BIOSC-101 Lecture Notes - Lecture 3: Chemical Energy, Surface Tension, Organic Compound

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turquoiseturtle299

9 Sep 2020

School

Diablo Valley College

Department

Biological Science

Course

BIOSC-101

Professor

hoffman

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Document Summary

Solutions are mixtures of 2 or more substances. The substances are evenly distributed throughout the solution; this means that you can sample any part of the solution and the composition of the solution will be the same. Solvent: the component of the solution in the greatest quantity. Solute: the component(s) present in lower quantities. Substances that will dissolve in water are hydrophilic or water loving. Molecules that do not dissolve in water are hydrophobic. Oils and fats are nonpolar and will not form a solution in water. Cohesion is a property of matter in which particles tend to stick together. Cohesion causes surface tension (which is the capacity of a liquid"s surface to resist being ruptured when place under tension or stress) to develop. Cohesion results from water molecules sticking to other water molecules due to the hydrogen bonds that form between them. Adhesion is the attraction between water molecules and other molecules.

Related Questions

I JUST NEED SIMPLE/BASIC ANSWERS NOT LONG ANSWERS

1. Explain how life can be viewed at different levels of biological complexity.

2. Explain how researchers study biology at different levels, ranging from molecules to ecosystems.

3. Distinguish between discovery-based science and hypothesis testing, and describe the steps of the scientific method.

4. Tell whether a given topic or research study is about biology. Tell whether that study is discovery-based or hypothesis testing, or both.

5. If presented with a research study, propose what the Research Question was.

6. If presented with an example, tell whether a statement is a hypothesis, theory or law and why you think so.

Describe the general structure of atoms and their constituent particles.

Relate atomic structure to the periodic table of the elements. List the elements that make up most of the mass of all living organisms.

Explain how a single element may exist in more than one form, called isotopes, and how certain isotopes have importance in human medicine.

Compare and contrast the types of atomic interactions (bonds) that lead to the formation of molecules.

Tell which atoms and how many of each make up a given molecule (formula or diagram).

For a bond in a given molecule, tell whether the bond is covalent, and if it is, tell whether it is polar or nonpolar and why you think so.

Explain the concept of electronegativity and how it contributes to the formation of polar and nonpolar covalent bonds. Tell whether a given atom is electronegative or not, and why you think so. Label partial charges in a polar bond.

Draw five water molecules and label the atoms and bonds within and between the 5 molecules.

Describe how hydrogen bonding determines many properties of water.

List the properties of water that make it a valuable solvent, and distinguish between hydrophilic and hydrophobic substances.

Explain how water has the ability to ionize into hydroxide ions (OH^â) and into hydrogen ions (H⁺), and how the H⁺ concentration is expressed as a solution's pH.

Explain the properties of carbon that make it the chemical basis of all life.

Describe the variety and chemical characteristics of common functional groups of organic compounds.

Diagram how small molecules may be assembled into larger ones by dehydration reactions and how hydrolysis reactions can reverse this process.

List the four major classes of organic molecules and macromolecules found in living organisms

If shown a molecule, tell whether it is organic or not and how you know.

If shown an organic molecule, tell whether it is an amino acid, nucleotide, fatty acid, steroid, monosaccharide or disaccharide and how you know.

Distinguish among different forms of carbohydrate molecules, including monosaccharides, disaccharides, and polysaccharides.

Relate the functions of plant and animal polysaccharides to their structure.

List the several different classes of lipid molecules important in living organisms.

Diagram the structure of a triglyceride and explain how it is affected by the presence of saturated and unsaturated fatty acids. Explain why some fats are solid at room temperature, and others are liquid.

Discuss how fats function as energy-storage molecules.

Apply knowledge of the structure of phospholipids to the formation of cellular membranes.

Describe the chemical nature of steroids and give an example of their biological importance.

Give examples of the general types of functions that are carried out in cells by different types of proteins.

Explain how amino acids are joined to form a polypeptide, and distinguish between a polypeptide and protein.

