메뉴 건너뛰기




Volumn 106, Issue 30, 2009, Pages 12289-12294

Direct evidence for a dry molten globule intermediate during the unfolding of a small protein

Author keywords

Continuous transition; Protein unfolding; Single chain monellin; Steady state FRET

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GUANIDINE; MONELLIN; TRYPTOPHAN;

EID: 68149147539     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0905744106     Document Type: Article
Times cited : (120)

References (42)
  • 1
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W (1959) Some factors in the interpretation of protein denaturation. Adv Protein Chem 14:1-63.
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 2
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C (1968) Protein denaturation. Adv Protein Chem 23:121-242.
    • (1968) Adv Protein Chem , vol.23 , pp. 121-242
    • Tanford, C.1
  • 3
    • 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
  • 4
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov PL (1979) Stability of proteins: Small globular proteins. Adv Protein Chem33:167-241.
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 5
    • 0028931751 scopus 로고
    • Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange
    • Kiefhaber T, Baldwin RL (1995) Kinetics of hydrogen bond breakage in the process of unfolding of ribonuclease A measured by pulsed hydrogen exchange. Proc Natl Acad Sci USA 92:2657-2661.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 2657-2661
    • Kiefhaber, T.1    Baldwin, R.L.2
  • 6
    • 0024745242 scopus 로고
    • Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution
    • Finkelstein AV, Shakhnovich EI (1989) Theory of cooperative transitions in protein molecules. II. Phase diagram for a protein molecule in solution. Biopolymers 28:1681-1694.
    • (1989) Biopolymers , vol.28 , pp. 1681-1694
    • Finkelstein, A.V.1    Shakhnovich, E.I.2
  • 7
    • 0024742246 scopus 로고
    • Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition
    • Shakhnovich EI, Finkelstein AV (1989) Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition. Biopolymers 28:1667-1680.
    • (1989) Biopolymers , vol.28 , pp. 1667-1680
    • Shakhnovich, E.I.1    Finkelstein, A.V.2
  • 8
    • 68149163431 scopus 로고    scopus 로고
    • Cooperative transitions in protein molecules
    • Academic, London, pp
    • Finkelstein AV, Ptitsyn OB (2002) Cooperative transitions in protein molecules. Protein Physics (Academic, London), pp 205-277.
    • (2002) Protein Physics , pp. 205-277
    • Finkelstein, A.V.1    Ptitsyn, O.B.2
  • 9
    • 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 375:513-515.
    • (1995) Nature , vol.375 , pp. 513-515
    • Kiefhaber, T.1    Labhardt, A.M.2    Baldwin, R.L.3
  • 10
    • 0029079665 scopus 로고
    • 19F-tryptophan-labeled Escherichia coli dihydrofolate reductase
    • 19F-tryptophan-labeled Escherichia coli dihydrofolate reductase. Proc Natl Acad Sci USA 92:9318-9322.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9318-9322
    • Hoeltzli, S.D.1    Frieden, C.2
  • 11
    • 0037065672 scopus 로고    scopus 로고
    • Mechanism of formation of a productive molten globule form of barstar
    • Rami BR, Udgaonkar JB (2002) Mechanism of formation of a productive molten globule form of barstar. Biochemistry 41:1710-1716.
    • (2002) Biochemistry , vol.41 , pp. 1710-1716
    • Rami, B.R.1    Udgaonkar, J.B.2
  • 12
    • 0030964627 scopus 로고    scopus 로고
    • Real-time measurement of multiple intra-molecular distances during protein folding reactions: A multisite stopped-flow fluorescence energy-transfer study of yeast phosphoglycerate kinase
    • Lillo MP, Szpikowska BK, Mas MT, Sutin JD, Beechem JM (1997) Real-time measurement of multiple intra-molecular distances during protein folding reactions: A multisite stopped-flow fluorescence energy-transfer study of yeast phosphoglycerate kinase. Biochemistry 36:11273-11281.
    • (1997) Biochemistry , vol.36 , pp. 11273-11281
    • Lillo, M.P.1    Szpikowska, B.K.2    Mas, M.T.3    Sutin, J.D.4    Beechem, J.M.5
  • 15
    • 0037452559 scopus 로고    scopus 로고
    • Surface expansion is independent of and occurs faster than core solvation during the unfolding of barstar
    • Sridevi K, Udgaonkar JB (2003) Surface expansion is independent of and occurs faster than core solvation during the unfolding of barstar. Biochemistry 42:1551-1563.
    • (2003) Biochemistry , vol.42 , pp. 1551-1563
