메뉴 건너뛰기




Volumn 107, Issue 11, 2010, Pages 4908-4913

Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity

Author keywords

Conformational stability; Ligand binding affinity; Linkage analysis; Thermal stability; Thiol protection

Indexed keywords

BINDING PROTEIN; MALTOSE BINDING PROTEIN; NUCLEASE; RIBOSE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 77950440622     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910421107     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman J (1964) Linked functions and reciprocal effects in hemoglobin: A second look. Adv Protein Chem 19:223-286.
    • (1964) Adv Protein Chem , vol.19 , pp. 223-286
    • Wyman, J.1
  • 2
    • 0016699207 scopus 로고
    • Macromolecular Binding
    • Schellman JA (1975) Macromolecular Binding. Biopolymers 14(5):999-1018.
    • (1975) Biopolymers , vol.14 , Issue.5 , pp. 999-1018
    • Schellman, J.A.1
  • 3
    • 0004244695 scopus 로고
    • University Science Books,Mill Valley, CA
    • Wyman J, Gill SJ (1990) Binding and Linkage (University Science Books,Mill Valley, CA) p 330.
    • (1990) Binding and Linkage , pp. 330
    • Wyman, J.1    Gill, S.J.2
  • 5
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt A, Neilson SO (1966) Hydrogen exchange in proteins. Adv Protein Chem 21:287-386.
    • (1966) Adv Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Neilson, S.O.2
  • 7
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • SwintKruse L, Robertson AD (1996) Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry-US 35(1):171-180.
    • (1996) Biochemistry-US , vol.35 , Issue.1 , pp. 171-180
    • Swintkruse, L.1    Robertson, A.D.2
  • 8
    • 0032876680 scopus 로고    scopus 로고
    • Protein conformational stabilities can be determined from hydrogen exchange rates
    • Huyghues-Despointes BMP, Scholtz JM, Pace CN (1999) Protein conformational stabilities can be determined from hydrogen exchange rates. Nat Struct Biol 6(10):910-912.
    • (1999) Nat Struct Biol , vol.6 , Issue.10 , pp. 910-912
    • Huyghues-Despointes, B.M.P.1    Scholtz, J.M.2    Pace, C.N.3
  • 10
    • 0031853168 scopus 로고    scopus 로고
    • Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange
    • Ha JH, Loh SN (1998) Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange. Nat Struct Biol 5(8):730-737.
    • (1998) Nat Struct Biol , vol.5 , Issue.8 , pp. 730-737
    • Ha, J.H.1    Loh, S.N.2
  • 11
    • 0035900542 scopus 로고    scopus 로고
    • On the nature of conformational openings: Native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin
    • Feng ZY, Butler MC, Alam SL, Loh SN (2001) On the nature of conformational openings: Native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin. J Mol Biol 314(1):153-166.
    • (2001) J Mol Biol , vol.314 , Issue.1 , pp. 153-166
    • Feng, Z.Y.1    Butler, M.C.2    Alam, S.L.3    Loh, S.N.4
  • 12
    • 0037022179 scopus 로고    scopus 로고
    • Unfolding rates of barstar determined in native and low denaturant conditions indicate the presence of intermediates
    • DOI 10.1021/bi011494v
    • Sridevi K, Udgaonkar JB (2002) Unfolding rates of barstar determined in native and low denaturant conditions indicate the presence of intermediates. Biochemistry-US 41(5):1568-1578. (Pubitemid 34112746)
    • (2002) Biochemistry , vol.41 , Issue.5 , pp. 1568-1578
    • Sridevi, K.1    Udgaonkar, J.B.2
  • 13
    • 38049108092 scopus 로고    scopus 로고
    • Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry
    • Jha SK, Udgaonkar JB (2007) Exploring the cooperativity of the fast folding reaction of a small protein using pulsed thiol labeling and mass spectrometry. J Biol Chem 282(52):37479-37491.
    • (2007) J Biol Chem , vol.282 , Issue.52 , pp. 37479-37491
    • Jha, S.K.1    Udgaonkar, J.B.2
  • 15
    • 6344285316 scopus 로고    scopus 로고
    • Probing the high energy states in proteins by proteolysis
    • DOI 10.1016/j.jmb.2004.08.085, PII S002228360401085X
    • Park C, Marqusee S (2004) Probing the high energy states in proteins by proteolysis. J Mol Biol 343:1467-1476. (Pubitemid 39387837)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1467-1476
    • Park, C.1    Marqusee, S.2
  • 17
    • 0032766705 scopus 로고    scopus 로고
    • Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c
    • DOI 10.1006/jmbi.1999.2924
    • Milne JS, Xu YJ, Mayne LC, Englander SW (1999) Experimental study of the protein folding landscape: Unfolding reactions in cytochrome c. J Mol Biol 290(3):811-822. (Pubitemid 29355709)
    • (1999) Journal of Molecular Biology , vol.290 , Issue.3 , pp. 811-822
    • Milne, J.S.1    Xu, Y.2    Mayne, L.C.3    Englander, S.W.4
  • 18
    • 0018588511 scopus 로고
    • Stability of proteins
    • Privalov P (1979) Stability of proteins. Adv Protein Chem 33:167-241.
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.1
  • 19
    • 0030971891 scopus 로고    scopus 로고
    • Possible origin of differences between van't Hoff and calorimetric enthalpy estimates
    • Chaires JB (1997) Possible origin of differences between van't Hoff and calorimetric enthalpy estimates. Biophys Chem 64(1-3):15-23.
    • (1997) Biophys Chem , vol.64 , Issue.1-3 , pp. 15-23
    • Chaires, J.B.1
  • 22
