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Structure and dynamics of membrane proteins as studied by infrared spectroscopy.
  • J. Arrondo, F. Goñi
  • Chemistry, Medicine
  • Progress in biophysics and molecular biology
  • 1 November 1999
The present review describes the applications of IR spectroscopy to the study of membrane proteins, with an emphasis on recent work and on spectra recorded in the transmission mode, rather than using reflectance techniques. Expand
Ceramides in phospholipid membranes: effects on bilayer stability and transition to nonlamellar phases.
31P-NMR indicates the coexistence, within a certain range of temperatures, of lamellar and hexagonal phases, or hexagonal phase precursors, relevant in the interpretation of certain forms of interfacial enzyme activation and in the regulation and dynamics of the bilayer structure of cell membranes. Expand
Triton X-100-Resistant Bilayers: Effect of Lipid Composition and Relevance to the Raft Phenomenon
The molecular basis for the existence of the so-called “detergent-resistant membranes” has been explored. With that aim, vesicles composed of phosphatidylcholine, sphingolipid, and cholesterol wereExpand
Characterization of the interaction of natural proline-rich peptides with five different SH3 domains.
Analysis of the SH3 domain complexes with these peptides suggests that proline-rich peptides do not necessarily adopt an overall PPII structure over their entire length upon binding to the different SH3 domains. Expand
Differential interaction of equinatoxin II with model membranes in response to lipid composition.
Although the presence of sphingomyelin within the membrane creates conditions for irreversible insertion and pore formation, this lipid is not essential for the initial partitioning event, and its role as a specific receptor for the toxin is not so clear-cut. Expand
Interaction of Biotin with Streptavidin
The data provide a rationale for previous suggestions that biotin binding induces an increase in protein tightness (structural cooperativity) leading, in turn, to a higher thermostability. Expand
Infrared studies of protein-induced perturbation of lipids in lipoproteins and membranes.
A number of general conclusions are presented on the perturbations caused by proteins on either the hydrocarbon chains, the polar headgroups or the interface region on the impact of infrared spectroscopy on lipid-protein interactions in native cell membranes. Expand
DNA-induced Secondary Structure of the Carboxyl-terminal Domain of Histone H1*
Examination of the changes in the amide I components in the 20–80 °C temperature interval showed that the secondary structure of the DNA-bound C-H1t is for the most part extremely stable. Expand
Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
The results suggest that the effects of phosphorylation are mediated by specific structural changes and are not simply a consequence of the net charge. Expand