    • The hydrogen bond mimic approach: Solid-phase synthesis of a peptide stabilized as an α-helix with a hydrazone link
    • Cabezas E., Satterthwait A.C. The hydrogen bond mimic approach: solid-phase synthesis of a peptide stabilized as an α-helix with a hydrazone link. J. Am. Chem. Soc. 12:1999;3862-3875.
    • (1999) J. Am. Chem. Soc. , vol.12 , pp. 3862-3875
    • Cabezas, E.1    Satterthwait, A.C.2
  • 6
    • 0031027124 scopus 로고    scopus 로고
    • A general method for constraining short peptides to an alpha-helical conformation
    • Phelan J.C., Skelton N.J., Braisted A.C., McDowell R.S. A general method for constraining short peptides to an alpha-helical conformation. J. Am. Chem. Soc. 119:1997;455.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 455
    • Phelan, J.C.1    Skelton, N.J.2    Braisted, A.C.3    McDowell, R.S.4
  • 8
    • 0028465478 scopus 로고
    • Entropic effects of disulfide bonds on protein stability
    • Zhang T., Bertelsen E., Alber T. Entropic effects of disulfide bonds on protein stability. Nature Struct. Biol. 1:1994;434-438.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 434-438
    • Zhang, T.1    Bertelsen, E.2    Alber, T.3
  • 9
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg D.P., Creighton T.E. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 165:1983;407-413.
    • (1983) J. Mol. Biol. , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 10
    • 0026766974 scopus 로고
    • Constrained peptides: Models of bioactive peptides and protein substructures
    • Rizo J., Gierasch L.M. Constrained peptides: models of bioactive peptides and protein substructures. Annu. Rev. Biochem. 61:1992;387-418.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 387-418
    • Rizo, J.1    Gierasch, L.M.2
  • 11
    • 0033575092 scopus 로고    scopus 로고
    • Biosynthesis of a head to tail cyclized protein with improved biological activitiy
    • Camarero J.A., Muir T.W. Biosynthesis of a head to tail cyclized protein with improved biological activitiy. J. Am. Chem. Soc. 121:1999;5597-5598.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5597-5598
    • Camarero, J.A.1    Muir, T.W.2
  • 12
    • 0034634005 scopus 로고    scopus 로고
    • Striking stabilization of Arc repressor by an engineered disulfide bond
    • Robinson C.R., Sauer R.T. Striking stabilization of Arc repressor by an engineered disulfide bond. Biochemistry. 39:2000;12494-12502.
    • (2000) Biochemistry , vol.39 , pp. 12494-12502
    • Robinson, C.R.1    Sauer, R.T.2
  • 14
    • 0024384198 scopus 로고
    • Protein engineering of disulfide bonds in subtilisin BPN′
    • Mitchison C., Wells J.A. Protein engineering of disulfide bonds in subtilisin BPN′ Biochemistry. 28:1989;4807-4815.
    • (1989) Biochemistry , vol.28 , pp. 4807-4815
    • Mitchison, C.1    Wells, J.A.2
  • 15
    • 0025641617 scopus 로고
    • Stability and activity of human immunodeficiency virus protease: Comparison of the natural dimer with a homologous, single-chain tethered dimer
    • Cheng Y.-S., Yin F.H., Foundling S., Blomstrom D., Kettner C.A. Stability and activity of human immunodeficiency virus protease: comparison of the natural dimer with a homologous, single-chain tethered dimer. Proc. Natl Acad. Sci. USA. 87:1990;9660-9664.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9660-9664
    • Cheng, Y.-S.1    Yin, F.H.2    Foundling, S.3    Blomstrom, D.4    Kettner, C.A.5
  • 16
    • 0028810342 scopus 로고
    • Chemical ligation of cysteine-containing peptides: Synthesis of a 22 kDa tethered dimer of HIV-1 protease
    • Baca M., Muir T.W., Scholzer M., Kent S.B.H. Chemical ligation of cysteine-containing peptides: synthesis of a 22 kDa tethered dimer of HIV-1 protease. J. Am. Chem. Soc. 117:1995;1881-1887.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1881-1887
    • Baca, M.1    Muir, T.W.2    Scholzer, M.3    Kent, S.B.H.4
  • 17
    • 0001675749 scopus 로고    scopus 로고
    • Interlocked macromolecules
    • Raymo F.M., Stoddart J.F. Interlocked macromolecules. Chem. Rev. 99:1999;1643-1663.
