-
1
-
-
0020712137
-
Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction
-
S. C. Quay and C. C. Condie (1983). Conformational studies of aqueous melittin: Thermodynamic parameters of the monomer-tetramer self-association reaction. Biochemistry 22, 695-700.
-
(1983)
Biochemistry
, vol.22
, pp. 695-700
-
-
Quay, S.C.1
Condie, C.C.2
-
2
-
-
0020479083
-
The structure of melittin. I. Structure determination and partial refinement
-
T. C. Terwillinger and D. Eisenberg (1982). The structure of melittin. I. Structure determination and partial refinement. J. Biol. Chem. 257, 6010-6015.
-
(1982)
J. Biol. Chem.
, vol.257
, pp. 6010-6015
-
-
Terwillinger, T.C.1
Eisenberg, D.2
-
3
-
-
0020479123
-
The structure of melittin. II. Interpretation of the structure
-
T. C. Terwillinger and D. Eisenberg (1982). The structure of melittin. II. Interpretation of the structure. J. Biol. Chem. 257, 6016-6021.
-
(1982)
J. Biol. Chem.
, vol.257
, pp. 6016-6021
-
-
Terwillinger, T.C.1
Eisenberg, D.2
-
4
-
-
0027056421
-
Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding
-
W. Wilcox and D. Eisenberg (1992). Thermodynamics of melittin tetramerization determined by circular dichroism and implications for protein folding. Protein Sci. 1, 641-653.
-
(1992)
Protein Sci.
, vol.1
, pp. 641-653
-
-
Wilcox, W.1
Eisenberg, D.2
-
5
-
-
0032532218
-
The structure of the melittin tetramer at different temperatures
-
M. Iwadate, T. Asakura, and M. P. Williamson (1998). The structure of the melittin tetramer at different temperatures. Eur. J. Biochem. 257, 479-487.
-
(1998)
Eur. J. Biochem.
, vol.257
, pp. 479-487
-
-
Iwadate, M.1
Asakura, T.2
Williamson, M.P.3
-
6
-
-
0026910992
-
Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength and temperature - Models for protein folding and halophilic proteins
-
K. Ramalingam, S. Aimoto, and J. Bello (1992). Conformational studies of anionic melittin analogues: Effect of peptide concentration, pH, ionic strength and temperature - models for protein folding and halophilic proteins. Biopolymers 32, 981-992.
-
(1992)
Biopolymers
, vol.32
, pp. 981-992
-
-
Ramalingam, K.1
Aimoto, S.2
Bello, J.3
-
7
-
-
0023334542
-
Structural dynamics in the environment of the tryptophan residue in melittin
-
A. P. Demchenko, A. S. Ladokhin, E. G. Kostrzhewskaya, and T. L. Dibrova (1987). Structural dynamics in the environment of the tryptophan residue in melittin. Mol. Biol. 21, 663-671.
-
(1987)
Mol. Biol.
, vol.21
, pp. 663-671
-
-
Demchenko, A.P.1
Ladokhin, A.S.2
Kostrzhewskaya, E.G.3
Dibrova, T.L.4
-
8
-
-
0018487558
-
The self-association of melittin and its binding to lipids
-
J. F. Faucon, J. Dufourcq, and C. Lussan (1979). The self-association of melittin and its binding to lipids. FEBS Lett. 102, 187-190.
-
(1979)
FEBS Lett.
, vol.102
, pp. 187-190
-
-
Faucon, J.F.1
Dufourcq, J.2
Lussan, C.3
-
9
-
-
0018483723
-
Conformational change and self-association of monomeric melittin
-
J. C. Talbot, J. Dufourcq, J de Bony, J. F. Faucon, and C. Lussan (1979). Conformational change and self-association of monomeric melittin. FEBS Lett. 102, 191-193.
-
(1979)
FEBS Lett.
, vol.102
, pp. 191-193
-
-
Talbot, J.C.1
Dufourcq, J.2
De Bony, J.3
Faucon, J.F.4
Lussan, C.5
-
10
-
-
0036363969
-
The red-edge effect: 30 years of exploration
-
A. P. Demchenko (2002). The red-edge effect: 30 years of exploration. Lumin. 17, 19-42.
-
(2002)
Lumin.
, vol.17
, pp. 19-42
-
-
Demchenko, A.P.1
-
11
-
-
0000864144
-
Cold-denaturated ensemble of apomyoglobin: Implications for the early steps of folding
-
J. Sabelko, J. Erwin, and M. Gruebelle (1998). Cold-denaturated ensemble of apomyoglobin: Implications for the early steps of folding. J. Phys. Chem. B102, 1806-1816.
-
(1998)
J. Phys. Chem. B
, vol.102
, pp. 1806-1816
-
-
Sabelko, J.1
Erwin, J.2
Gruebelle, M.3
-
12
-
-
0030610813
-
La and Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins
-
P. R. Callis (1994). La and Lb transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 228, 113-150.
-
(1994)
Methods Enzymol.
, vol.228
, pp. 113-150
-
-
Callis, P.R.1
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