Preview

Protein Structure Lab Report

Better Essays
Open Document
Open Document
1410 Words
Grammar
Grammar
Plagiarism
Plagiarism
Writing
Writing
Score
Score
Protein Structure Lab Report
Task 1
• Describe the structure of an enzyme as a protein, in terms of tertiary/ quaternary structures.
1) Primary Structure

This is in reference to the order of way that amino acids are connected to form a protein. These are built up from 20 amino acids, and follow these structures o A carbon (the alpha carbon) bonded to the four groups below: o A hydrogen atom (H) o A Carboxyl group (-COOH) o An Amino group (-NH2) o A "variable" group or "R" group

2) Secondary Structure

This is in reference to the fold like structure of a polypeptide chain that gives the protein a 3d like shape. There is 2 types of secondary structure which are:
Alpha Helix
This would resemble a coiled spring which is secured by hydrogen bonding in a polypeptide chain.
Beta Pleated Sheet
This would resemble folds/pleats that is held together again by a hydrogen bond between a polypeptide of the folded chain that lie next to each other.

3) Tertiary
…show more content…
Indicate from your results, what the optimal temperature for enzyme activity was.
PH was 4 and Temperature was 70 degrees
c. What happens to the enzyme activity at temperatures higher than the optimal temperature/PH?

PH
Most proteins, and therefore enzymes, are active only within a narrow pH range usually between 5 and 9. Several factors are influenced directly by the pH in which the reaction takes place.
• the binding of substrate to the enzyme
• The ionization states of the amino acid residues involved in the catalytic activity of the enzyme.
• the ionization of the substrate
• Variation in the protein structure at extreme pH.
Temperature
The temperature range over which enzymes show activity is limited between the melting point (0oC) and boiling point (100oC) of water. If a temperature is too low, there can be no noticeable reaction rate since the enzyme is operating at a temperature far below its optimum. If the temperature at which the enzyme is operating at is well above 100oC, then thermal deactivation can

You May Also Find These Documents Helpful

  • Good Essays

    The tertiary structure is the folding of the polypeptide chain after it has determined its secondary structure. Its shape is due to bonding between the side chains (R groups) (see figure 11), these include;…

    • 803 Words
    • 4 Pages
    Good Essays
  • Good Essays

    Biology 101 Study Guide

    • 476 Words
    • 2 Pages

    The directions for each amino acid in a polypeptide are indicated by a codon that consists of…

    • 476 Words
    • 2 Pages
    Good Essays
  • Good Essays

    etched

    • 686 Words
    • 3 Pages

    Q: Describe and give examples of proteins that have a variety of tertiary structures. Relate the tertiary structure of these proteins to their biological functions.…

    • 686 Words
    • 3 Pages
    Good Essays
  • Good Essays

    Proteins are complex molecules that each has a very unique shape, structure and function. The shape of the proteins is held up by a chain of subunits called amino acids that are connected by peptide bonds. Protein structures are formed by four levels of folding. The primary structure is the linear sequence of amino acids. The secondary structure describes the folding of alpha helixes and beta pleated sheets. The tertiary structure represents the overall shape of the protein and the quaternary structure only occurs in a protein consisting of more than one amino acid chain. When the shape, the structure or the function of proteins is incorrect, it is likely because of some type of change in the sequence of the amino acids or whether a certain amino acid required is present.…

    • 581 Words
    • 2 Pages
    Good Essays
  • Good Essays

    Secondary structure; Formed when the chain of amino acid coils or folds to form an alpha helix or beta pleated sheet.…

    • 701 Words
    • 2 Pages
    Good Essays
  • Good Essays

    The secondary structure is the folding of the amino acid chains into an alpha-helix or a beta-pleated sheet. It is determined by the sequence of amino acids in the primary structure. The polypeptides within the secondary structure are held together by many hydrogen bonds, which give the structure great…

    • 1424 Words
    • 6 Pages
    Good Essays
  • Good Essays

    Quaternary: Protein consisting of more than one amino acid chain. Relationship between structure (3-D shape) and function…

    • 4655 Words
    • 19 Pages
    Good Essays
  • Good Essays

    Enzyme Summary

    • 654 Words
    • 2 Pages

    The secondary structure is a regular, repeated, coiling and folding of a protein's polypeptide backbone. This folding is stabilized by hydrogen bonds between peptide linkages. These sections of polypeptide chains are repeatedly coiled or folded into patterns that add to the protein's overall conformation. There are two types of secondary structures. They are alpha helixes and beta pleated sheets. Alpha helixes are helical coils stabilized by a hydrogen bond between every fourth peptide bond. They are usually found in fibrous protein such as keratin and collagen. Beta pleated sheets are structures where two regions of the polypeptide chain lie parallel to each other. Again hydrogen bonds between the parts of the backbone in the parallel regions hold the structure together. The cores of many globular proteins are made of beta pleated sheets.…