    • (1999) Chem. Rev. , vol.99 , pp. 1643-1663
    • Raymo, F.M.1    Stoddart, J.F.2
  • 18
    • 0032504044 scopus 로고    scopus 로고
    • Protein chainmail: Catenated protein in viral capsids
    • Duda R.L. Protein chainmail: catenated protein in viral capsids. Cell. 94:1998;55-60.
    • (1998) Cell , vol.94 , pp. 55-60
    • Duda, R.L.1
  • 20
    • 0035477587 scopus 로고    scopus 로고
    • Design and synthesis of a protein catenane
    • Yan L.Z., Dawson P.E. Design and synthesis of a protein catenane. Angew. Chem. Int. Ed. 40:2001;3625-3627.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 3625-3627
    • Yan, L.Z.1    Dawson, P.E.2
  • 21
    • 0030722137 scopus 로고    scopus 로고
    • Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain
    • McCoy M., Stavridi E.S., Waterman J.L.F., Wieczorek A.M., Opella S.J., Halazonetis T.D. Hydrophobic side-chain size is a determinant of the three-dimensional structure of the p53 oligomerization domain. EMBO J. 16:1997;6230-6236.
    • (1997) EMBO J. , vol.16 , pp. 6230-6236
    • McCoy, M.1    Stavridi, E.S.2    Waterman, J.L.F.3    Wieczorek, A.M.4    Opella, S.J.5    Halazonetis, T.D.6
  • 22
    • 0032525133 scopus 로고    scopus 로고
    • Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain
    • Mateu M.G., Fersht A.R. Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain. EMBO J. 17:1998;2748-2758.
    • (1998) EMBO J. , vol.17 , pp. 2748-2758
    • Mateu, M.G.1    Fersht, A.R.2
  • 24
    • 0032536553 scopus 로고    scopus 로고
    • Chemical synthesis of a circular protein domain: Evidence for folding-assisted cyclization
    • Camarero J.A., Pavel J., Muir T.W. Chemical synthesis of a circular protein domain: evidence for folding-assisted cyclization. Angew. Chem. Int. Ed. 37:1998;347-349.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 347-349
    • Camarero, J.A.1    Pavel, J.2    Muir, T.W.3
  • 25
    • 0033532889 scopus 로고    scopus 로고
    • Conformationally assisted protein ligation using C-terminal thioester peptides
    • Beligere G.S., Dawson P.E. Conformationally assisted protein ligation using C-terminal thioester peptides. J. Am. Chem. Soc. 121:1999;6332-6333.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 6332-6333
    • Beligere, G.S.1    Dawson, P.E.2
  • 26
    • 0030973396 scopus 로고    scopus 로고
    • Modulation of reactivity in native chemical ligation through the use of thiol additives
    • Dawson P.E., Churchill M.J., Ghadiri R.M., Kent S.B.H. Modulation of reactivity in native chemical ligation through the use of thiol additives. J. Am. Chem. Soc. 119:1997;4325-4329.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4325-4329
    • Dawson, P.E.1    Churchill, M.J.2    Ghadiri, R.M.3    Kent, S.B.H.4
  • 27
    • 0023055086 scopus 로고
    • Correlation between sites of limited proteolysis and segmental mobility in thermolysin
    • Fontana A., Fassina G., Vita C., Dalzappo D., Zamai M., Zambonin M. Correlation between sites of limited proteolysis and segmental mobility in thermolysin. Biochemistry. 25:1986;1847-1851.
    • (1986) Biochemistry , vol.25 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzappo, D.4    Zamai, M.5    Zambonin, M.6
  • 28
    • 0028336661 scopus 로고
    • Modeling studies of the change in conformation required for cleavage of limited proteolytic sites
    • Hubbard S.J., Eisenmerger F., Thornton J.M. Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Sci. 3:1994;757-768.