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in stability from thermophilic proteins
    • Razvi A, Scholtz JM (2006) Lessons in stability from thermophilic proteins. Protein Sci 15(7):1569-1578.
    • (2006) Protein Sci , vol.15 , Issue.7 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 23
    • 0035000257 scopus 로고    scopus 로고
    • Some thermodynamic implications for the thermostability of proteins
    • DOI 10.1110/ps.180101
    • Rees D, Robertson AD (2001) Some thermodynamic implications for the thermostability of proteins. Protein Sci 10:1187-1194. (Pubitemid 32476479)
    • (2001) Protein Science , vol.10 , Issue.6 , pp. 1187-1194
    • Rees, D.C.1    Robertson, A.D.2
  • 24
    • 44349104231 scopus 로고    scopus 로고
    • p, of protein unfolding and validation across a wide temperature range
    • p, of protein unfolding and validation across a wide temperature range. Proteins 71(4):1607-1616.
    • (2008) Proteins , vol.71 , Issue.4 , pp. 1607-1616
    • Talla-Singh, D.1    Stites, W.E.2
  • 25
    • 35148850244 scopus 로고    scopus 로고
    • Identification and thermodynamic characterization of molten globule states of periplasmic binding proteins
    • DOI 10.1021/bi700577m
    • Prajapati RS, Indu S, Varadarajan R (2007) Identification and thermodynamic characterization of molten globule states of periplasmic binding proteins. Biochemistry-US 46(36):10339-10352. (Pubitemid 350067627)
    • (2007) Biochemistry , vol.46 , Issue.36 , pp. 10339-10352
    • Prajapati, R.S.1    Indu, S.2    Varadarajan, R.3
  • 26
    • 0026755510 scopus 로고
    • Contributions of the polar, uncharged aminoacids to the stability of Staphylococcal nuclease - Evidence for mutational effects on the free-energy of the denatured state
    • Green SM, Meeker AK, Shortle D (1992) Contributions of the polar, uncharged aminoacids to the stability of Staphylococcal nuclease - evidence for mutational effects on the free-energy of the denatured state. Biochemistry-US 31(25):5717-5728.
    • (1992) Biochemistry-US , vol.31 , Issue.25 , pp. 5717-5728
    • Green, S.M.1    Meeker, A.K.2    Shortle, D.3
  • 28
    • 0030445415 scopus 로고    scopus 로고
    • Stability and folding of a mutant ribose-binding protein of Escherichia coli
    • DOI 10.1007/BF01887146
    • Kim JS, Kim H (1996) Stability and folding of a mutant ribose-binding protein of Escherichia coli. J Protein Chem 15(8):731-736. (Pubitemid 27027129)
    • (1996) Journal of Protein Chemistry , vol.15 , Issue.8 , pp. 731-736
    • Kim, J.-S.1    Kim, H.2
  • 29
  • 30
    • 0038333283 scopus 로고    scopus 로고
    • Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics
    • Waldron TT, Murphy KP (2003) Stabilization of proteins by ligand binding: Application to drug screening and determination of unfolding energetics. Biochemistry-US 42(17):5058-5064.
    • (2003) Biochemistry-US , vol.42 , Issue.17 , pp. 5058-5064
    • Waldron, T.T.1    Murphy, K.P.2
  • 32
    • 0019321060 scopus 로고
    • Substrate stabilization of lysozyme to thermal and guanidine- hydrochloride denaturation
    • Pace CN, McGrath T (1980) Substrate stabilization of lysozyme to thermal and guanidine-hydrochloride denaturation. J Biol Chem 255(9):3862-3865.
    • (1980) J Biol Chem , vol.255 , Issue.9 , pp. 3862-3865
    • Pace, C.N.1    McGrath, T.2
  • 33
    • 0014198139 scopus 로고
    • Catalytic properties and specificty of extracellular nuclease of Staphylococcus aureus
    • Cuatrecasas P, Fuchs S, Anfinsen CB (1967) Catalytic properties and specificty of extracellular nuclease of Staphylococcus aureus. J Biol Chem 242(7):1541-1547.
    • (1967) J Biol Chem , vol.242 , Issue.7 , pp. 1541-1547
    • Cuatrecasas, P.1    Fuchs, S.2    Anfinsen, C.B.3
  • 34
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli Cytoplasmic Environment Activates Long-Lived and Efficient Cell-Free Protein Synthesis
    • DOI 10.1002/bit.20026
    • Jewett M, Swartz J (2004) Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86(1):19-26. (Pubitemid 38339387)
    • (2004) Biotechnology and Bioengineering , vol.86 , Issue.1 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 36
    • 0023714467 scopus 로고
    • A short polypeptide marker sequence useful for recombinant protein identification and purification
    • Hopp T, et al. (1988) A short polypeptide marker sequence useful for recombinant protein identification and purification. Nat Biotechnol 6(10):1204-1210.
    • (1988) Nat Biotechnol , vol.6 , Issue.10 , pp. 1204-1210
    • Hopp, T.1
  • 37
    • 0041935939 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Bethesda, Maryland
    • Rasband W (1997-2009) ImageJ (U.S. National Institutes of Health, Bethesda, Maryland).
    • (1997) ImageJ
    • Rasband, W.1
  • 38
    • 0027179892 scopus 로고
    • Mechanism of the reaction catalyzed by staphylococcal nuclease: Identification of the rate-determining step
    • Hale S, Poole L, Gerlt J (1993) Mechanism of the reaction catalyzed by Staphylococcal nuclease: Identification of the rate-limiting step. Biochem J 32(29):7479-7487. (Pubitemid 23232322)
    • (1993) Biochemistry , vol.32 , Issue.29 , pp. 7479-7487
    • Hale, S.P.1    Poole, L.B.2    Gerlt, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.