Secondary structure and dynamics study of the intrinsically disordered silica-mineralizing peptide P S during silicic acid condensation and silica decondensation.

The silica forming repeat R5 of sil1 from Cylindrotheca fusiformis was the blueprint for the design of P S , a 50-residue peptide which can be produced in large amounts by recombinant bacterial expression. It contains 5 protein kinase A target sites and is highly cationic due to 10 lysine and 10 arginine residues. In the presence of supersaturated orthosilicic acid P S enhances silica-formation whereas it retards the dissolution of amorphous silica (SiO ) at globally undersaturated concentrations.

High yield recombinant production of a self-assembling polycationic peptide for silica biomineralization.

We report the recombinant bacterial expression and purification at high yields of a polycationic oligopeptide, P5S3. The sequence of P5S3 was inspired by a diatom silaffin, a silica precipitating peptide. Like its native model, P5S3 exhibits silica biomineralizing activity, but furthermore has unusual self-assembling properties.

Silica entrapment for significantly stabilized, energy-conducting light-harvesting complex (LHCII).

The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants consists of a membrane protein and numerous noncovalently bound pigments that make up about one-third of the molecular mass of the pigment-protein complex. Due to this high pigment density, LHCII is potentially interesting as a light-harvesting component in synthetic constructs. However, for such applications its stability needs to be significantly improved.

Designed peptides for biomineral polymorph recognition: a case study for calcium carbonate.

With their unique ability for substrate recognition and their sequence-specific self-assembly properties, peptides play an important role in controlling the mineralization of inorganic materials in natural systems and in controlling the assembly of soft materials into complex structures required for biological functions. Here we report the use of an engineered heptapeptide that can differentiate between the crystalline anhydrous polymorphs of calcium carbonate. This peptide contains the positively charged amino acid arginine as well as proline rather than the prototypical negatively charged aspartate or glutamate units.

Assembly of the major light-harvesting chlorophyll-a/b complex: Thermodynamics and kinetics of neoxanthin binding.

The major light-harvesting chlorophyll-a/b complex in most higher plants contains three carotenoids, lutein, neoxanthin, and violaxanthin. How these pigments are assembled into the complex during its biogenesis is largely unknown. Here we show that neoxanthin but not lutein can dissociate from the fully assembled complex.

Determination of relative chlorophyll binding affinities in the major light-harvesting chlorophyll a/b complex.

The major light-harvesting complex (LHCIIb) of photosystem II can be reconstituted in vitro from its recombinant apoprotein in the presence of a mixture of carotenoids and chlorophylls a and b. By varying the chlorophyll a/b ratio in the reconstitution mixture, the relative amounts of chlorophyll a and chlorophyll b bound to LHCIIb can be changed. We have analyzed the chlorophyll stoichiometry in recombinant wild type and mutant LHCIIb reconstituted at different chlorophyll a/b ratios in order to assess relative affinities of the chlorophyll-binding sites.

The binding of Xanthophylls to the bulk light-harvesting complex of photosystem II of higher plants. A specific requirement for carotenoids with a 3-hydroxy-beta-end group.

The pigment composition of the light-harvesting complexes (LHCs) of higher plants is highly conserved. The bulk complex (LHCIIb) binds three xanthophyll molecules in combination with chlorophyll (Chl) a and b. The structural requirements for binding xanthophylls to LHCIIb have been examined using an in vitro reconstitution procedure.