NDLI: Total synthesis and functional properties of the membrane-intrinsic protein phospholamban.

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Conformational change of chaperone Hsc70 upon binding to a decapeptide: a circular dichroism study.

Extending the diffraction limit of protein crystals: the example of glutamine synthetase from Salmonella typhimurium in the presence of its cofactor ATP.

Total synthesis and functional properties of the membrane-intrinsic protein phospholamban.

Frequency analysis of infrared absorption and vibrational circular dichroism of proteins in D2O solution.

Mapping the surface properties of macromolecules.

Structural analysis based on state-space modeling.

Reconstruction of protein conformations from estimated positions of the C alpha coordinates.

Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: effects of the solvent dielectric.

Ribonuclease S-peptide as a carrier in fusion proteins.

Controlling the regiospecificity and coupling of cytochrome P450cam: T185F mutant increases coupling and abolishes 3-hydroxynorcamphor product.

Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.

Packing and hydrophobicity effects on protein folding and stability: effects of beta-branched amino acids, valine and isoleucine, on the formation and stability of two-stranded alpha-helical coiled coils/leucine zippers.

Unnatural amino acid packing mutants of Escherichia coli thioredoxin produced by combined mutagenesis/chemical modification techniques.

Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution.

Bacterial expression and photoaffinity labeling of a pheromone binding protein.

Structure of recombinant ricin A chain at 2.3 A.

Structure of Paramecium tetraurelia calmodulin at 1.8 A resolution.

Crystal structure of human annexin I at 2.5 A resolution.

My life with tryptophan--never a dull moment.

Poly-alpha-amino acids as the simplest protein models: recollections of a retired state president.

Year: 1993 Volume: 2 Issue: 2

Year: 1993 Volume: 2 Issue: 1

Year: 1992 Volume: 1

Total synthesis and functional properties of the membrane-intrinsic protein phospholamban.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wrzosek, A. Chiesi, M. Carafoli, E. Vorherr, T.
Description	Author Affiliation: Vorherr T ( Institute of Biochemistry, Swiss Federal Institute of Technology (ETH), Zürich.)
Abstract	The membrane-intrinsic protein phospholamban (PLN), the regulatory protein of the sarcoplasmic reticulum (SR) Ca(2+)-ATPase, was chemically synthesized. The synthesis was accomplished by double couplings and efficient capping procedures, thus eliminating hydrophobic failure sequences. The crude peptide was purified by high-performance liquid chromatographic ion exchange and gel permeation chromatography in chloroform-methanol mixtures. Ion spray mass spectroscopy showed that the product had the correct molecular mass. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis runs produced the typical monomer-pentamer structural pattern. A predominantly helical CD spectrum was obtained in 0.075% C12E8 (67.9% helix, 1.8% beta, 12.2% turn, 18.1% random coil). Synthetic PLN was phosphorylated in detergent solutions by protein kinase A with a stoichiometry close to 1:1 (Pi to PLN monomer). Reconstitution of the isolated skeletal muscle SR Ca2+ ATPase in phosphatidylcholine membranes in the presence of PLN using the freezing and thawing technique yielded a preparation with lower Ca(2+)-dependent ATPase activity. The inhibition was mainly due to a decrease in the affinity (Km(Ca)) of the ATPase for Ca2+ and was partially reversed by PLN phosphorylation with protein kinase A. By contrast, addition of PLN to diluted intact SR vesicles uncoupled the Ca(2+)-transport reaction, suggesting an ionophoric effect of PLN. Because this effect was observed at very high PLN-to-SR vesicle ratios and was not influenced by PLN phosphorylation, its biological function is doubtful.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	3
Volume Number	2
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1993-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium-binding Proteins Chemical Synthesis Amino Acid Sequence Animals Chemistry Metabolism Calcium-transporting Atpases Physiology Circular Dichroism In Vitro Techniques Molecular Sequence Data Protein Structure, Secondary Rabbits Sarcoplasmic Reticulum Ultracentrifugation Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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