    • Sridevi, K.1    Udgaonkar, J.B.2
  • 16
    • 1542358783 scopus 로고    scopus 로고
    • Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble
    • Sridevi K, Lakshmikanth GS, Krishnamoorthy G, Udgaonkar JB (2004) Increasing stability reduces conformational heterogeneity in a protein folding intermediate ensemble. J Mol Biol 337:699-711.
    • (2004) J Mol Biol , vol.337 , pp. 699-711
    • Sridevi, K.1    Lakshmikanth, G.S.2    Krishnamoorthy, G.3    Udgaonkar, J.B.4
  • 17
    • 26244466045 scopus 로고    scopus 로고
    • Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: Evidence for a continuous transition
    • Sinha KK, Udgaonkar JB (2005) Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: Evidence for a continuous transition. J Mol Biol 353:704-718.
    • (2005) J Mol Biol , vol.353 , pp. 704-718
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 18
    • 34249748424 scopus 로고    scopus 로고
    • Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements
    • Sinha KK, Udgaonkar JB (2007) Dissecting the non-specific and specific components of the initial folding reaction of barstar by multi-site FRET measurements. J Mol Biol 370:385-405.
    • (2007) J Mol Biol , vol.370 , pp. 385-405
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 19
    • 40049106475 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of the folding pathway of Engrailed Homeodomain
    • Huang F, Settanni G, Fersht AR (2008) Fluorescence resonance energy transfer analysis of the folding pathway of Engrailed Homeodomain. Protein Eng Des Sel 21:131-146.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 131-146
    • Huang, F.1    Settanni, G.2    Fersht, A.R.3
  • 20
    • 14544272814 scopus 로고    scopus 로고
    • Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin
    • Kimura T, et al. (2005) Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin. Proc Natl Acad Sci USA 102:2748-2753.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2748-2753
    • Kimura, T.1
  • 21
    • 35448932093 scopus 로고    scopus 로고
    • Characterization of the folding and unfolding reactions of single-chain monellin: Evidence for multiple intermediates and competing pathways
    • Patra AK, Udgaonkar JB (2007) Characterization of the folding and unfolding reactions of single-chain monellin: Evidence for multiple intermediates and competing pathways. Biochemistry 46:11727-11743.
    • (2007) Biochemistry , vol.46 , pp. 11727-11743
    • Patra, A.K.1    Udgaonkar, J.B.2
  • 22
    • 51649090393 scopus 로고    scopus 로고
    • Dehydration of main-chain amides in the final folding step of single-chain monellin revealed by time-resolved infrared spectroscopy
    • Kimura T, et al. (2008) Dehydration of main-chain amides in the final folding step of single-chain monellin revealed by time-resolved infrared spectroscopy. Proc Natl Acad Sci USA 105:13391-13396.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13391-13396
    • Kimura, T.1
  • 23
    • 0017178548 scopus 로고
    • Three-state denaturation of α-lact-albumin by guanidine hydrochloride
    • Kuwajima K, Nitta K, Yoneyama M, Sugai S (1976) Three-state denaturation of α-lact-albumin by guanidine hydrochloride. J Mol Biol 106:359-373.
    • (1976) J Mol Biol , vol.106 , pp. 359-373
    • Kuwajima, K.1    Nitta, K.2    Yoneyama, M.3    Sugai, S.4
  • 24
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB (1995) Molten globule and protein folding. Adv Protein Chem 47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 25
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interactions
    • Privalov PL, Gill SJ (1988) Stability of protein structure and hydrophobic interactions. Adv Protein Chem 39:191-234.
    • (1988) Adv Protein Chem , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 26
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA (1990) Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 27
    • 0027250627 scopus 로고
    • Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration
    • Privalov PL, Makhatadze GI (1993) Contribution of hydration to protein folding thermodynamics. II. The entropy and Gibbs energy of hydration. J Mol Biol 232:660-679.
    • (1993) J Mol Biol , vol.232 , pp. 660-679
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 28
    • 33947476272 scopus 로고
    • The factors affecting the stability of hydrogen-bonded polypeptide structures in aqueous solution
