Essay about What are Proteins and What do They Do?

This Lab Report is an analysis of the results of a two-part experiment. In the first part, we used a gel filtration column to separate the components of a mixture composed of protein and non-protein molecules. By doing so we hoped to obtain fractions that contained single components of the mixture, while also gaining insight into the relative molecular weight of each component compared to each other. We would then plot these fractions onto nitrocellulose paper in order to determine which fractions had protein. In the second part, we would use the fractions which we had determined had protein to conduct an SDS-PAGE. By doing so we hoped to determine an estimate on the molecular weight of the proteins present in each fraction by comparing it to a tracker dye composed of a variety of molecules of differing molecular weight.

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

This technique separates Rubisco samples based on their size. The electrophoresis has a positive and a negative end. Positive charge proteins are loaded from the positive end and migrate towards the negative end. Negative charge proteins are loaded from the negative end and migrate towards the positive end (Sakthivel & Palani, 2016). The sample that contained the highest molecular weight of Rubisco will travel the shortest distance on the gel while the protein with the smallest molecular weight will travel the longest distance (Sakthivel & Palani, 2016). The size proportion of each Rubisco molecule correlates with the distance traveled. Rubisco will be in its purest form after running through SDS-page since each technique will increase the purity of the protein. If the salting out, the ion exchange and the SDS-page protein isolation techniques are performed on protein Rubisco, then it is purified and separated by solubility, charge, and size. The rationale of this experiment is to isolate the purest form of Rubisco so that it can perform carbon fixation at an optimal

Figure 1 contains gel electrophoresis for protein samples. The lanes were labeled from 1 to 10 from the right to the left. Lane 1 contained the ladder fragment. Lane 2 contained the filtrate. Lane 3 contained the S1 sample. Lane 4 contained the P1 sample. Lane 5 contained the P1 medium salt sample. Lane 6 contained the P1 high salt sample. Lane 7 contained the S2 sample. Lane 8 contained the P2 sample. Lane 9 contained the P2 medium salt sample. Lane 10 contained the P2 high salt sample.

Data from previous studies suggest that the inactive sHSP takes on the oligomer conformation Upon stress, these oligomers assemble into active dimeric species, exposing previously inaccessible hydrophobic surfaces that can then interact with nonpolar patches on the misfolded substrate, capturing them in large complexes. The sHSP-substrate complexes maintain the substrate in a folding-competent state for extended periods of time. Biologically this is of utmost importance since it is

3. Explain why the structure of a protein is important to how the protein functions. It’s important because it can make many complex shape and each shapes can have different functions.

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.

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

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.

The Functions of Proteins Introduction Protein accounts for about three-fourths of the dry matter in human tissues other than fat and bone. It is a major structural component of hair, skin, nails, connective tissues, and body organs. It is required for practically every essential function in the body. Proteins are made from the following elements; carbon, hydrogen, oxygen, nitrogen and often sulphur and phosphorus.

Introduction: The goal of this experiment was to practice using the FirstGlance in Jmol molecular visualization to examine key structural features of proteins. This work is important because protein structure can be related to function, multiple-sequence alignments and evolutionary preservation, and designing drug. FirstGlance in Jmol makes it fairly easy to perceive structure-function relationships in the protein you chose. Using FirstGlance, it is easy to visualize and distinguish chains, and disulfide bonds are obvious. Alpha helices and beta strands are evident due to the "cartoon" secondary structural schematic.

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

These new formations are held together by hydrogen bonds. The third level is the tertiary structure. The tertiary structure of a protein is a contorted secondary structure being twisted and folded all out of shape to form a 3-d complex. The type of bonding that holds these formations together are weak interactions such as hydrophilic, hydrophobic, ionic, and hydrogen bonds. These bonds are individually weak, but collectively strong. The forth level, which completes a protein, is quaternary structure, which occurs when two or more tertiary structures are joined together by polypeptide bonds.