Describe the levels of protein structure and the factors that determine them. If shown a protein diagram, label parts that represent its levels of structure. Tell what kind of research techniques are used to determine protein structure.

Outline the bonding forces important in determining protein shape and function.

Explain what domains are and their importance in proteins.

Describe the three components of nucleotides.

Distinguish between the structures of DNA and RNA.

Tell how certain bases pair with others in DNA and RNA.

Discuss the 4 major categories of organic macromolecules found in living things, including structure, function and location of each.

Compare and contrast the general structural features of prokaryotic and eukaryotic cells.

Outline the differences in complexity among bacteria, animal, and plant cells.

Describe how a eukaryotic cell can be viewed as four interacting systems: the nucleus, cytosol, endomembrane system, and semiautonomous organelles.

Explain how the proteome underlies the structure and function of cells.

Analyze how cell size and shape affect the surface area/volume ratio.

Identify the location of the cytosol in a eukaryotic cell and list its general functions.

Describe the three types of protein filaments that make up the cytoskeleton. Identify which underlie cilia, flagella, centrioles, the nuclear lamina, and the brush border. Tell which are readily assembled and disassembled. Tell which are involved in various cell shape changes or movements.

Explain how motor proteins interact with microtubules or actin filaments to promote cellular movement.

Describe the structure and organization of the cell nucleus. Describe the structure and function of nuclear pores.

Outline the structures and general functions of the components of the endomembrane system.

Distinguish between the rough endoplasmic reticulum and the smooth endoplasmic reticulum.

Identify three important functions of the plasma membrane.

Tell why mitochondria and chloroplasts are called semi-autonomous organelles.

Discuss the evidence for the endosymbiosis theory.

Outline the structures and general functions of mitochondria and chloroplasts.

Explain how proteins are moved via vesicles through the endomembrane system.

If you are told about the function of a specific protein, tell where and in what type of cell that protein might be found.

Sketch and label a âtypicalâ animal cell and a real animal cell such as a red blood cell or a muscle cell. Tell how it might be different than the âtypicalâ cell in terms of its organelles and shape.

Sketch and label a âtypicalâ plant cell and a real plant cell such as a root or leaf cell. Tell how it might be different than the âtypicalâ cell in terms of its organelles and shape.

Describe the fluid-mosaic model of membrane structure. Tell why membranes are described as âfluid mosaicsâ.

Draw 10 phospholipid molecules as they would be arranged in a bilayer. Label the hydrophobic and hydrophilic parts.

61. Name all the places in a cell where membranes are found.

62. Describe at least three different categories of membrane proteins and tell what they do.

63. Describe what determines how fluid membranes are.

64. Explain how lipids are synthesized at the ER membrane.

65. Explain how transmembrane proteins are inserted into the ER membrane.

66. Compare and contrast diffusion, facilitated diffusion, passive transport, and active transport.

67. Explain the process of osmosis and how it affects cell structure.

68. Outline the functional differences between channels and transporters. Compare and contrast uniporters, symporters, and antiporters.

69. Explain the difference between primary active transport and secondary active transport.

70. Describe the structure and function of the sodium-potassium pump in animal cells and a similar pump in plants and prokaryotes.

71. Describe exocytosis and endocytosis and tell what molecules are moved across the membrane by these.

Discuss membrane transport, including its function and various forms and why all membranes have each form.

73. If a given cellular process is described, tell which form of transport might be involved.

List the different categories of animal tissue, providing general functions and specific examples of each.

Name the various organ systems found in many animals, list the components of each, and describe their general functions.

bluebeaver798

Human body can be described by many means â one of them â it is relatively big vessel with complex body fluid. For diagnostic purpose it is very complicated to detect insignificant number of biomarkers on very early stages of pathological process. This article, present pioneering method to initiate and conduct diagnostic by researching body fluids.

