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Cooperativity and specificity of association of a designed transmembrane peptide.
- Source :
-
Biophysical journal [Biophys J] 2002 Sep; Vol. 83 (3), pp. 1613-9. - Publication Year :
- 2002
-
Abstract
- Thermodynamics studies aimed at quantitatively characterizing free energy effects of amino acid substitutions are not restricted to two state systems, but do require knowing the number of states involved in the equilibrium under consideration. Using analytical ultracentrifugation and NMR methods, we show here that a membrane-soluble peptide, MS1, designed by modifying the sequence of the water-soluble coiled-coil GCN4-P1, exhibits a reversible monomer-dimer-trimer association in detergent micelles with a greater degree of cooperativity in C14-betaine than in dodecyl phosphocholine detergents.
- Subjects :
- Amino Acid Sequence
Betaine pharmacology
Detergents pharmacology
Dimerization
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Micelles
Molecular Sequence Data
Peptide Biosynthesis
Phosphorylcholine pharmacology
Thermodynamics
Ultracentrifugation
Cell Membrane metabolism
Peptides chemistry
Phosphorylcholine analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3495
- Volume :
- 83
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biophysical journal
- Publication Type :
- Academic Journal
- Accession number :
- 12202385
- Full Text :
- https://doi.org/10.1016/S0006-3495(02)73930-1