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Volumn 89, Issue 1, 2001, Pages 77-85

No effect of trimethylamine N-oxide on the internal dynamics of the protein native fold

Author keywords

Acrylamide quenching; Osmolytes; Phosphorescence; Protein dynamics; Protein stability; Trimethylamine N oxide

Indexed keywords

TRIMETHYLAMINE OXIDE;

EID: 0035977663     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(00)00219-2     Document Type: Article
Times cited : (14)

References (35)
  • 2
    • 0006370469 scopus 로고    scopus 로고
    • L.J. Borowitzka, in: R. Gilles, M. Gilles-Baillien (Eds.), Transport processes, iono- and osmoregulation, glycerol and other carbohydrate osmotic effectors, Springer-Verlag, Berlin, 1985, p. 437.
  • 4
    • 0018474573 scopus 로고
    • Solute compatibility with enzyme function and structure: rationales for selection of osmotic agent and end-product of anaerobic metabolism in marine invertebrates
    • (1979) J. Exp. Zool. , vol.208 , pp. 137-151
    • Bowlus, R.D.1    Somero, G.N.2
  • 6
    • 0029812281 scopus 로고    scopus 로고
    • Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigma
    • (1996) Biophys. J. , vol.71 , pp. 2117-2122
    • Wang, A.1    Bolen, D.W.2
  • 7
    • 0028150954 scopus 로고
    • Why do some organisms use a urea-methylamine mixture as osmolytes: thermodynamic compensation of urea and Trimethylamine N-oxide interactions with protein
    • (1994) Biochemistry , vol.33 , pp. 12695-12701
    • Lin, T.Y.1    Timasheff, S.N.2
  • 8
    • 0030762556 scopus 로고    scopus 로고
    • A natural occurring protective system in urea-rich cells: mechanism of osmolytes protection of protein against urea denaturation
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 9
    • 0031965750 scopus 로고    scopus 로고
    • Time-dependent effects of Trimethylamine N-oxide/urea on lactate dehydrogenase activity: an unexplored dimension of the adaptation paradigm
    • (1998) Biophys. J. , vol.74 , pp. 2655-2658
    • Baskakov, I.1    Bolen, D.W.2
  • 10
    • 0031967834 scopus 로고    scopus 로고
    • Trimethyl-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis
    • (1998) Biophys. J. , vol.74 , pp. 2666-2673
    • Baskakov, I.1    Wang, A.2    Bolen, D.W.3
  • 12
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 16
    • 0032884397 scopus 로고    scopus 로고
    • Probing the conformation of a human apolipoprotein C-1 by amino acid substitutions and Trimethylamine-N-oxide
    • (1999) Protein Sci. , vol.8 , pp. 2055-2064
    • Gursky, O.1
  • 29
    • 0019011405 scopus 로고
    • Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants
    • (1980) Biopolymers , vol.19 , pp. 1049-1068
    • Knox, D.G.1    Rosenberg, A.2
  • 31
    • 0023700230 scopus 로고
    • The influence of glycerol on hydrogen isotope exchange in lysozyme
    • (1988) Biopolymers , vol.27 , pp. 1699-1709
    • Gregory, R.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.