**With additional research provide additional examples of scientific way of dealing with solutions to improve functionality of human life. (QUESTION - This is exactly what is witten on my assignment)**

Analyzing human blood for a very low virus concentration or a sample of water for a bioterrorism agent has always been a time-consuming and difficult process. Researchers at the Georgia Institute of Technology and Emory University have developed an easier and faster method to detect these types of target molecules in liquid samples using highly porous, micron-sized, silica beads. The researchers developed a technique to simultaneously or sequentially add optical and magnetic nanoparticles into the beads. Adding magnetic nanoparticles allows the use of a magnetic field to attract and easily remove the beads from a liquid sample. âThese nanoparticles enter the pores of the microbeads so quickly and so completely -- essentially more than 99 percent of the nanoparticles go into the pores of the beads,â explained Shuming Nie, the head researcher on the project and the Wallace H. Coulter Distinguished Chair in Biomedical Engineering and director of Emory-Georgia Tech Nanotechnology Center. The beads are mixed in a liquid such as urine. Viruses, proteins or other biomarkers are captured on the bead surface. After the beads are removed from the liquid, optical imaging is used to determine the concentration of a specific protein or virus in the liquid sample based on the number of proteins or viruses attached to the surface of the beads. Tushar Sathe, a graduate student in the Wallace H. Coulter Department of Biomedical Engineering at Georgia Tech and Emory University, described the process of creating these novel beads and their clinical applications on Jan. 20 at SPIE Photonics West in San Jose, California. The work was also published in the Aug. 15 issue of Analytical Chemistry. The technology involves embedding fluorescent quantum dots and magnetic iron oxide nanoparticles inside the beads to create dual-modality magneto-optical beads. Nie and Sathe synthesize the quantum dots in different colors by varying their size, giving the beads a unique optical signature. Having different color beads allows the researchers to detect several target molecules at the same time in the same liquid sample. âWe use the quantum dots to create a set of beads that are unique and can be distinguished from each other. Itâs similar to bar-coding -- once you barcode the beads and put them in the urine or blood sample, you can remove them and decode what proteins or viruses have attached to individual beads based on their spectral signature,â explained Sathe. The process of creating these beads is quite simple, according to Sathe. The surface of the beads contains a long-chain carbon molecule that makes the beads hydrophobic, meaning they repel water. The beads are dissolved in butanol and washed several times. Then the beads are counted and optical and magnetic nanocrystals are added to the suspension either simultaneously or sequentially. After 15-20 minutes, the butanol is removed to get rid of any remaining nanoparticles that didnât get incorporated into the beads and the beads are washed with ethanol. Then the beads are coated with a polymer that creates a hydrophilic surface on the beads. This allows the beads to be functionalized by adding antibodies or DNA molecules to the surface that will capture the target molecules. These beads are dual-function -- both optical and magnetic -- but according to Sathe, more functions can be added to the beads. âAdding them is as easy as adding the nanoparticles into the solution. You just have to make sure the nanoparticle surface is hydrophobic so that it interacts with the beads,â said Sathe. The primary biomedical applications for this new technology will be to detect cancer and neurological diseases by identifying certain molecules present in human blood or urine that indicate specific diseases, according to Nie, who is also professor of biomedical engineering, chemistry, materials science & engineering, and hematology and oncology at Emory University and the Georgia Institute of Technology. âSome of the biomarkers for Alzheimerâs disease have very low concentrations in the blood so you need highly sensitive techniques that can find a specific molecule to diagnose this disease,â explained Nie. âOur technique could also be used to monitor therapeutic response. For example, if the viral level decreases in samples taken at later dates, then we know the drug is probably working.â This new technology allows the researchers to analyze very low concentrations of target molecules. âInstead of analyzing a liter of sample where the concentration could be very dilute and you might not see the target molecule youâre looking for, you can let the beads capture the molecules on their surface, remove them from the liquid, and then just measure the number of molecules attached to the beads,â said Nie. This ongoing research is funded by the National Cancer Institute, the Department of Energyâs Genomes to Life (GTL) Program, the Department of Defense and the Georgia Cancer Coalition, a public-private partnership established by the Georgia General Assembly in 2001.