    • 654 Words
    • 2 Pages
    Good Essays
  • Good Essays

    Four Primary Levels

    • 915 Words
    • 4 Pages

    The third of four levels of protein structure is the tertiary level. The primary level are strands of the 20 amino acids, the secondary level are alpha helix and beta pleats, the tertiary level are a combination of helix, pleats, and bends, and the quaternary level involves multiple polypeptide bonds. The tertiary level is a three dimensional level that allows the protein to be fluid and move and make up the R group in the protein structure. There are four different bonds and interactions which may be polar, nonpolar, or charged. The structure is important as it determines what that protein will do in the cell whether it be an enzyme or transporter. (Particle Sciences, 2009) . The first interaction…

    • 915 Words
    • 4 Pages
    Good Essays
  • Good Essays

    Quaternary Structure

    • 1027 Words
    • 5 Pages

    For this assignment you don't need to use other sources besides the information given in the commentary, animations, and/or textbook. However, you may consult outside sources as necessary for completing this assignment. Please, always cite your sources: that includes citations from the commentary, the textbook, and the animations, as well as outside sources (if used). See APA Style for appropriate citation style.The last protein structure to mention is quaternary (4º). This type of structure refers to the arrangement of subunits and to the nature of the subunits interactions. To sum this up proteins that consist of more than one polypeptide chain will display quaternary structure. Each individual polypeptide chain in a protein is referred to as a subunit. A dimer is known to be the simplest sort of quaternary structure as it…

    • 1027 Words
    • 5 Pages
    Good Essays
  • Good Essays

    Structures of Proteins

    • 716 Words
    • 3 Pages

    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.…

    • 716 Words
    • 3 Pages
    Good Essays
  • Powerful Essays

    A proteins secondary structure comes from the folding and coiling of the proteins polypeptide chains. A secondary structure can be a helix, or pleated sheet. Helix secondary structures is a coil formed together by hydrogen bonding, pleated sheets have two or more parts of the polypeptide chain lying beside one another. An overall shape of a polypeptide is referred to as a tertiary structure, that results from interactions between the R groups of amino acids. One interaction that shapes polypeptides is called a hydrophobic interaction, which occurs when a nonpolar substance is excluded by water.…

    • 1401 Words
    • 6 Pages
    Powerful Essays
  • Good Essays

    As the temperature increases, there is more movement of molecules and more random collisions between enzymes and substrates. This results in an increase in enzyme activity, but there is a limit to which enzyme activity can increase because at a certain temperature an enzyme will denature due to disruption of noncovalent bonds. Reactions…

    • 580 Words
    • 3 Pages
    Good Essays
  • Better Essays

    Protein Folding

    • 679 Words
    • 3 Pages

    The primary structure of a protein contains the distinct chain of amino acids. (Reece, 2011). The secondary structure refers to segments of polypeptide chains which are folded or coiled, as a result of hydrogen bonding on the polypeptide backbones. (Reece, 2011). The electrognetaive oxygen and nitrogen atoms both have a partial negative charge and attach to the weakly positive hydrogen atom. (Reece, 2011). There are two secondary structures that can form: an ɑ helix, with hydrogen bonding every fourth amino acid, and a β pleated sheet when the polypeptided backbones bond to form parallel or anti-parallel sheets.(Reece, 2011). The tertiary structure creates the overall shape of a polypeptides produced by interactions between the amino acid’s side chains. (Fitzpatrick et al, 2011). This interaction plays an important role in stabilizing the protein.(Reece, 2011). The non polar side chains will move, away from water, to the core of the protein, as a because of hydrophobic interactions (Reece, 2011). Once the non polar amino acids are close by they are held together by van der Waals interactions. Other interactions include more hydrogen…

    • 679 Words
    • 3 Pages
    Better Essays
  • Good Essays

    Different sequence of amino acid produces different structure of protein, which determines the property of protein, thus each kind of enzymes has its unique active site, which only fits to complementary – shaped substrate to form product. Because of the feature of active site, each kind of enzymes therefore is specific for a particular reaction. However, there are several factors affect the rate of enzyme reactions, they are temperature, pH, concentration of enzyme, concentration of substrate and inhibitors. High temperature and pH affects the structure of enzyme, irreversible denaturation occurs, the shape of active site is changed, enzymes therefore no longer function. The effect of the other factors is slowing down the rate of enzyme reactions, it depends on the concentration of those factors. Since enzymes are catalyst of chemical reactions, they are responsible to the activities of cells, and they determine the function of tissues and organs as well.…

    • 625 Words
    • 3 Pages
    Good Essays