메뉴 건너뛰기




Volumn 108, Issue 3, 2011, Pages 481-490

Chimeric avidin shows stability against harsh chemical conditions-biochemical analysis and 3D structure

Author keywords

Avidin biotin; Nanobiotechnology; Protein engineering; Thermodynamics; X ray structure

Indexed keywords

3D STRUCTURE; AVIDIN-BIOTIN; BIOCHEMICAL ANALYSIS; CHEMICAL CONDITIONS; E. COLI; ELEVATED TEMPERATURE; ISOTHERMAL TITRATION CALORIMETRY; LIFE-SCIENCES; LIGAND BINDING; NEW APPLICATIONS; PILOT-SCALE PRODUCTION; POTENTIAL TOOL; PROTEIN ENGINEERING; STREPTAVIDIN; X-RAY STRUCTURE;

EID: 78751523876     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22962     Document Type: Article
Times cited : (35)

References (35)
  • 1
    • 0347148007 scopus 로고
    • Protein structure, folding, and design: Proceedings of a Genex-UCLA Symposium
    • In: Oxender DL, editor. New York, Liss, A. L.
    • Ahern TJ, Klibanov AM. 1986. Why do enzymes irreversibly inactivate at high temperature? In: Oxender DL, editor. Protein structure, folding, and design: Proceedings of a Genex-UCLA Symposium. New York: Liss, A. L. p. 283-289.
    • (1986) Why do enzymes irreversibly inactivate at high temperature? , pp. 283-289
    • Ahern, T.J.1    Klibanov, A.M.2
  • 2
    • 0025353404 scopus 로고
    • The basis for toxicity of certain cryoprotectants: A hypothesis
    • Arakawa T, Carpenter JF, Kita YA, Crowe JH. 1990. The basis for toxicity of certain cryoprotectants: A hypothesis. Cryobiology 27:401-415.
    • (1990) Cryobiology , vol.27 , pp. 401-415
    • Arakawa, T.1    Carpenter, J.F.2    Kita, Y.A.3    Crowe, J.H.4
  • 3
    • 0034727681 scopus 로고    scopus 로고
    • Methanol-induced conformations of myoglobin at pH 4.0
    • Babu KR, Douglas DJ. 2000. Methanol-induced conformations of myoglobin at pH 4.0. Biochemistry 39:14702-14710.
    • (2000) Biochemistry , vol.39 , pp. 14702-14710
    • Babu, K.R.1    Douglas, D.J.2
  • 4
    • 0015071141 scopus 로고
    • Biochemical effects of kidney of exposure to high concentrations of dimethyl sulphoxide
    • Baxter SJ, Lathe GH. 1971. Biochemical effects of kidney of exposure to high concentrations of dimethyl sulphoxide. Biochem Pharmacol 20:1079-1091.
    • (1971) Biochem Pharmacol , vol.20 , pp. 1079-1091
    • Baxter, S.J.1    Lathe, G.H.2
  • 5
    • 0029793803 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoretic method for assessing the quaternary state and comparative thermostability of avidin and streptavidin
    • 17370
    • Bayer EA, Ehrlich-Rogozinski S, Wilchek M. 1996. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic method for assessing the quaternary state and comparative thermostability of avidin and streptavidin. Electrophoresis 17370:1319-1324.
    • (1996) Electrophoresis , pp. 1319-1324
    • Bayer, E.A.1    Ehrlich-Rogozinski, S.2    Wilchek, M.3
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 8
    • 0026124848 scopus 로고
    • Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media
    • Chen KQ, Robinson AC, Van Dam ME, Martinez P, Economou C, Arnold FH. 1991. Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media. Biotechnol Prog 7:125-129.
    • (1991) Biotechnol Prog , vol.7 , pp. 125-129
    • Chen, K.Q.1    Robinson, A.C.2    Van Dam, M.E.3    Martinez, P.4    Economou, C.5    Arnold, F.H.6
  • 9
  • 13
    • 0034633284 scopus 로고    scopus 로고
    • A labeling, detection, and purification system based on 4-hydroxyazobenzene-2-carboxylic acid: An extension of the avidin-biotin system
