Conformational studies of aqueous melittin. Characteristics of a fluorescent probe binding site.
Open Access
- 1 July 1983
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 258 (13) , 8231-8234
- https://doi.org/10.1016/s0021-9258(20)82053-5
Abstract
No abstract availableThis publication has 25 references indexed in Scilit:
- Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reactionBiochemistry, 1983
- Essential role of arginine residues in the folding of deoxyribonucleic acid into nucleosome coresBiochemistry, 1982
- Anilinonaphthalene sulfonate as a probe of membrane composition and functionBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1982
- Dependence of melittin structure on its interaction with multivalent anions and with model membrane systems*International Journal of Peptide and Protein Research, 1982
- Conformation of poly(L‐homoarginine)Biopolymers, 1980
- Conformation of poly(L-arginine). II. Complexes with polyanionsBiopolymers, 1978
- Conformation of poly(L‐arginine). I. Effects of anionsBiopolymers, 1978
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Interaction of the fluorescent probe 2-p-toluidinylnaphthalene-6-sulfonate with peptides. Structural requirements for binding and fluorescence enhancementBiochemistry, 1972
- Bee and Wasp VenomsScience, 1972