Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add more filters










Database
Language
Publication year range
1.
Biochim Biophys Acta ; 979(1): 139-41, 1989 Feb 13.
Article in English | MEDLINE | ID: mdl-2917163

ABSTRACT

Samples of pure lipid (dipalmitoylphosphatidylcholine) and lipid containing short alpha-helical peptides were oriented and examined by X-ray diffraction, together with unoriented samples of pure peptide. X-ray reflections from the bilayer and the alpha-helices showed that the peptides had oriented in the bilayer with their helical axes perpendicular to the surface.


Subject(s)
Membrane Proteins/ultrastructure , 1,2-Dipalmitoylphosphatidylcholine , Hydrogen Bonding , In Vitro Techniques , Lipid Bilayers , Oligopeptides/chemical synthesis , X-Ray Diffraction
2.
Biochemistry ; 24(20): 5396-406, 1985 Sep 24.
Article in English | MEDLINE | ID: mdl-3841008

ABSTRACT

Differential scanning calorimetry (DSC) experiments have been performed on the amphiphilic peptide/1,2-bis(perdeuteriopalmitoyl)-sn-glycero-3-phosphocholine system for which partial phase diagrams have been measured by deuterium nuclear magnetic resonance. The solute concentration dependence of the transition enthalpy in such systems is often interpreted in terms of an annulus of lipid withdrawn, by the solvent, from participation in the transition while the bulk lipid melts with its fully enthalpy. This idea is equivalent to postulating ideal mixing between the lipid and the peptide/lipid complex, and there is little justification for such an assumption. Adaptation of regular solution theory to this system demonstrates that the peptide concentration dependence of the transition enthalpies can be incorporated into a thermodynamic model which reproduces the observed phase behavior fairly well without postulating that a complexing annulus of lipid around the peptide be withdrawn from participating in the chain-melting transition. The model parameters determined by simultaneous fitting of the phase behavior and transition enthalpies are used to simulate the DSC scan shapes. The asymmetry of the calorimetric scans for chi 2 less than or equal to 0.02 is reproduced by the model, but a broad component observed for higher concentration is not. In light of the results presented here, previous analyses of the calorimetric behavior of two-component systems in terms of symmetric transitions which do not account for the possible extent of a region of two-phase equilibrium must be questioned.


Subject(s)
Liposomes , Oligopeptides , Pulmonary Surfactants , Calorimetry, Differential Scanning/methods , Chemical Phenomena , Chemistry , Deuterium , Mathematics , Models, Biological , Phosphatidylcholines , Protein Binding , Structure-Activity Relationship
SELECTION OF CITATIONS
SEARCH DETAIL
...