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Volumn 76, Issue 6, 1999, Pages 3235-3242

Tryptophan rotamer distributions in amphipathic peptides at a lipid surface

Author keywords

[No Author keywords available]

Indexed keywords

LIPID; PEPTIDE; PHOSPHATIDYLCHOLINE; TRYPTOPHAN;

EID: 0033002410     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77475-8     Document Type: Article
Times cited : (55)

References (24)
  • 1
    • 0023357309 scopus 로고
    • Interpretation of fluorescence decays in proteins using continuous lifetime distributions
    • Alcala, J. R., E. Gratton, and F. G. Prendergast. 1987a. Interpretation of fluorescence decays in proteins using continuous lifetime distributions. Biophys. J. 51:925-936.
    • (1987) Biophys. J. , vol.51 , pp. 925-936
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 2
    • 0023317270 scopus 로고
    • Fluorescence lifetime distributions in proteins
    • Alcala, J. R., E. Gratton, and F. G. Prendergast. 1987b. Fluorescence lifetime distributions in proteins. Biophys. J. 51:597-604.
    • (1987) Biophys. J. , vol.51 , pp. 597-604
    • Alcala, J.R.1    Gratton, E.2    Prendergast, F.G.3
  • 4
    • 0028298474 scopus 로고
    • The allosteric interaction between D-galactose and the Escherichia coli galactose repressor protein
    • Brown, M. P., N. Shaikh, M. Brenowitz, and L. Brand. 1994. The allosteric interaction between D-galactose and the Escherichia coli galactose repressor protein. J. Biol. Chem. 269:12600-12605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12600-12605
    • Brown, M.P.1    Shaikh, N.2    Brenowitz, M.3    Brand, L.4
  • 5
    • 0030749502 scopus 로고    scopus 로고
    • Ionization, partitioning, and dynamics of tryptophan octyl ester: Implications for membrane-bound tryptophan residues
    • Chattopadhyay, A., R. Mukherjee, R. Rukmini, J. S. Rawat, and S. Sudha. 1997. Ionization, partitioning, and dynamics of tryptophan octyl ester: implications for membrane-bound tryptophan residues. Biophys. J. 73: 839-849.
    • (1997) Biophys. J. , vol.73 , pp. 839-849
    • Chattopadhyay, A.1    Mukherjee, R.2    Rukmini, R.3    Rawat, J.S.4    Sudha, S.5
  • 6
    • 0025830305 scopus 로고
    • Fluorescence of tryptophan dipeptides: Correlations with the rotamer model
    • Chen, R. F., J. R. Knutson, H. Ziffer, and D. Porter. 1991. Fluorescence of tryptophan dipeptides: correlations with the rotamer model. Biochemistry. 30:5184-5195.
    • (1991) Biochemistry , vol.30 , pp. 5184-5195
    • Chen, R.F.1    Knutson, J.R.2    Ziffer, H.3    Porter, D.4
  • 7
    • 0032932097 scopus 로고    scopus 로고
    • The structure and orientation of class a amphipathic peptides on a phospholipid bilayer surface
    • Clayton, A. H. A., and W. H. Sawyer. 1999. The structure and orientation of class A amphipathic peptides on a phospholipid bilayer surface. Eur. Biophys. J. 28:133-141.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 133-141
    • Clayton, A.H.A.1    Sawyer, W.H.2
  • 8
    • 0029151752 scopus 로고
    • Probing local secondary structure by fluorescence: Time-resolved and circular dichroism studies of highly purified neurotoxins
    • Dahms, T. E. S., and A. G. Szabo. 1995. Probing local secondary structure by fluorescence: time-resolved and circular dichroism studies of highly purified neurotoxins. Biophys. J. 69:569-576.
    • (1995) Biophys. J. , vol.69 , pp. 569-576
    • Dahms, T.E.S.1    Szabo, A.G.2
  • 9
    • 0029167814 scopus 로고
    • Conformational heterogeneity of tryptophan in a protein crystal
    • Dahms, T. E. S., K. J. Willis, and A. G. Szabo. 1995. Conformational heterogeneity of tryptophan in a protein crystal. J. Am. Chem. Soc. 117:2321-2326.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2321-2326
    • Dahms, T.E.S.1    Willis, K.J.2    Szabo, A.G.3
  • 10
    • 0018115846 scopus 로고
    • Conformation of amino acid side-chains in proteins
    • Janin, J., S. Wodak, M. Levitt, and B. Maigrett. 1978. Conformation of amino acid side-chains in proteins. J. Mol. Biol. 125:357-386.
    • (1978) J. Mol. Biol. , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2    Levitt, M.3    Maigrett, B.4
  • 11
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation, and secondary structure in globular proteins
    • McGregor, M. J., S. A. Islam, and M. J. E. Sternberg. 1987. Analysis of the relationship between side-chain conformation, and secondary structure in globular proteins. J. Mol. Biol. 198:295-310.
    • (1987) J. Mol. Biol. , vol.198 , pp. 295-310
    • McGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.E.3
  • 12
    • 0028352135 scopus 로고
    • Motionally restricted tryptophan environment at the peptide-lipid interface of gramicidin channels