    • Hofstetter H, Morpurgo M, Hofstetter O, Bayer EA, Wilchek M. 2000. A labeling, detection, and purification system based on 4-hydroxyazobenzene-2-carboxylic acid: An extension of the avidin-biotin system. Anal Biochem 284:354-366.
    • (2000) Anal Biochem , vol.284 , pp. 354-366
    • Hofstetter, H.1    Morpurgo, M.2    Hofstetter, O.3    Bayer, E.A.4    Wilchek, M.5
  • 17
    • 0003592534 scopus 로고
    • Dimethyl sulfoxide (basic concepts)
    • New York, Marcel Dekker Ink.
    • Jacob SW, Rosenbaum EE, Wood DC. 1971. Dimethyl sulfoxide (basic concepts). New York: Marcel Dekker Ink.
    • (1971)
    • Jacob, S.W.1    Rosenbaum, E.E.2    Wood, D.C.3
  • 18
    • 0003548906 scopus 로고    scopus 로고
    • Enzymatic reactions in organic media
    • 1st edition. Glasgow, UK, Blackie Academic & Professional.
    • Koskinen AMP, Klibanov AM. 1996. Enzymatic reactions in organic media. 1st edition. Glasgow, UK: Blackie Academic & Professional, p. 314.
    • (1996) , pp. 314
    • Koskinen, A.M.P.1    Klibanov, A.M.2
  • 19
    • 51249120701 scopus 로고    scopus 로고
    • Free sulfhydryl measurement as an indicator of antibody stability
    • Lacy ER, Baker M, Brigham-Burke M. 2008. Free sulfhydryl measurement as an indicator of antibody stability. Anal Biochem 382:66-68.
    • (2008) Anal Biochem , vol.382 , pp. 66-68
    • Lacy, E.R.1    Baker, M.2    Brigham-Burke, M.3
  • 24
    • 0027164314 scopus 로고
    • Three-dimensional structures of avidin and the avidin-biotin complex
    • 90297
    • Livnah O, Bayer EA, Wilchek M, Sussman JL. 1993. Three-dimensional structures of avidin and the avidin-biotin complex. Proc Natl Acad Sci USA 90297:5076-5080.
    • (1993) Proc Natl Acad Sci USA , pp. 5076-5080
    • Livnah, O.1    Bayer, E.A.2    Wilchek, M.3    Sussman, J.L.4
  • 26
    • 33750055009 scopus 로고    scopus 로고
    • Synthesis of a ketone analogue of biotin via the intramolecular Pauson-Khand reaction
    • McNeill E, Chen I, Ting AY. 2006. Synthesis of a ketone analogue of biotin via the intramolecular Pauson-Khand reaction. Org Lett 8:4593-4595.
    • (2006) Org Lett , vol.8 , pp. 4593-4595
    • McNeill, E.1    Chen, I.2    Ting, A.Y.3
  • 28
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. 1994. AMoRe: An automated package for molecular replacement. Acta Crystallogr A 50(2): 157-163.
    • (1994) Acta Crystallogr A , vol.50 , Issue.2 , pp. 157-163
    • Navaza, J.1
  • 29
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 276:307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS. 1999. Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6:458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 32
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant JM. 1977. Heat capacity and entropy changes in processes involving proteins. Proc Natl Acad Sci USA 74:2236-2240.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 33
    • 0015521986 scopus 로고
    • Thermochemistry of the avidin-biotin reaction
    • Suurkuusk J, Wadso I. 1972. Thermochemistry of the avidin-biotin reaction. Eur J Biochem 28:438-441.
    • (1972) Eur J Biochem , vol.28 , pp. 438-441
    • Suurkuusk, J.1    Wadso, I.2
  • 34
    • 0029555149 scopus 로고
    • Thermodynamic analysis of biotin binding to avidin. A high sensitivity titration calorimetric study
    • Swamy MJ. 1995. Thermodynamic analysis of biotin binding to avidin. A high sensitivity titration calorimetric study. Biochem Mol Biol Int 36:219-225.
    • (1995) Biochem Mol Biol Int , vol.36 , pp. 219-225
    • Swamy, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.