Functions Of Protein Gamma Secretase Essay

Different types of bonds/interactions in proteins lead to different kinds of structures. Three of the most commonly known chemical bonds in proteins include the hydrogen bond, the covalent bond, and the ionic bond. In hydrogen bonds, hydrogen interacts with oxygen, nitrogen, or fluorine to form either the alpha helix, or the beta sheet, which in turn determines its secondary, tertiary, or quaternary structure. Another type of bonds, the covalent bond, links amino acids together by sharing electrons;

A protein has multiple existing structures, these are the primary, secondary, tertiary and quaternary structures which occur progressively. A protein is essentially a sequence of amino acids which are bonded adjacently, and interact with one another in various ways depending on the R group that the amino acid contains. There are 20 different amino acids which are able to be arranged in any given order, thus giving rise to a potential 2.433x1018 (4.s.f) different combinations, and therefore interactions between the various amino acids.

Proteins are complex structures made up of chains of amino acids. Each protein has a different function such as enzymes to catalyze reactions or protein hormones to trigger certain functions of a cell. First let’s start with the most basic component of a protein: an amino acid. An amino acid is made up of a central carbon atom attached to a hydrogen atom, a carboxyl group, an amino group, and an R group which varies

their normal shape to an abnormal shape, however, the chemical composition of the protein remains

They are made up of amino acids (consists of amino group, carboxyl group, hydrogen atom, and R group). Polypeptide bonds form between amino acids to form polypeptide chains. Amino acid sequence is primary protein structure. The secondary structure is the bonding pattern of the amino acids (e.g. helix, sheet, etc.). The tertiary structure consists of the domain, where the sheets or helixes fold on each other and become stable. The quaternary structure consists of several polypeptide chains that form advanced proteins such as human leukocyte

Proteins are molecules containing amino acids, which our body and cells need to keep our bodies functioning properly. Body structure, functions and regulates the body's cells, tissues

Proteins are biological macromolecules made from smaller building units called amino acids. There are 20 natural occurring amino acids which can combine in various ways to form a polypeptide. There are four distinctive levels of protein structure: primary, secondary, tertiary and quaternary. The primary structure of a protein is important in determining the final three dimensional structure and hence the role and function of a particular protein, both in the human body and in life around us. The secondary structure of a protein can fall into two major categories; α-helices or β-sheets, other variants also exist such as β-turns {{20 Brändén, Carl-Ivar, 1934- 1991}}. The precise folding or these secondary structures into a three dimensional shape is known as the tertiary structure of a protein and multiple polypeptides bound together via covalent and non-covalent bonds forms the complex quaternary structure of a protein.

B. Original diagram of the different levels of protein structure (i.e., primary, secondary, tertiary, and quaternary).

The primary structure of a protein is simply the sequence of amino acids. The structure or

The four levels of protein structure are primary, secondary, tertiary, and quaternary. All of the levels are made from the primary structure of the protein. Primary structure contains covalent bonds and is the foundation and basis for the other levels of a protein. Secondary structure is a repeated continuation of a peptide chain.

The sequence of amino acids determines each protein's unique 3-dimensional structure and its specific function. Antibodies bind to specific foreign particles, such as viruses and bacteria, to help protect the body. Enzymes carry out almost all of the thousands of chemical reactions that take place in cells. Proteins do most of the work in cells and are required for the structure of the cell, the function of the cell, and the regulation of the body’s tissues and organs in the cell. They are made of groups called amino acids.Proteins have a large variety of different shapes and sizes. If the shape changes, it becomes a new protein. Protein is found in your muscles and the cell

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

3. The structure of a protein such as hemoglobin is very similar to an enzyme. The primary structure is the amino acid sequence. The secondary structure is the bonding of primary structures with the use of hydrogen. Tertiary structure is the bonding of the previous stage by covalent bonds. The final Quarternary structure involves more than one amino acid sequence. When a protein such as hemoglobin is heated, its bonds will be broken, causing a delay on the speed in which it is able to carry oxygen.

2014). Ultimately, a protein can take on the tertiary structure which is a combination of all the secondary structures (Alberts, B. 2014). Furthermore, most proteins take on the quaternary structure which consist of two or more polypeptide chains that form a protein complex of a honomer or heteromer (Alberts, B. 2014).

These complexes are called dynamic or fuzzy complexes. These are protein complexes wherein the disordered protein has bound to its partner and undergone a conformational change into a fixed structure but has retained a disordered region that significantly contributes to the function of the complex. There are four known categories for these fuzzy complexes, dependent on the location of the disordered region: polymorphic, clamp, random, and flanking. Polymorphic refers to a static disorder where the molecule that binds changes into two unrelated conformations; the clamp model refers to when two regions are connected by a linker that remains disordered; flanking refers to when a disordered region remains near the binding site and increases binding affinity; and random complexes refer to when the majority of the complex retains its disordered state. These fuzzy regions have been suggested to be an evolutionary advantage because these intrinsically disordered regions aid in complex formation, allow for longer range interactions between their target partners, and overall increases the functionality of the protein. One study has also suggested that the environment has a larger than previously thought role in the binding of IDPs to other proteins, particularly they are far more sensitive to ionic environments than their folded counterparts.