Publication

Structural fluctuations of polypeptides in lipid membranes

Horst Arthur Vogel
1988
Journal Articles

Abstract

Time-resolved fluorescence anisotropy (FA) measurements are reported for 5 helical, bilayer-spanning heneicosapeptides, each contg. 1 tryptophan (Trp) at sequence positions 1, 6, 11, 16, and 21, resp. The FA decay reflected 2 mol. processes in all cases, local internal fluctuations of the Trp side-chain with a relaxation time of 200-500 ps and motions of the whole polypeptide mol. with a relaxation time of 9-10 ns. Concomitant mol. dynamics calcns. indicated a correlation between the fast FA decay and conformational fluctuations within the helix. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/68b62eef-04ee-421c-b46d-122bd5cacbe7

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Horst Arthur Vogel
1988
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/68b62eef-04ee-421c-b46d-122bd5cacbe7

About this result

Related concepts (27)

Lipid bilayer

The lipid bilayer (or phospholipid bilayer) is a thin polar membrane made of two layers of lipid molecules. These membranes are flat sheets that form a continuous barrier around all cells. The cell membranes of almost all organisms and many viruses are made of a lipid bilayer, as are the nuclear membrane surrounding the cell nucleus, and membranes of the membrane-bound organelles in the cell. The lipid bilayer is the barrier that keeps ions, proteins and other molecules where they are needed and prevents them from diffusing into areas where they should not be.

Lipid raft

The plasma membranes of cells contain combinations of glycosphingolipids, cholesterol and protein receptors organised in glycolipoprotein lipid microdomains termed lipid rafts. Their existence in cellular membranes remains somewhat controversial. It has been proposed that they are specialized membrane microdomains which compartmentalize cellular processes by serving as organising centers for the assembly of signaling molecules, allowing a closer interaction of protein receptors and their effectors to promote kinetically favorable interactions necessary for the signal transduction.

Protein structure

Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers - specifically polypeptides - formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond.

Related publications (24)

Structural fluctuations of polypeptides in lipid membranes

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