    • Mukherjee, S., and A. Chattopadhyay. 1994. Motionally restricted tryptophan environment at the peptide-lipid interface of gramicidin channels. Biochemistry. 33:5089-5097.
    • (1994) Biochemistry , vol.33 , pp. 5089-5097
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 13
    • 0003143015 scopus 로고
    • Preparation of liposomes
    • IRL Press, Oxford, U.K.
    • New, R. R. C. 1990. Preparation of liposomes. In Liposomes: A Practical Approach, IRL Press, Oxford, U.K., 1-33.
    • (1990) Liposomes: A Practical Approach , pp. 1-33
    • New, R.R.C.1
  • 14
    • 0020763601 scopus 로고
    • On the origin of nonexponential fluorescence decay in tryptophan and its derivatives
    • Petrich, J. W., M. C. Chang, D. B. Mcdonald, and G. R. Fleming. 1983. On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J. Am. Chem. Soc. 105:3824-3832.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    Mcdonald, D.B.3    Fleming, G.R.4
  • 15
    • 0024991372 scopus 로고
    • Fluorescence lifetime distributions in human superoxide dismutase. Effect of temperature and denaturation
    • Rosato, N., E. Gratton, G. Mei, and A. Finazzi-Agro. 1990. Fluorescence lifetime distributions in human superoxide dismutase. Effect of temperature and denaturation. Biophys. J. 58:817-822.
    • (1990) Biophys. J. , vol.58 , pp. 817-822
    • Rosato, N.1    Gratton, E.2    Mei, G.3    Finazzi-Agro, A.4
  • 17
    • 0027208112 scopus 로고
    • Rotamers: To be or not to be? An analysis of amino-acid side-chain conformations in globular proteins
    • Shrauber, H., F. Eisenhaber, and P. Argos. 1993. Rotamers: to be or not to be? An analysis of amino-acid side-chain conformations in globular proteins. J. Mol. Biol. 230:592-612.
    • (1993) J. Mol. Biol. , vol.230 , pp. 592-612
    • Shrauber, H.1    Eisenhaber, F.2    Argos, P.3
  • 18
    • 0027985340 scopus 로고
    • Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state
    • Swaminathan, R., G. Krishnamoortny, and N. Periasamy. 1994. Similarity of fluorescence lifetime distributions for single tryptophan proteins in the random coil state. Biophys. J. 67:2013-2023.
    • (1994) Biophys. J. , vol.67 , pp. 2013-2023
    • Swaminathan, R.1    Krishnamoortny, G.2    Periasamy, N.3
  • 19
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo, A. G., and D. M. Rayner. 1980. Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102:554-563.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 20
    • 0028198619 scopus 로고
    • Equilibrium unfolding of yeast phosphoglycerate kinase, and its mutants lacking one or both native tryptophans: A circular dichroism, and steady-state, and time-resolved fluorescence study
    • Szpikowska, B. K., J. M. Beecham, M. A. Sherman, and M. T. Mas. 1994. Equilibrium unfolding of yeast phosphoglycerate kinase, and its mutants lacking one or both native tryptophans: a circular dichroism, and steady-state, and time-resolved fluorescence study. Biochemistry. 33: 2217-2225.
    • (1994) Biochemistry , vol.33 , pp. 2217-2225
    • Szpikowska, B.K.1    Beecham, J.M.2    Sherman, M.A.3    Mas, M.T.4
  • 21
    • 0028175552 scopus 로고
    • Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation
    • Willis, K. J., W. Neugebawer, M. Sikorska, and A. G. Szabo. 1994. Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation. Biophys. J. 66:1623-1630.
    • (1994) Biophys. J. , vol.66 , pp. 1623-1630
    • Willis, K.J.1    Neugebawer, W.2    Sikorska, M.3    Szabo, A.G.4
  • 22
    • 0026701231 scopus 로고
    • Conformation of parathyroid hormone: Time-resolved fluorescence studies
    • Willis, K. J., and A. G. Szabo. 1992. Conformation of parathyroid hormone: time-resolved fluorescence studies. Biochemistry. 31: 8924-8931.
    • (1992) Biochemistry , vol.31 , pp. 8924-8931
    • Willis, K.J.1    Szabo, A.G.2
  • 23
    • 0027170648 scopus 로고
    • Membrane partitioning: Distinguishing bilayer effects from the hydrophobic effect
    • Wimley, W. C., and S. H. White. 1993. Membrane partitioning: distinguishing bilayer effects from the hydrophobic effect. Biochemistry. 32:6307-6312.
    • (1993) Biochemistry , vol.32 , pp. 6307-6312
    • Wimley, W.C.1    White, S.H.2
  • 24
    • 0028886931 scopus 로고
    • Microenvironmental effects on the solvent quenching rate in constrained tryptophan derivatives
    • Yu, H. T., M. A. Vela, F. R. Fronczek, M. L. McLauglin, and M. D. Barkley. 1995. Microenvironmental effects on the solvent quenching rate in constrained tryptophan derivatives. J. Am. Chem. Soc. 117: 348-357.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 348-357
    • Yu, H.T.1    Vela, M.A.2    Fronczek, F.R.3    McLauglin, M.L.4    Barkley, M.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.