메뉴 건너뛰기




Volumn 20, Issue 2, 2011, Pages 336-340

Calorimetric study of a series of designed repeat proteins: Modular structure and modular folding

Author keywords

Differential scanning calorimetry (DSC); Ising model; Protein design; Protein folding; Repeat protein; Tetratricopeptide repeat (TPR); Thermal denaturation; Thermodynamic analysis

Indexed keywords

TETRATRICOPEPTIDE REPEAT PROTEIN;

EID: 79251582498     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.564     Document Type: Article
Times cited : (36)

References (28)
  • 1
    • 23044475553 scopus 로고    scopus 로고
    • A recurring theme in protein engineering: The design, stability and folding of repeat proteins
    • DOI 10.1016/j.sbi.2005.07.003, PII S0959440X05001259, Membranes/Engineering and Desing
    • Main E, Lowe A, Mochrie S, Jackson S, Regan L (2005) A recurring theme in protein engineering: the design, stability and folding of repeat proteins. Curr Opin Struc Biol 15:464-471. (Pubitemid 41073839)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.4 , pp. 464-471
    • Main, E.R.G.1    Lowe, A.R.2    Mochrie, S.G.J.3    Jackson, S.E.4    Regan, L.5
  • 3
    • 36749050344 scopus 로고    scopus 로고
    • Repeat-protein folding: New insights into origins of cooperativity, stability, and topology
    • DOI 10.1016/j.abb.2007.08.034, PII S0003986107004511, Highlight Issue: Protein Folding
    • Kloss E, Courtemanchea N, Barrick D (2008) Repeat-protein folding: New insights into origins of cooperativity, stability, and topology. Arch Biochem Biophys 469:83-99. (Pubitemid 350212850)
    • (2008) Archives of Biochemistry and Biophysics , vol.469 , Issue.1 , pp. 83-99
    • Kloss, E.1    Courtemanche, N.2    Barrick, D.3
  • 4
    • 0025122590 scopus 로고
    • The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae
    • Schultz J, Marshall-Carlson L, Carlson M (1990) The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae. Mol Cell Biol 10:4744-4756.
    • (1990) Mol Cell Biol , vol.10 , pp. 4744-4756
    • Schultz, J.1    Marshall-Carlson, L.2    Carlson, M.3
  • 5
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: To TPR or not to TPR?
    • Lamb JR, Tugendreich S, Hieter P (1995) Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends Biochem Sci 20:257-259.
    • (1995) Trends Biochem Sci , vol.20 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 6
    • 0344628648 scopus 로고    scopus 로고
    • TPR proteins: The versatile helix
    • D'Andrea L, Regan L (2003) TPR proteins: the versatile helix. Trends Biochem Sci 28:655-662.
    • (2003) Trends Biochem Sci , vol.28 , pp. 655-662
    • D'Andrea, L.1    Regan, L.2
  • 7
    • 0041428117 scopus 로고    scopus 로고
    • The folding and design of repeat proteins: Reaching a consensus
    • Main ERG, Jackson SE, Regan L (2003) The folding and design of repeat proteins: reaching a consensus. Curr Opin Struct Biol 13:482-489.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 482-489
    • Main, E.R.G.1    Jackson, S.E.2    Regan, L.3
  • 8
    • 0037648552 scopus 로고    scopus 로고
    • Design of stable alpha-helical arrays from an idealized TPR motif
    • Main ERG, Xiong Y, Cocco MJ, D'Andrea L, Regan L (2003) Design of stable alpha-helical arrays from an idealized TPR motif. Structure 11:497-508.
    • (2003) Structure , vol.11 , pp. 497-508
    • Main, E.R.G.1    Xiong, Y.2    Cocco, M.J.3    D'Andrea, L.4    Regan, L.5
  • 10
    • 33749055081 scopus 로고    scopus 로고
    • Consensus design as a tool for engineering repeat proteins
    • Kajander T, Cortajarena AL, Regan L (2006) Consensus design as a tool for engineering repeat proteins. Methods Mol Biol 340:151-170.
    • (2006) Methods Mol Biol , vol.340 , pp. 151-170
    • Kajander, T.1    Cortajarena, A.L.2    Regan, L.3
  • 12
    • 33749350156 scopus 로고    scopus 로고
    • Repeat motions and backbone flexibility in designed proteins with different numbers of identical consensus tetratricopeptide repeats
    • DOI 10.1021/bi060819a
    • Cheng CY, Jarymowycz VA, Cortajarena AL, Regan L, Stone MJ (2006) Repeat motions and backbone flexibility in designed proteins with different numbers of identical consensus tetratricopeptide repeats. Biochemistry 45:12175-12183. (Pubitemid 44497837)
    • (2006) Biochemistry , vol.45 , Issue.39 , pp. 12175-12183
    • Cheng, C.Y.1    Jarymowycz, V.A.2    Cortajarena, A.L.3    Regan, L.4    Stone, M.J.5
  • 13
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • Zimm BH, Bragg JK (1959) Theory of the phase transition between helix and random coil in polypeptide chains. J Chem Phys 31:526-535.
    • (1959) J Chem Phys , vol.31 , pp. 526-535
