429 results about "Polypeptide chain" patented technology

The invention provides for a polyvalent protein complex (PPC) comprising two polypeptide chains generally arranged laterally to one another. Each polypeptide chain typically comprises 3 or 4 “v-regions”, which comprise amino acid sequences capable of forming an antigen binding site when matched with a corresponding v-region on the opposite polypeptide chain. Up to about 6 “v-regions” can be used on each polypeptide chain. The v-regions of each polypeptide chain are connected linearly to one another and may be connected by interspersed linking regions. When arranged in the form of the PPC, the v-regions on each polypeptide chain form individual antigen binding sites.

The invention provides antibody-like binding proteins comprising four polypeptide chains that form four antigen binding sites, wherein each pair of polypeptides forming an antibody-like binding protein possesses dual variable domains having a cross-over orientation. The invention also provides methods for making such antigen-like binding proteins.

Disclosed herein is a multilayer film comprising two or more layers of polyelectrolytes, wherein adjacent layers comprise oppositely charged polyelectrolytes. A first layer polyelectrolye comprises a composite polypeptide comprising one or more surface adsorption regions covalently linked to one or more functional regions forming a single polypeptide chain. The surface adsorption regions comprise one or more amino acid sequence motifs consisting of 5 to 15 amino acid residues. The one or more functional regions comprise 3 to about 250 amino acid residues.

The invention relates to a polyvinyl alcohol-polypeptide-polyethylene glycol graft copolymer and a preparation method thereof. The molecular weight of polyvinyl alcohol is 20,000-80,000; the molecular weight of a polypeptide chain segment is 4,000-8,000; and the molecular weight of a polyethylene glycol chain segment is 350-750. The preparation method comprises the following steps of: (1) synthesizing a polypeptide homopolymer which contains an end-NCO radical: adding the polypeptide homopolymer, diisocyanate, dibutyltin dilaurate serving as a catalyst and dimethyl sulfoxide serving as a solvent into a reactor for reacting to obtain a target product; (2) synthesizing a polyvinyl alcohol-polypeptide graft copolymer: adding the polypeptide homopolymer which contains the end-NCO radical, the solvent and the catalyst into the reactor, adding polyvinyl alcohol and reacting to obtain a target product; and (3) synthesizing a polyvinyl alcohol-polypeptide-polyethylene glycol graft copolymer: adding the polyvinyl alcohol-polypeptide graft copolymer, the solvent and the catalyst into a drying reactor, adding polyethylene glycol monomethyl ether and reacting to obtain a target product.

A method and a device are disclosed for monitoring the synthesis of proteins by the ribosome in real time, in vivo as well as in in-vitro. The ribosome is engineered to carry a donor fluorophore, and tRNA and/or amino acids and/or some other part of the ribosome are either engineered to carry acceptor fluorophores or else their natural fluorescent properties are utilized as acceptors. As the ribosomes mechanism processed the mRNA and tRNA molecules and synthesizes a polypeptide chain, a light source illuminates the ribosome, exciting the donor fluorophores and thereby the acceptor fluorophores whenever these are in sufficient proximity to a donor. The resulting signals are detected and used as a key for real-time database searching and identification of the protein being synthesized. The resulting data can be tabulated and interpreted in different ways. FIG. (1) describes the properties of a FRET pair and the dependence of FRET on pair distance.

Described herein are, proteins comprising amino acid substitutions in at least one of a first and a second polypeptide chain. Furthermore, is described the uses and methods related to said proteins.

The invention relates to a polyurethane-polypeptide graft copolymer and a preparation method thereof. The graft copolymer is a comb-shaped polymer, wherein the molecular weight of polyurethane is 10,000 to 100,000; and the molecular weight of the polypeptide chain segment is 500 to 5,000. The preparation method comprises the following steps of: 1) synthesis of polyurethane provided with lateral carboxyl on the molecular chain: adding diisocyanate, polypropylene glycol, polyethylene glycol, dibutyltin dilaurate catalyst and dimethyl formamide solvent into a dry reaction bottle, performing stirring reaction under inert atmosphere, adding dimethylolpropionic acid dissolved in dimethyl formamide to react, adding butanediol to react, finally adding butanol to react, and obtaining a target product; and 2) synthesis of the polyurethane-polypeptide graft copolymer: putting the polyurethane provided with lateral carboxyl on the molecular chain, a solvent and a condensation agent into a dry reactor, adding polypeptide homopolymer into the reactor, and performing stirring reaction under the inert atmosphere to obtain a target product with pH response.

