High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution
- 1 April 1980
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 622 (2) , 231-244
- https://doi.org/10.1016/0005-2795(80)90034-3
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- High-resolution 1H-NMR studies of monomeric melittin in aqueous solutionBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- Use of fully deuterated micelles for conformational studies of membrane proteins by high resolution 1H nuclear magnetic resonanceBiochimica et Biophysica Acta (BBA) - Biomembranes, 1979
- Physicochemical studies of the protein-lipid interactions in melittin-containing micellesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1979
- The self‐association of melittin and its binding to lipidsFEBS Letters, 1979
- Conformational change and self association of monomeric melittinFEBS Letters, 1979
- 1H‐nmr parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H‐Gly‐Gly‐X‐L‐Ala‐OHBiopolymers, 1979
- A 1H Nuclear‐Magnetic‐Resonance Study of the Conformation and the Molecular Dynamics of the Glycoprotein Cow‐Colostrum Trypsin InhibitorEuropean Journal of Biochemistry, 1978
- 1H NMR studies at 360 Mhz of the methyl groups in native and chemically modified basic pancreatic trypsin inhibitor (BPTI)European Biophysics Journal, 1977
- The Peptide Components of Bee VenomEuropean Journal of Biochemistry, 1976
- Bee and Wasp VenomsScience, 1972