Summary of BIOQUÍMICA PARA VETERINARIOS. PROTEÍNAS

00:00:00 - 00:40:00

This video explains the different types of amino acids and their role in protein synthesis. Amino acids are classified according to their nutritional value, with essential amino acids being those that the body cannot produce on its own and must be obtained from food. Amino acids can also be classified according to their structural shape, with alpha-amino acids being linear and beta-amino acids being branched. Finally, the video discusses the two most common amino acid notation systems.

• 00:00:00 This video discusses the chemistry behind protein synthesis and protein function, with a focus on the 20 most common amino acids. The main points made are that proteins are composed of linear chains of amino acids, and that they can be divided into two main categories based on their molecular weight: small proteins (between 50 and 1000 amino acids in length) and large proteins (more than 1000 amino acids in length). Proteins can be broken down into their component amino acids through hydrolysis, a chemical process that cleaves a protein chain into amino acids.
• 00:05:00 This video discusses the different types of amino acids and their roles in protein synthesis. Amino acids are classified according to their nutritional value, with essential amino acids being those that the body cannot produce on its own and must be obtained from food. Amino acids can also be classified according to their structural shape, with alpha-amino acids being linear and beta-amino acids being branched. Finally, the video discusses the two most common amino acid notation systems.
• 00:10:00 This video discusses the role of amino acids in protein synthesis and metabolism. The main points are that amino acids are the building blocks of protein and that they form an array of hydrocarbons when combined together. Aromatic amino acids (those containing a ring structure) are particularly important because they form hydrocarbons that are Insaturated. One of the most common aromatics is benzoic acid, which forms benzene rings. Amino acids that are standard (those that contain a carboxyl group) have side chains that contain groups that interact with water, which gives them the ability to form bridges between water molecules. These bridges allow proteins to interact with other molecules more easily, which is important for their biological activity. Amino acids that have a positive charge at a physiological pH also have the ability to form peptides. Finally, amino acids are also important for their role in metabolizing other molecules and acting as intermediaries in biochemical pathways.
• 00:15:00 This video discusses the biochemical properties of proteins. It covers nitrogenated proteins, which contain derivatives of amino acids that are formed after proteins are synthesized as chains of oligopepptides. One of these proteins is the carbonic anhydrase, which is a by-product of amino acid synthesis. The image shows various modified amino acids, which are found in proteins. Amino acids that contain a hydroxy group (4-hydroxyproline and 5-hydroxylinoleate) are structural components of collagen. Collagen is the protein with the most abundance in connective tissue. The fosforilation of amino acids that contain a hydroxyl group (serine, threonine, and methionine) is often used to regulate protein activity. The biochemical reactions that proteins undergo are as follows: they can release their groups of carbon atoms, lose their amino groups, and undergo reactions with other compounds that lack a functional group. Two amino acids can join together to form a peptide, which is a new molecule that has the properties of both amino acids. The name for this type of bond is covalent bond, and it is strong enough to share atoms between the molecules. Proteins are soluble in water and can present
• 00:20:00 This video explains the biochemistry behind protein synthesis, and how proteins are made from amino acids. There is an important relationship between carboxyl and amino groups on adjacent molecules, and this interaction leads to the formation of peptides. Peptides are chains of amino acids linked by peptide bonds, and they are the basic building blocks of proteins. Proteins are the most abundant molecules in living organisms, and they are essential for the function of cells. Some important peptides include glutamine, oxytocin, and vasopressin.
• 00:25:00 This video discusses the biosynthesis of proteins and the importance of proteins in the body. The video explains that proteins are composed of amino acids and that there are different levels of protein organization, including the primary structure, which is determined by the sequence of amino acids in a protein's genetic code. The secondary structure is determined by the arrangement of these amino acids within the protein and the tertiary structure is the overall 3-dimensional shape of the protein. Proteins can have multiple secondary structures, and some proteins have a primary and a tertiary structure.
• 00:30:00 This video sequence is determined by the DNA in the cell nucleus and this also determines the specificity of each protein, that is, this order or sequence of amino acids with respect to the secondary structure of polypeptides, which consist of several repeated patterns. The structure secondary is called because it is the spatial arrangement of the peptide chain's molecular structure, and in which circular and weak links are observed between group carbon atoms and amino group of the chain's main protein structure, these links being of type hydrogen bridge. These links can also adopt several forms, such as alpha helices and beta sheets folded. In the case of alpha helices or alpha helices, these are rigid structures formed when a peptide chain is twisted into a helicoidal right configuration at this point, and the links of hydrogen are formed in the nitrogen or amino group of each acid wine molecule and the carbon albox group, and the amino acid to 4 residues of distance from the carbon albox group in the case of beta sheets, these are second type of structural secondary structures in which a peptide segment is extended completely in a structure of type exact types. The solitary beta chains found in birds are caused by the proteins because they are unstable. However, when two or more beta chains align side
• 00:35:00 This video discusses the molecular composition of proteins, which are composed of many small molecular weight proteins. These complexes are called proteomes. Each protein in a proteome consists of several Polipéptidos chains each made up of different Polipéptidos molecules. These molecular complexes are called subunits and the number of subunits in a proteome can be identical or quite different. This assembly or self-assembly is given by weak non-covalent bonds and, in general, all proteins have at least one such bond. Some proteins do not have this bond, and proteins have more than one Polipéptido chain. Some proteins, such as hemoglobin, have multiple Polipéptido chains. The primary structure of a protein is made up of linear chains of union of amino acids. The secondary structure is made up of several secondary structures, each of which is composed of numerous proteins. The tertiary structure is made up of several tertiary structures, each of which is composed of several proteins. The quaternary structure is made up of several quaternary structures, each of which is composed of several proteins. Certain interactions between functional groups in proteins allow them to break down or degrade. This process is called denaturation and is
• 00:40:00 This video discusses the biochemistry of proteins. Other molecules and elements, for example hemoglobin which contains a quaternary protein as well as iron and other elements, are shown in the table below. We see examples oflasseter proteins or proteins with "jumped" amino acids--that is, they have a part of protein, but also have an non-protein component. The first is the nucleoprotein, which has the protein and the non-protein component in the same molecule, and the most common example is the ribosomes. The nuclei or more of the chromatin in cells. And in the case of lipoproteins, the non-protein component are the lipids, and the examples are the different types of lipoprotein, such as LDL, HDL, and B-Ldlr. Finally, we discuss proteins in terms of their structural composition and can be classified as fibrous or filamentous, due to their structural support in tissue. They are highly resistant to cutting, have parallel political chains, and can form networks of several phases to form a macro-fiber. They are also only soluble in water and in saline solutions, and are more resistant to degradation--that is, breaking down into their constituent peptides.