The present invention provides novel blockers of the potassium channel Kv1.3, polynucleotides encoding them, and methods of making and using them.

Synthetic apolipoproteins based on native/naturally occurring homolog proteins can be prepared using solid-phase peptide synthesis approaches combined with native chemical ligation methods to create analogs of full length apolipoproteins. The chemical synthesis is expected to allow introduction of non-natural amino acids, e.g., α,α′-dialkyl amino acids, with a periodicity that encourages both helix formation and amphipathicity. Such apolipoprotein analogs are expected to encourage, in some embodiments, facile and more complete NLP formation, enabling consideration of full spectrum of nanoparticle-based biotechnology applications ranging from therapeutic sequestration and delivery to energy/biofuel production to biopolymer production.

The present invention relates to engineered IgG Fc constructs and uses thereof.

Disclosed herein are polypeptides having the amino acid sequence that is at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the full length of the amino acid sequence selected from the group consisting of SEQ ID NO: 1-33 and 36, wherein the polypeptides include at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% of the identified interface residues, and wherein the polypeptides are capable of end-to-end homo-polymerization, homo-polymers of the polypeptides, and related capping and anchor proteins to facilitate homo-polymer formation.

Disclosed herein are polypeptides having the amino acid sequence that is at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% identical to the full length of the amino acid sequence selected from the group consisting of SEQ ID NO: 1-33 and 36, wherein the polypeptides include at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, or 100% of the identified interface residues, and wherein the polypeptides are capable of end-to-end homo-polymerization, homo-polymers of the polypeptides, and related capping and anchor proteins to facilitate homo-polymer formation.

A multifunctional chemical agents comprising functional agents Fn1, Fn2 and linkers, for the linchpin directed (LDM), protein directed (PDPM) modifications of proteins, and Fn1 accelerated kinetic labeling by Fn2.

A method of purifying an antifreeze protein (AFP) and methods of producing AFPs are disclosed. The method of purifying an AFP includes heating a crude AFP in an aqueous medium to a temperature and for a length of time sufficient to precipitate at least some thermally unstable proteins in the crude AFP and form a precipitate and a supernatant; and removing the precipitate from the supernatant. One method of producing an AFP includes collecting a crude source of the AFP; and purifying the AFP by the purification method. Another method of producing an AFP includes growing or culturing a host configured to express a recombinant AFP in a growth medium, and collecting a crude AFP from the host and/or the growth medium. The growth medium comprises water, a protein hydrolysate or other source of amino acids, a yeast extract, a biologically metabolizable C.sub.3-C.sub.6 polyol, and one or more phosphate salts.

The present invention relates to a novel protein comprising novel genes that is extracted from Burkholderia gladioli strain NGJ1. A nucleotide sequence encoding the novel protein is represented by sequence SEQ ID No. 1 and amino acid sequence of the novel protein is represented by the sequence SEQ ID No. 2 is further provided. A nucleotide sequence and the amino acid sequence are obtained from genetically engineered Bg_9562 gene. The novel protein as well as encoding gene is adapted for broad spectrum anti-fungal and mycophagous activities.

The present invention relates to a protein composition formed of dry matter of a dispersion in which a protein is dispersed in a stabilizer solution, in which the stabilizer includes at least one type selected from the group consisting of a catechol-based stabilizer, 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid, 2,6-di-tert-butyl-p-cresol, 2-tert-butyl-4-methoxyphenol, and 6,6′-di-tert-butyl-4,4′-butylidenedi-m-cresol.

The present invention relates to a protein composition formed of dry matter of a dispersion in which a protein is dispersed in a stabilizer solution, in which the stabilizer includes at least one type selected from the group consisting of a catechol-based stabilizer, 6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid, 2,6-di-tert-butyl-p-cresol, 2-tert-butyl-4-methoxyphenol, and 6,6′-di-tert-butyl-4,4′-butylidenedi-m-cresol.