Experiment 1: Paper Chromatography

I need all the data tables and questions filled out!

Chromatography is routinely used to separate components of a mixture. In this experiment, you will perform a paper chromatography procedure. The objective for this experiment is to determine the best solvent (ionic, polar covalent or non-polar covalent) for the dyes found in candy-coated chocolate pieces. The chromatography paper acts as the stationary phase for the procedure, and a variety of mobile phases (solvents) will be tested. Multiple tests with different eluting solvents must be run to determine the best eluting solvent to separate the food dyes. Some of the factors you will investigate include polarity and electrical charge (ionic characteristics).

Chromatography is based on two phases: the mobile phase and the stationary phase. The mobile phase is the phase which moves up the chromatography paper. This is also referred to as the eluting solvent, which the mixture of analytes is placed in.

The stationary phase is the material held in place for the chromatography procedure. Think of the mobile phase as a moving stream and the stationary phase as the stream bed. If you were to toss in a leaf, a stick, and a large rock, what would happen? Each different component would travel at different rates along the stationary phase, using the mobile phase as a vehicle. Many properties affect the affinity of a substance for the mobile or stationary phase, including polarity, solubility, particle size and electrical charge. Chemists can use their knowledge of these properties to separate a mixture effectively.

Materials

(3) 50 mL Beakers
1 Pipette
1 Stir Rod
10 mL Graduated Cylinder
100 mL Graduated Cylinder
(6) 5.5 x 9 cm. Pieces of Chromatography Paper
3 Capillary Tubes
600 mL Beaker
Ruler
*36 M&MsÂ® (12 Blue, 12 Green, and 12 Red)
30 mL of each of the following eluting solvents:
0.5% Sodium Chloride (Salt), NaCl solution

0.2% Sodium Chloride (Salt), NaCl solution
*Distilled Water (eluting solvent)
*70% Isopropyl Alcohol, C₃H₈O
*Create Your Own: Use your knowledge of eluting solvents to create two additional eluting solvents (30 mL each).
*Pencil
*20 mL 70% Isopropyl Alcohol, C₃H₈O

*Note: The individual candies have been repackaged by eScience Labs. Do not eat the candies.
*You must provide

Procedure:

1. Gather three 50 mL beakers, one for each color candy you will test.

2. Place two M&MsÂ® candies of one color into a beaker.

3. Repeat for each color of the candy you will test. You should have two green candies in one beaker, two red candies in a second beaker, and two blue candies in the third beaker.

Preparation of the Analyte

4. Use a pipette and the 10 mL graduated cylinder to add one mL of 70% isopropyl alcohol to each beaker.

5. Stir gently with a stir rod until the candy's white undercoating appears. Remove the candies. Be sure to rinse the stir rod every time you insert it into a new beaker.

6. Allow the solutions to sit and concentrate while stationary phase is prepared.

Preparation of Stationary Phase

7. Obtain a piece of chromatography paper that is approximately 5.5 cm wide and 9.0 cm long.

8. Using a pencil, mark the paper according to the sample provided in Figure 7 at the end of the procedure.

9. Using a capillary tube, place small spots of the analyte equally spaced along the marked line. Since there are three colors to be tested, there will be three spots on the line (use one capillary tube per color; save the tubes for the additional trials).

Note: Capillary tubes are extremely thin tubes. They are useful when working with very small amounts of a sample, and collect liquid samples through capillary action. To use the capillary tube, simply place the open end of the tube in the sample. The liquid molecules will be drawn into the tube and stick to the inner walls. Figure 6 provides a references for this process.

Figure 6: Capillary tubes use capillary action to pull up liquid.

10. Allow the spot to dry, and re-spot the analyte in the exact same area as done in Step 9. Repeat this process at least five times, or until the colored dots appear distinct on the paper.

11. Pour the deionized water (your eluting solvent) into the 600 mL beaker until it has reached a height of approximately 0.5 cm. This will take approximately 20 - 30 mL.

