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The Main Features And Structure Of Protein

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Proteins are large biomolecules, or huge molecules, made up of a long chain or more of amino acid residues. Proteins perform a wide range of functions within organisms, including stimulating metabolic reactions, replicating DNA, and responding to stimuli that provide structures for cells, organisms, and molecules from one place to another.

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The proteins differ primarily in their sequence of amino acids, dictated by the nucleotide sequence of their genes, which usually results in protein folding in a specific three-dimensional structure that determines its activity. The linear chain of amino acid residues is called polypeptide. Protein contains at least one polypeptide. Rare polypeptides are rarely considered to contain less than 20-30 residues of proteins and are usually called peptides, or sometimes oligopeptides. The residues of individual amino acids are linked together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in the protein is defined by the sequence of an encoded gene in the genetic code. In general, the genetic code identifies 20 standard amino acids; however, in some organisms the genome can include selenocysteine and-in Certain arches – Perulin. Soon after or even during synthesis, the residues in the protein are often chemically adjusted by post-translation modification, which changes the physical and chemical properties, stability, stability, activity, and, ultimately, the function of the proteins. Sometimes proteins contain non-peptides, which can be called artificial groups or adjuvants.

Proteins can also work together to achieve a specific function, often associated with the formation of stable protein complexes. Once proteins are formed only for a certain period they are then degraded and recycled by the cell device through the protein turnover process. Protein life is measured in terms of half-life and covers a wide range. They can be present for minutes or years with an average lifetime of 1-2 days in mammalian cells. Abnormal or abnormal proteins decompose more quickly either because they are targeted for destruction or because of their instability. Like other biomolecules such as sugars and nucleic acids, proteins are essential parts of living organisms and participate in almost every process within cells. Many proteins are enzymes that stimulate biochemical reactions and are vital to metabolism. Proteins also contain structural or mechanical functions, such as actin and myosin in muscles and proteins in the cytoskeleton, which form a system of scaffolds that preserve the shape of the cell.

Other proteins are important in cell signaling, immune responses, cell adhesion, and cell cycle. In animals, proteins are needed in the diet to provide essential amino acids that cannot be synthesized. Digestion breaks proteins for use in metabolism. Proteins can be purified from other cellular components using a variety of techniques such as super filtration, sedimentation, electrophoresis, and chromatography; the advent of genetic engineering has provided a number of ways to facilitate purification. Methods commonly used to study the protein structure and function include immunochemistry, site-oriented mutation, crystal crystallization of X-rays, nuclear magnetic resonance (NMR) and mass spectrometry.

Most proteins fall into a unique three-dimensional structure. The form in which the protein naturally develops is known as its original form. Although many proteins can be folded without help, simply by the chemical properties of their amino acids, others need to help molecular accomplices bend in their original states. Biochemists often refer to four distinct aspects of protein structure.

Primary structure: Sequence of amino acids. Protein is polyamide.

Secondary structure: Replicate local structures regularly through hydrogen bonds. The most common examples are alpha – and – sheet – and – paper. Because secondary structures are localized, many areas with different secondary structures can be found in the same protein molecule.

Triple structure: The general shape of a single protein molecule; the spatial relationship between the secondary structures of each other. The tripartite structure is generally stabilized through non-local reactions, most commonly the formation of a frantic nucleus, but also through salt bridges, hydrogen bonds, bipolar bonds, and even post-transfer modifications. The term “triple structure” is often used as a synonym for “fold”. The trigeminal structure controls the essential function of the protein.

Quad structure: The structure consists of several protein molecules (peptide chains), usually called protein subunits in this context, which act as a single protein compound. Proteins are not completely rigid molecules. In addition to these levels of structure, proteins may move among many relevant structures while performing their functions. In the context of these functional rearrangements, these triangular or quadrilateral structures are usually referred to as “matching”, and they are called transitions. These changes are often made by binding the substrate molecule to an active site of the enzyme, or the physical area of the protein involved in the chemical catalysis. In solution proteins, a change in structure occurs through thermal vibration and collisions with other molecules.

Proteins can be divided informally into three main categories associated with typical triangular structures:

  • Spherical proteins
  • Fiber proteins
  • Membrane proteins.

Almost all spherical proteins are soluble, many of which are enzymes. Fibroids are often structural, such as collagen, the main component of connective tissue, or keratin, the protein component of hair and nails. Membrane proteins often act as receptors or provide channels for polar or charged molecules to pass through the membrane. A special case of hydrogen bonds between molecules within proteins is called, poorly protected from water attack, thus promoting their own dehydration, dehydrations.

18 March 2020

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