    • Zimm, B.H.1    Bragg, J.K.2
  • 14
    • 33947716431 scopus 로고
    • Beitrag zur Theorie des Ferromagnetismus
    • Ising E (1925) Beitrag zur Theorie des Ferromagnetismus. Z Phys 31:253-258.
    • (1925) Z Phys , vol.31 , pp. 253-258
    • Ising, E.1
  • 15
    • 43449134372 scopus 로고    scopus 로고
    • Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
    • Cortajarena AL, Mochrie SG, Regan L (2008) Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange. J Mol Biol 379:617-626.
    • (2008) J Mol Biol , vol.379 , pp. 617-626
    • Cortajarena, A.L.1    Mochrie, S.G.2    Regan, L.3
  • 16
    • 17644425688 scopus 로고    scopus 로고
    • Local and long-range stability in tandemly arrayed tetratricopeptide repeats
    • SEJ
    • Main ER, Stott K, SEJ, Regan L (2005) Local and long-range stability in tandemly arrayed tetratricopeptide repeats. Proc Natl Acad Sci USA 102:5721-5726.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5721-5726
    • Main, E.R.1    Stott, K.2    Regan, L.3
  • 17
    • 0029198941 scopus 로고
    • Differential scanning calorimetry
    • Freire E (1995) Differential scanning calorimetry. Methods Mol Biol 40:191-218.
    • (1995) Methods Mol Biol , vol.40 , pp. 191-218
    • Freire, E.1
  • 18
    • 0029203156 scopus 로고
    • Differential scanning calorimetry of proteins
    • Sanchez-Ruiz J (1995) Differential scanning calorimetry of proteins. Subcell Biochem 24:133-176.
    • (1995) Subcell Biochem , vol.24 , pp. 133-176
    • Sanchez-Ruiz, J.1
  • 19
    • 0029147930 scopus 로고
    • Energetics of protein structure
    • Makhatadze G, Privalov P (1995) Energetics of protein structure. Adv Prot Chem 47:307-425.
    • (1995) Adv Prot Chem , vol.47 , pp. 307-425
    • Makhatadze, G.1    Privalov, P.2
  • 20
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • Privalov PL, Khechinashvili NN (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol 86:665-684.
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 21
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov PL (1979) Stability of proteins: small globular proteins. Adv Prot Chem 33:167-241.
    • (1979) Adv Prot Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 22
    • 0031957916 scopus 로고    scopus 로고
    • Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1
    • Cziepluch C, Kordes E, Poirey R, Grewenig A, Rommelaere J, Jauniaux J (1998) Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1. J Virol 72:4149-4159.
    • (1998) J Virol , vol.72 , pp. 4149-4159
    • Cziepluch, C.1    Kordes, E.2    Poirey, R.3    Grewenig, A.4    Rommelaere, J.5    Jauniaux, J.6
  • 24
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci 4:2138-2148.
    • (1995) Protein Sci , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 25
    • 49349102875 scopus 로고    scopus 로고
    • Extensive non-native polyproline II secondary structure induces compaction of a protein's denatured state
    • Cortajarena AL, Lois G, Sherman E, O'Hern CS, Regan L, Haran G (2008) Extensive non-native polyproline II secondary structure induces compaction of a protein's denatured state. J Mol Biol 382:203-212.
    • (2008) J Mol Biol , vol.382 , pp. 203-212
    • Cortajarena, A.L.1    Lois, G.2    Sherman, E.3    O'Hern, C.S.4    Regan, L.5    Haran, G.6
  • 26
    • 0035807936 scopus 로고    scopus 로고
    • Studies of the ankyrin repeats of the Drosophila melanogaster notch receptor. 2. Solution stability and cooperativity of unfolding
    • Zweifel ME, Barrick D (2001) Studies of the ankyrin repeats of the Drosophila melanogaster notch receptor. 2. Solution stability and cooperativity of unfolding. Biochemistry 40:14357-14367.
    • (2001) Biochemistry , vol.40 , pp. 14357-14367
    • Zweifel, M.E.1    Barrick, D.2
  • 27
    • 0036438808 scopus 로고    scopus 로고
    • Limits of cooperativity in a structurally modular protein: Response of the Notch ankyrin domain to analogous alanine substitutions in each repeat
    • Bradley CM, Barrick D (2002) Limits of cooperativity in a structurally modular protein: response of the Notch ankyrin domain to analogous alanine substitutions in each repeat. J Mol Biol 324:373-386.
    • (2002) J Mol Biol , vol.324 , pp. 373-386
    • Bradley, C.M.1    Barrick, D.2
  • 28
    • 4644306518 scopus 로고    scopus 로고
    • An experimentally determined protein folding energy landscape
    • Mello CC, Barrick D (2004) An experimentally determined protein folding energy landscape. Proc Natl Acad Sci USA 101:14102-14107.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14102-14107
    • Mello, C.C.1    Barrick, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.