Publication

Small-angle neutron scattering from diblock copolymer poly(styrene-d8)-b-poly(γ-benzyl L-glutamate) solutions: Rod-coil to coil-coil transition

2003
Journal Articles

Abstract

The elastic properties of rod-coil diblock copolymer poly(styrene-d8)-b-poly(γ-benzyl L-glutamate) (PSd-b-PBLG) rod-coil diblock copolymer solutions were investigated using small-angle neutron scattering (SANS). PBLG is known to undergo a transition from a rodlike α-helical secondary structure to a random coil conformation under specific solvent conditions: the PBLG is (i) rodlike in dioxane and (ii) random coil in dioxane/trifluoroacetic acid (80/20). For the PSd-b-PBLG diblock copolymer, this conformational transition results in a topological change from a rod-coil to a coil-coil type structure. SANS results indeed show the presence of the expected scattering peaks-copolymer signature-for both conformational topologies. The position and the height of these scattering peaks are found in good agreement with a recent theoretical model that describes the conformational change in rod-coil diblock copolymer solutions. Circular dichroism experiments confirmed the change in secondary structure in the peptide block that accompanies the topological transition observed by SANS.

Official source

https://infoscience.epfl.ch/entities/publication/7c99546a-9977-41d9-b58c-53feff95a6e4

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2003
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/7c99546a-9977-41d9-b58c-53feff95a6e4

About this result

Related concepts (32)

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.

Protein secondary structure

Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone.

Random coil

In polymer chemistry, a random coil is a conformation of polymers where the monomer subunits are oriented randomly while still being bonded to adjacent units. It is not one specific shape, but a statistical distribution of shapes for all the chains in a population of macromolecules. The conformation's name is derived from the idea that, in the absence of specific, stabilizing interactions, a polymer backbone will "sample" all possible conformations randomly.

Related publications (5)

Small-angle neutron scattering from diblock copolymer poly(styrene-d8)-b-poly(γ-benzyl L-glutamate) solutions: Rod-coil to coil-coil transition

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