The present invention proposes formative agent of protein complex, in which a polyphenol is useful component, and the agent is useful as gene complex, cell adhesion inhibitor or immune tolerogen. The polyphenol of forming the agent is selected from catechin group consisting of epigallocatechin-gallate, tannic acids, or proanto-dianisidine, a protein of the protein complex is selected from proteins consisting of animal proteins composed of polypeptide chain of peptide-combined amino acids, vegetative proteins, nucleus proteins, glycogen proteins, lipo-proteins and metal proteins, the gene complex comprises by compositing genes by polyphenol catechins in order to introduce genes to cells of animals or human bodies, a cell composed of the cell adhesion inhibitor is selected from cells consisting of an animal cell including a stem cell, skin cell, mucosa cell, hepatocyte, islet cell, neural cell, cartilage cell, endothelial cell, epidermal cell, osteocyte or muscle cell isolated from human or animal organism, or sperm, ovum or fertilized egg of domestic animals or fishes and a tissue or an organ for transplantation of the immune tolerogen is selected from the tissue or the organ consisting of skin, blood vessel, cornea, kidney, heart, liver, umbilical cord, bowels, nerve, lung, placenta or pancreas.

The invention relates to a construction of an electrochemical luminescence sensor for detecting acetyltransferase activity. The construction comprises the following steps: firstly, polishing, cleaning and activating a gold electrode, assembling captured DNA on the surface of the electrode through action of gold-sulfur bond, and enclosing non-specific binding sites on the surface of the electrode with MCH; then adsorbing a polypeptide chains through electrostatic action, performing acetylation treatment on the polypeptide chains under the action of HATp300, so as to separate from the surface of the electrode; secondly, performing hybrid chain reaction on the electrode in a hybrid chain solution containing two hairpin DNA, and reducing a silver cluster; and finally, detecting electrochemical luminescence signal of the assembled electrochemical luminescence sensor in the solution. The ECL biosensor has remarkable advantages on the quantitative analysis of HAT p300 and the activity analysis on HAT p300 in complicated cell lysis buffering solution.

The invention relates to compounds which contain an antigen binding region which is bound to at least one enzyme which is able to metabolize a compound (prodrug) which has little or no cytotoxicity to a cytotoxic compound (drug), where the antigen binding region is composed of a single polypeptide chain. It is advantageous for covalently bonded carbohydrates to be present on the polypeptide chain.

A combination of polypeptide chains used as a plurality of target substance-binding domains are selected by: (1) reacting a target substance with a first polypeptide chain with a known target substance-binding domain to obtain a first complex; (2) reacting the first complex with a second polypeptide chain library composed of polypeptide chains each having a site to be associated with the first polypeptide chain to obtain second complexes in which the second polypeptide chain is bonded with the target substance in the first complex; (3) washing the second complexes to obtain a third complex in which the first polypeptide chain and the second polypeptide chain are associated with each other and bonded with the target substance; and (4) obtaining a nucleic acid sequence of the second polypeptide chain from the third complex.

The present invention features inter alia nucleic acid molecules which encode polypeptides comprising a single chain Fc region and the polypeptides they encode. The Fc moieties of these constructs are linked by a cleavable scFc linker which is adjacent to at least one enzymatic cleavage site, e.g., an intracellular processing site. The resulting processed molecules comprise two polypeptide chains and substantially lack the extraneous amino acid sequence found in single chain Fc linker molecule. Methods of making and using these dimeric molecules are also described.

The invention relates to the field of polypeptide, and especially relates to a preparation method of polypeptide. The preparation method comprises the following steps: coupling Arg with resin to prepare Arg-resin; individually coupling Arg-resin with Ala, Arg, Arg, Arg, Ala, and Cys (X) in sequence, carrying out amino acetylation on the nitrogen terminal to obtain a first peptide resin; removing the side chain protective group X in Cys (X) of the first peptide resin, then coupling the first peptide resin with Y-Cys to obtain a second peptide resin, and cracking the second peptide resin to obtain the polypeptide. The preparation method is carried out in pure solid state, the operation is simple and convenient, and the pseudo-dilution effect avoid the disulfide bond mispairing reactions between polypeptide chains in liquid phase reactions ( no reactions happens between peptide chains). The yield and purity of polypeptide Velcalcetide are both improved, and the side reactions are reduced.