Lab 2 Chemistry

3. State the name and structure of the functional group for each type of biologically

Polymers have different structures. They also have different functions. Describe how the structures of different polymers relate to their function?

-The more dissolved oxygen in the water, the more fish is observed in that area of water.

There are many types of chemical bonds and forces that bind molecules together. The two most basic types of bonds are characterized as either ionic or covalent. In the lab we separated Citric Acid, Calcium Chloride, Sucrose, Potassium Iodine, Phenyl Salicylate ,and Sodium Chloride into two groups ionic and Covalent bonds .The Chemical Difference between ionic bonding and covalent bonding is, a covalent bond is formed between two nonmetals that have similar electronegativities. Metals are left half and center of the Periodic Table and Nonmetals are upper right of the Periodic Table. The electrical attraction between large numbers of cations and anions which is the transfer of the

8) Look at water as a gas. The molecules now have two types of motion. Linear and rotational.

1. Place a small amount of wax from a birthday candle into a test tube. Heat gently over a burner flame until the wax melts completely; then allow

1. Arrange the following molecules from least to most specific with respect to the original nucleotide sequence: RNA, DNA, Amino Acid, Protein

The range of normal resting systolic BP for the subjects in this experiment is 115-125 mmHg. Did systolic BP increase, decrease, or not change with exercise?

C) Each organic molecule is modular and the smaller molecules or monomers can be constructed into larger molecules or polymers (Open Learning Initiative, 2015, pg.63).

The proof (twice the % alcohol) starts at its maximum and goes down (as the alcohol evaporates). If we start with a high concentration of alcohol, we will get the azeotrope (95% alcohol, 5% water) for a while, then the concentration will decrease.

as the cytosine at position 34, cytosine at position 12, and tyrosine at position 29. In

After questions are answered, move to the next section .In the right side of the page, there is an animation about ATP and their bonds. The bonds of the ATP break by clicking on its latch. After, the ATP was reassembled by moving the ATP back together to form the latch once again. After, the questions are answered. After in the next part of the experiment, the instructions are read then a prediction was made; after, the effort slider was moved to the right then an observation was made. After the observation was made, the correct answer was recorded. Next page, the start bottom was clicked on. The next page an animation of the four processes of the cellular respiration. The step button was clicked on to see the breakdown then reset. After, a diagram was presented of the four processes and answered the questions .Afterword’s, the cyclist animation was present, based on the information presented a prediction was made. After prediction was made, the exercise was completed. In the right side of the page, clicked on minimal to change oxygen; also, the effort slider was moved to the right and compared back and forth between normal and minimal. After an observation was made then the questions are answered. In the other page, the redox bottom was clicked on and an observation was made . After, the questions are answered; then check the answers. Next page is the redox exercise , the labels located at

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.

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.

The purpose of this lab is to test substances and to determine the physical and chemical properties of substances.