42 results about "Primary amino acids" patented technology

Methods, compositions, kits, and apparatus are provided wherein the aminoacyl-tRNA synthetase system is used to analyze amino acids. The method allows very small devices for quantitative or semi-quantitative analysis of the amino acids in samples or in sequential or complete proteolytic digestions. The methods can be readily applied to the detection and / or quantitation of one or more primary amino acids by using cognate aminoacyl-tRNA synthetase and cognate tRNA. The basis of the method is that each of the 20 synthetases and / or a tRNA specific for a different amino acid is separated spatially or differentially labeled. The reactions catalyzed by all 20 synthetases may be monitored simultaneously, or nearly simultaneously, or in parallel. Each separately positioned synthetase or tRNA will signal its cognate amino acid. The synthetase reactions can be monitored using continuous spectroscopic assays. Alternatively, since elongation factor Tu:GTP (EF-Tu:GTP) specifically binds all AA−tRNAs, the aminoacylation reactions catalyzed by the synthetases can be monitored using ligand assays. Microarrays and microsensors for amino acid analysis are provided. Additionally, amino acid analysis devices are integrated with protease digestions to produce miniaturized enzymatic sequenators capable of generating either N- or C-terminal sequence and composition data for a protein or peptide. The possibility of parallel processing of many samples in an automated manner is discussed.

The invention provides a protein composition derived from silk fibroin, which composition possesses enhanced solubility and stability in aqueous solutions. The primary amino acid sequence of native fibroin is modified in the SDP such that cysteine disulfide bonds between the fibroin heavy and fibroin light protein chains are reduced or eliminated. Additionally, the composition can have a serine content that is reduced by greater than 40% compared to native fibroin protein, and the average molecular weight of the SDP is less than about 100 kDa.

This invention pertains to nucleic acid fragments encoding plant glucosyltransferases, heretofore undescribed, that exhibit catalytic activity with p-hydroxybenzoic acid (pHBA) as a substrate and only attach glucose to the aromatic carboxyl group of pHBA, to form the pHBA glucose ester. These enzymes have potential applications both in vitro and in vivo, and their primary amino acid sequences can be used to identify other proteins that have similar kinetic properties.

The present invention provides a method utilizing primary amino acid sequence of a protein, energy minimization, molecular dynamics and protein vibrational modes to predict three-dimensional structure of a protein. The present invention also determines possible intermediates in the protein folding pathway. The present invention has important applications to the design of novel drugs as well as protein engineering. The present invention predicts the three-dimensional structure of a protein independent of size of the protein, overcoming a significant limitation in the prior art.

The invention discloses a leucine dehydrogenase mutant and an application thereof, belonging to the technical fields of enzyme engineering and microorganism engineering. The present invention provides a leucine dehydrogenase mutant, compared with the leucine dehydrogenase whose amino acid sequence is shown in SEQ ID NO.2, the 72nd amino acid of the leucine dehydrogenase mutant is Mutating from lysine to alanine, the present invention conducts site-directed mutation of basic amino acid residues in the substrate channel of leucine dehydrogenase for the first time, transforms the structure and environment near the possible substrate binding site of the enzyme, and obtains Leucine dehydrogenase for more efficient production of L‑2‑GABA. The leucine dehydrogenase mutant leucine dehydrogenase mutant K72A that the substrate tolerance provided by the present invention improves can tolerate 4.5g / L 2-ketobutyric acid and for the substrate 2-ketobutyric acid Catalytic activity increased by 15%.

The invention relates to the biotechnology field, specifically relates to an improvement method of natural anticancer peptide. The method comprises the design improvements at two stages by use of natural polypeptide as a template; in the design improvement at the first stage, a series of polypeptide derivatives are obtained by changing the percentage of polypeptide net charge and the hydrophobic residue in the polypeptide; in the design improvement at the second stage, the variety and the number of the screened polypeptide amino acid residue are unchanged, only the primary amino acid sequence is changed, so that the alpha-helix in the high-level structure is located at different positions or disappeared to obtain the series of polypeptide again. The anticancer peptide prepared by use of the method disclosed by the invention is not only high in anticancer property, but also small in toxicity and safer to the human body.

Provided herein are Erysiphe necator resistance conferring genes, plants, plant parts and seeds comprising the present resistance providing genes and the use thereof for selecting Erysiphe necator resistant plants. Specifically, provided herein are Erysiphe necator resistance conferring genes, wherein the amino acid sequence encoded by said resistance conferring genes is the primary amino acid sequence represented SEQ ID No. 1, or a primary amino acid sequence with more than 70% identity, preferably more than 80% identity, more preferably more than 90% identity, and most preferably more than 95% identity with SEQ ID No. 1; and wherein said resistance conferring gene is impaired.

[Problem] To provide a polymer for nucleic acid delivery. [Solution] A polymer compound selected from a homopolymer of (a) and a block copolymer of (b). (a) A homopolymer comprising a polyglycidyl chain having a side chain including a primary amine. (b) A block copolymer of a polyglycidyl chain having a side chain including a primary amino acid, and a polyethylene glycol chain.

The invention relates to a preparation method and application of a composite targeting drug controlled release system using gold nano-cages as a carrier, and effectively solves the problems of existing tumor therapeutic drugs such as large side effects, poor therapeutic effect and tumor photothermal therapy. Add Re2O3, Fe(NO3)3, Mn(NO3)2, Zn(NO3)2, citric acid, ethylene glycol, gold nanocages to HNO3, adjust pH to 6, centrifuge, reconstitute the precipitate with water, adjust pH to 6 , dried to obtain gold nano-cages coated with manganese-zinc ferrite; heat the temperature-sensitive material, add drugs and gold nano-cages coated with manganese-zinc ferrite, and centrifuge to obtain manganese-zinc ferrite and temperature-sensitive materials gold nanocages-manganese-zinc ferrite complex; add OPSS-PEG-SVA into PBS buffer solution with primary amino target molecule, add gold nanocages-manganese-zinc ferrite complex, centrifuge, and precipitate with PBS buffer It can be washed with liquid to form a compound targeted drug controlled release system with gold nano cages as a carrier. The present invention simultaneously achieves the purposes of hyperthermia, chemical (gene) therapy, targeting and controlled release.

The invention relates to a method for preparing bonito stick protein hydrolysate with an effect of reducing uric acid. The method comprises the following main steps of raw material heat treatment, restriction digestion, membrane separation-anion exchange chromatography-gel filtration chromatography separation, concentration and spray drying so as to obtain the bonito stick protein hydrolysate with an effect of reducing uric acid. The amino acid analysis indicates that the zymolyte peptide fragment primary amino acid sequence contains four amino acids, namely histidine, arginine, lysine and threonine, the total mass content of the four amino acids is 70 percent of the total amino acid content of zymolyte. MALDI-TOF-MS mass spectrum determines that the molecular weight of the main peptide effective ingredient is less than 700Da. In-vitro uric acid reduction experiments prove that the bonito stick protein hydrolysate has a remarkable effect of inhibiting generation of uric acid, and has an inhibition rate over 50 percent; an oteracil potassium molded hyperuricemic rat animal model indicates that the bonito stick protein hydrolysate can be used for remarkably reducing the level of serum uric acid and serum creatinine of rats, and shows a relatively good kidney protecting effect.