메뉴 건너뛰기




Volumn 19, Issue 10, 2010, Pages 1996-2000

Protein-protein binding affinities by pulse proteolysis: Application to TEM-1/BLIP protein complexes

Author keywords

Binding affinity; BLIP; Dissociation constant; Protein stability; Pulse proteolysis; TEM 1

Indexed keywords

BETA LACTAMASE; BETA LACTAMASE TEM 1; PROTEIN BLIP; UNCLASSIFIED DRUG;

EID: 77957292926     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.467     Document Type: Article
Times cited : (7)

References (11)
  • 1
    • 77950440622 scopus 로고    scopus 로고
    • Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity
    • Isom D, Vardy E, Oas T, Hellinga HW (2010) Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. Proc Natl Acad Sci USA 107:4908-4913.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4908-4913
    • Isom, D.1    Vardy, E.2    Oas, T.3    Hellinga, H.W.4
  • 2
    • 18744391410 scopus 로고    scopus 로고
    • Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
    • DOI 10.1038/nmeth740
    • Park C, Marqusee S (2005) Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding. Nat Methods 2:207-212. (Pubitemid 41122128)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 207-212
    • Park, C.1    Marqusee, S.2
  • 3
    • 44949229448 scopus 로고    scopus 로고
    • Thermodynamic analysis of protein stability and ligand binding using a chemical modification- And mass spectrometry-based strategy
    • DOI 10.1021/ac702610a
    • West GM, Tang L, Fitzgerald MC (2008) Thermodynamic analysis of protein stability and ligand binding using a chemical modification- and mass spectrometry-based strategy. Analyt Chem 80:4175-4185. (Pubitemid 351812772)
    • (2008) Analytical Chemistry , vol.80 , Issue.11 , pp. 4175-4185
    • West, G.M.1    Tang, L.2    Fitzgerald, M.C.3
  • 4
    • 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 255:3862-3865.
    • (1980) J Biol Chem , vol.255 , pp. 3862-3865
    • Pace, C.N.1    McGrath, T.2
  • 5
    • 77957305225 scopus 로고    scopus 로고
    • Quantitative determination of protein stability and ligand binding by pulse proteolysis
    • Park C, Marqusee S (2006) Quantitative determination of protein stability and ligand binding by pulse proteolysis. Curr Protoc Protein Sci 46:20.11.21-20.11.14.
    • (2006) Curr Protoc Protein Sci , vol.46
    • Park, C.1    Marqusee, S.2
  • 6
    • 0033524394 scopus 로고    scopus 로고
    • Biophysical characterization of the interaction of the β-lactamase TEM- 1 with its protein inhibitor BLIP
    • DOI 10.1021/bi981772z
    • Albeck S, Schreiber G (1999) Biophysical characterization of the interaction of the β-lactamase TEM-1 with its protein inhibitor BLIP. Biochemistry 38:11-21. (Pubitemid 29035666)
    • (1999) Biochemistry , vol.38 , Issue.1 , pp. 11-21
    • Albeck, S.1    Schreiber, G.2
  • 7
    • 0242580779 scopus 로고    scopus 로고
    • Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 β-lactamase with β-lactamase inhibitory protein
    • Zhang Z, Palzkill T (2003) Determinants of binding affinity and specificity for the interaction of TEM-1 and SME-1 β-lactamase with β-lactamase inhibitory protein. J Biol Chem 278:45706-45712.
    • (2003) J Biol Chem , vol.278 , pp. 45706-45712
    • Zhang, Z.1    Palzkill, T.2
  • 8
    • 0032539580 scopus 로고    scopus 로고
    • A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 β-lactamase
    • Vanhove M, Lejeune A, Guillaume G, Virden R, Pain RH, Schmid FX, Frere J-M (1998) A collapsed intermediate with nonnative packing of hydrophobic residues in the folding of TEM-1 β-lactamase. Biochemistry 37:1941-1950.
    • (1998) Biochemistry , vol.37 , pp. 1941-1950
    • Vanhove, M.1    Lejeune, A.2    Guillaume, G.3    Virden, R.4    Pain, R.H.5    Schmid, F.X.6    Frere, J.-M.7
  • 9
    • 0029063334 scopus 로고
    • Investigation of the folding pathway of the TEM-1 β-lactamase
    • Vanhove M, Raquet X, Frere J-M (1995) Investigation of the folding pathway of the TEM-1 β-lactamase. Proteins 22:110-118.
    • (1995) Proteins , vol.22 , pp. 110-118
    • Vanhove, M.1    Raquet, X.2    Frere, J.-M.3
  • 10
    • 27644593486 scopus 로고    scopus 로고
    • Protein quantification and its tolerance for different interfering reagents using the BCA-method with regard to 2D SDS PAGE
    • DOI 10.1016/j.jbbm.2005.08.005, PII S0165022X05001302
    • Krieg RC, Dong Y, Schwamborn K, Knuechel R (2005) Protein quantification and its tolerance for different interfering reagents using the BCA-method with regard to 2D SDS PAGE. J Biochem Biophys Met 65:13-19. (Pubitemid 41562866)
    • (2005) Journal of Biochemical and Biophysical Methods , vol.65 , Issue.1 , pp. 13-19
    • Krieg, R.C.1    Dong, Y.2    Schwamborn, K.3    Knuechel, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.