Disadvantages Of Syntactical Based Features

Each gene acts as a code, or set of instructions, for making a particular protein. They tell the cell what to do, give its characteristics, and determine the way its body works. Each protein has a unique sequence of amino acids. This means that the number and order of amino acids is different for each type of protein. The proteins fold into different shapes. The different shapes and sequences give the proteins different functions, e.g. keratin are a fibrous protein found in hair and nails. If the gene has even the slightest of disorder within its sequence it could lead to an inaccurate order of amino acids

For the peptide Ala-Arg-Lys-Ala-Asn-Ser-Ala-Ser, what would be the expected charges at pH 1, 7, and 13?

The main focus of this project is reducing the feature extraction time of the system. As a conclusion, it shows that our framework extracts the features from the parse tree very fast. This paper can be further enhanced by using the hybrid classification algorithm to get more accuracy in classification. In this paper, the parse tree is obtained from the PostgreSQL databases and in future, it will get from MySQL databases. To decrease the feature extraction time, fragmented files will be processed in

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

The amino acids bond together in bonds called peptide bonds. A chain of amino acids is called a polypeptide chain. The structure in which the amino acids are bonded determines the function of the protein. There are about twenty different amino acids, but there is a wide variety of possible combinations that amino acids can bond, therefore proteins have quite a lot of functions. Some things proteins are used for are the building of the muscles, tendons, organs, glands, nails, and hair. There are many more different functions for proteins. To detect proteins in test materials, there is an identifying agent called Biuret Solution which when mixed with the test material. It turns purple if it contains a protein. The darker the violet color, the more concentrated it is with protein.

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

There are 20 amino acids. Most of the time you use an L-enantiomer of the amino acid, however, you can have D-enantiomer forms.  D-forms are often found in antimicrobial compounds and ionophores.

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

Amino acids are the smaller building blocks which protein is made of. There are 20 different amino acids. Depending on length, sequence of amino acids and function; each protein has unique different from each other. These amino acids have unique 3D shapes by fold up in complex ways.

Primary folding is the first and most basic layer. This layer contains the sequence of amino acids themselves. The structure and order of the amino acids is important because it helps determine the interaction type seen in the protein while it is folding. The interaction of the amino acids will show what the secondary and tertiary structure of the protein will be.

For the second part of the experiment, one had to use the knowledge learn from viewing protein molecules in FirstGlance in Jmol to analyze the protein PDB ID: 4EEY. The analysis of this protein was done using the RSCB protein data bank (PDB) at (http://www.rcsb.org/pdb/home/home.do).2

a) The tertiary structure refers to the structural arrangement of amino acids that are found far away from one another along the polypeptide chain. The tertiary structure is overall a three dimensional shape of a protein molecule. It will bend and twist to achieve maximum stability. The shape of a tertiary structure is made when the secondary structure folds in on itself and is held in place by many bonds and interactions formed by the R groups in the amino acid chain. The bonds and interactions involved are hydrogen bonds, ionic bonds, hydrophobic interactions and disulphide bonds. These bonds and interactions are located in different areas of the tertiary structure, the hydrogen bonds are located inbetween polar R groups, ionic bonds are located between charged R groups, hydrophobic interactions are located between nonpolar R groups and disulphide bonds are formed generally in the endoplasmic reticulum by oxidation ."Hydrogen bonds may form between different side­chain groups." Hydrophobic interactions are brought about in an aqueous site. The tertiary structure is held together mainly by interactions that are located at the R groups.

In most instances, protein molecules are usually embedded from hundreds to thousands of amino acids. A repertoire of twenty different amino acids, joined in any possible sequence allows the existence of an inconceivably large number of proteins that is infinite in nature.

the amino acid is in an acidic or basic salt form). Another point of interest