Cooperativity and specificity of association of a designed transmembrane peptide. Academic Article

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.

authors

• Wand, Joshua

published proceedings

• Biophys J

author list (cited authors)

• Gratkowski, H., Dai, Q., Wand, A. J., DeGrado, W. F., & Lear, J. D.

citation count

• 24

complete list of authors

• Gratkowski, Holly||Dai, Qing-Hong||Wand, A Joshua||DeGrado, William F||Lear, James D

publication date

• September 2002

publisher

• Elsevier  Publisher

keywords

• Amino Acid Sequence
• Betaine
• Cell Membrane
• Detergents
• Dimerization
• Hydrogen-Ion Concentration
• Magnetic Resonance Spectroscopy
• Micelles
• Molecular Sequence Data
• Peptide Biosynthesis
• Peptides
• Phosphorylcholine
• Thermodynamics
• Ultracentrifugation

Digital Object Identifier (DOI)

• 10.1016/S0006-3495(02)73930-1

start page

• 1613

end page

• 1619

volume

• 83

issue

• 3

URL

• http://dx.doi.org/10.1016/s0006-3495(02)73930-1