    • Schellman JA (1958) The factors affecting the stability of hydrogen-bonded polypeptide structures in aqueous solution. J Phys Chem 62:1485-1494.
    • (1958) J Phys Chem , vol.62 , pp. 1485-1494
    • Schellman, J.A.1
  • 29
    • 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
  • 30
    • 59049097904 scopus 로고    scopus 로고
    • Local conformational dynamics in α-helices measured by fast triplet transfer
    • Fierz B, Reiner A, Kiefhaber T (2009) Local conformational dynamics in α-helices measured by fast triplet transfer. Proc Natl Acad Sci USA 106:1057-1062.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1057-1062
    • Fierz, B.1    Reiner, A.2    Kiefhaber, T.3
  • 32
    • 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 105:16928-16933.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16928-16933
    • Hua, L.1    Zhou, R.2    Thirumalai, D.3    Berne, B.J.4
  • 33
    • 0037424614 scopus 로고    scopus 로고
    • Computational simulation of the statistical properties of unfolded proteins
    • Goldenberg DP (2003) Computational simulation of the statistical properties of unfolded proteins. J Mol Biol 326:1615-1633.
    • (2003) J Mol Biol , vol.326 , pp. 1615-1633
    • Goldenberg, D.P.1
  • 35
    • 4444276136 scopus 로고    scopus 로고
    • Effect of salt on the urea-unfolded form of barstar probed by m value measurements
    • Pradeep L, Udgaonkar JB (2004) Effect of salt on the urea-unfolded form of barstar probed by m value measurements. Biochemistry 43:11393-11402.
    • (2004) Biochemistry , vol.43 , pp. 11393-11402
    • Pradeep, L.1    Udgaonkar, J.B.2
  • 36
    • 33646171099 scopus 로고    scopus 로고
    • Characterization of intramolecular distances and site-specific dynamics in chemically unfolded barstar: Evidence for denaturant-dependent non-random structure
    • Saxena AM, Udgaonkar JB, Krishnamoorthy G (2006) Characterization of intramolecular distances and site-specific dynamics in chemically unfolded barstar: Evidence for denaturant-dependent non-random structure. J Mol Biol 359:174-189.
    • (2006) J Mol Biol , vol.359 , pp. 174-189
    • Saxena, A.M.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 37
    • 0001738398 scopus 로고    scopus 로고
    • Formation of helical states in wormlike polymer chains
    • Kemp JP, Chen ZY (1998) Formation of helical states in wormlike polymer chains. Phys Rev Lett 81:3880-3883.
    • (1998) Phys Rev Lett , vol.81 , pp. 3880-3883
    • Kemp, J.P.1    Chen, Z.Y.2
  • 38
    • 47749149231 scopus 로고    scopus 로고
    • α-helix folding in the presence of structural constraints
    • Ihalainen JA, et al. (2008) α-helix folding in the presence of structural constraints. Proc Natl Acad Sci USA 105:9588-9593.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9588-9593
    • Ihalainen, J.A.1
  • 39
    • 45849127598 scopus 로고    scopus 로고
    • Barrierless evolution of structure during the submillisecond refolding reaction of a small protein
    • Sinha KK, Udgaonkar JB (2008) Barrierless evolution of structure during the submillisecond refolding reaction of a small protein. Proc Natl Acad Sci USA 105:7998-8003.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7998-8003
    • Sinha, K.K.1    Udgaonkar, J.B.2
  • 40
    • 44949102307 scopus 로고    scopus 로고
    • Temperature-dependent downhill unfolding of ubiquitin. II. Modeling the free energy surface
    • Chung HS, Tokmakoff A (2008) Temperature-dependent downhill unfolding of ubiquitin. II. Modeling the free energy surface. Proteins 72:488-497.
    • (2008) Proteins , vol.72 , pp. 488-497
    • Chung, H.S.1    Tokmakoff, A.2
  • 41
    • 84984082911 scopus 로고
    • Statistical mechanics of non-covalent bonds in polyamino acids. IX. The two-state theory of protein denaturation
    • Poland DC, Scheraga HA (1965) Statistical mechanics of non-covalent bonds in polyamino acids. IX. The two-state theory of protein denaturation. Biopolymers 3:401-419.
    • (1965) Biopolymers , vol.3 , pp. 401-419
    • Poland, D.C.1    Scheraga, H.A.2
  • 42
    • 67651087326 scopus 로고    scopus 로고
    • Continuous dissolution of structure during the unfolding of a small protein
    • Jha SK, Dhar D, Krishnamoorthy G, Udgaonkar JB (2009) Continuous dissolution of structure during the unfolding of a small protein. Proc Natl Acad Sci USA 106:11113-11118.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11113-11118
    • Jha, S.K.1    Dhar, D.2    Krishnamoorthy, G.3    Udgaonkar, J.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.