    • (1994) Protein Sci. , vol.3 , pp. 757-768
    • Hubbard, S.J.1    Eisenmerger, F.2    Thornton, J.M.3
  • 29
    • 0035961594 scopus 로고    scopus 로고
    • High-temperature protein mass mapping using a thermophilic protease
    • Bark S.J., Muster N., Yates J.R.I., Siuzdak G. High-temperature protein mass mapping using a thermophilic protease. J. Am. Chem. Soc. 123:2001;1774-1775.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1774-1775
    • Bark, S.J.1    Muster, N.2    Yates, J.R.I.3    Siuzdak, G.4
  • 31
    • 0032906377 scopus 로고    scopus 로고
    • Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53
    • Mateu M.G., Del Pino M.M., Fersht A.R. Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53. Nature Struct. Biol. 6:1999;191-198.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 191-198
    • Mateu, M.G.1    Del Pino, M.M.2    Fersht, A.R.3
  • 32
    • 0029961470 scopus 로고    scopus 로고
    • Equilibrium stability and sub-millisecond refolding of a designed single-chain Arc repressor
    • Robinson C.R., Sauer R.T. Equilibrium stability and sub-millisecond refolding of a designed single-chain Arc repressor. Biochemistry. 35:1996;13878-13884.
    • (1996) Biochemistry , vol.35 , pp. 13878-13884
    • Robinson, C.R.1    Sauer, R.T.2
  • 33
    • 0029090925 scopus 로고
    • Redesigning the topology of a four-helix-bundle protein: Monomeric Rop
    • Predki P.F., Regan L. Redesigning the topology of a four-helix-bundle protein: monomeric Rop. Biochemistry. 34:1995;9834-9839.
    • (1995) Biochemistry , vol.34 , pp. 9834-9839
    • Predki, P.F.1    Regan, L.2
  • 34
    • 0027282636 scopus 로고
    • Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding
    • Liang H., Sandberg W.S., Terwillinger T.C. Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding. Proc. Natl Acad. Sci. USA. 90:1993;7010-7014.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7010-7014
    • Liang, H.1    Sandberg, W.S.2    Terwillinger, T.C.3
  • 35
    • 0030025170 scopus 로고    scopus 로고
    • Oct-1 POU domain-DNA interactions: Cooperative binding of isolated subdomains and effects of covalent linkage
    • Klemm J.D., Pabo C.O. Oct-1 POU domain-DNA interactions: cooperative binding of isolated subdomains and effects of covalent linkage. Genes Dev. 10:1996;27-36.
    • (1996) Genes Dev. , vol.10 , pp. 27-36
    • Klemm, J.D.1    Pabo, C.O.2
  • 36
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 38
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco K.W., Simons K.T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:1998;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 39
    • 0034804243 scopus 로고    scopus 로고
    • Single-chain versus dimeric protein folding: Thermodynamic and kinetic consequences of covalent linkage
    • Zhou H.-X. Single-chain versus dimeric protein folding: thermodynamic and kinetic consequences of covalent linkage. J. Am. Chem. Soc. 123:2001;6730-6731.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6730-6731
    • Zhou, H.-X.1
  • 41
    • 0033621158 scopus 로고    scopus 로고
    • Protein synthesis by native chemical ligation: Expanded scope by using straightforward methodology
    • Hackeng T.M., Griffin J.H., Dawson P.E. Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc. Natl Acad. Sci. USA. 96:1999;10068-10073.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10068-10073
    • Hackeng, T.M.1    Griffin, J.H.2    Dawson, P.E.3
  • 42
    • 0030723697 scopus 로고    scopus 로고
    • Cleavage methods following Boc-based solid-phase peptide synthesis
    • Stewart J.M. Cleavage methods following Boc-based solid-phase peptide synthesis. Methods Enzymol. 289:1997;34-38.
    • (1997) Methods Enzymol. , vol.289 , pp. 34-38
    • Stewart, J.M.1
  • 44
    • 0030897311 scopus 로고    scopus 로고
    • Synthesis and application of unprotected cyclic peptides as building blocks for peptide dendrimers
    • Zhang L., Tam J.P. Synthesis and application of unprotected cyclic peptides as building blocks for peptide dendrimers. J. Am. Chem. Soc. 119:1997;2363-2370.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2363-2370
    • Zhang, L.1    Tam, J.P.2
  • 45
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:1989;319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 46
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-279.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-279
    • Pace, C.N.1
  • 47
    • 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. 34:1995;5309-5316.
    • (1995) Biochemistry , vol.34 , pp. 5309-5316
    • Johnson, C.R.1    Morin, P.E.2    Arrowsmith, C.H.3    Freire, E.4
  • 48
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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