12. Place the paper (line-side down) into the 600 mL beaker with the eluting solvent for 3 - 5 minutes. Your initial line should be above the solvent. When complete, the original spots near the bottom of the paper should be dissolved (as the colors traveled up the solvent front).

13. Mark the edge of the solvent front (the edge of the mobile phase) and the location of the analytes with a pencil (see Figure 7 for reference). Record your data and any additional observations in Table 1.

Note: Some M&MsÂ® colors may have more than one spot. The distance travelled by each spot should be measured and recorded.

14. Repeat the procedure five more times, incorporating one of the remaining eluting solvents (0.5% NaCl, 0.2% NaCl, 70% isopropyl alcohol, and the two solvents that you create) each time.

Figure 7: Sample paper chromatography results.

Table 1: Experiment 1 Variables
Solvent	Distance Traveled by Mobile Phase (mm)	Distance Traveled by Each Analyte (mm)	Additional Observations
1. Distilled Water		Green: Blue: Red:
2. 0.5% NaCl Solution		Green: Blue: Red:
3. 0.2% NaCl Solution		Green: Blue: Red:
4. 70% Isopropyl Alcohol		Green: Blue: Red:
5. Student Creation:		Green: Blue: Red:
6. Student Creation		Green: Blue: Red:

Experiment 2: Slime Time

Although you may not realize it, the inks which are used in writing utensils are chemical solutions which include different molecules. Some inks are polar, while others are non-polar. A polar solvent will attract polar inks, while a non-polar solvent will attract non-polar inks. In this experiment, you will use inks to identify slime and silly putty as polar or non-polar. You will also use paper chromatography to verify the inks are correctly identified as polar or non-polar.

Materials

(1) 250 mL Beaker
5 mL 4% Borax Solution, Na₂B₄O₇.10H₂O
Dry Erase Marker
(1) 10 mL Graduated Cylinder
(1) 100 mL Graduated Cylinder
Filter Paper (Disk)
Filter Paper (Rectangular)
0.5 g Guar Gum
Highlighter
Permanent Marker

1 Popsicle Stick
Silly PuttyÂ®
Ruler
Stir Rod
Uni-ballÂ® Roller Pen
*Distilled or Tap Water
*Newspaper
*Notebook Paper
*Scissors

*You must provide

Procedure:

Part 1: Making Slime

1. Transfer the 0.5 g of guar gum into an empty 250 mL beaker.

2. Use the 100 mL graduated cylinder to measure and pour 50.0 mL of distilled water into the 250 mL beaker with the guar gum.

3. Use the stir rod to thoroughly mix the solution.

Note: It may take a few minutes to fully dissolve the guar gum in the water.

4. Use the 10 mL graduated cylinder to measure and pour four mL of the 4% borax solution into the 250 mL beaker with the guar gum solution.

5. Use the stir rod to stir the solution until it forms a slime. This will take a few minutes. If the solution remains too runny, add an additional one mL of the 4% borax solution. Continue to stir until the solution is the right consistency.

6. Once you are satisfied with the slime's consistency, use the popsicle stick to carefully transfer it from the beaker into your hands. Be sure not to drop any of it on to the floor!

7. Manipulate the slime in your hands. When you are done, write down observations about how slime pours, stretches, breaks, feels, etc. in the Data: Part 1 section at the end of the procedure.
Caution: Slime is slippery and if dropped it can make the work area slick.

8. Transfer the slime back into the beaker and wash your hands.

Part 2: Slime and Putty Ink Tests

1. On a piece of notebook paper make one, 20 - 25 mm long mark of each of the inks you are testing. Space the marks at least one inch apart. Use a pencil to label each mark with the name of the ink source.

a. Water soluble inks include those in highlighters and certain pens.

b. Water insoluble inks include those in a permanent pen/markers, newsprint, and a Dry Erase markers.

2. While the inks are drying, select a passage or a picture in the newspaper to test with the slime.

3. Break off a small piece that is 3 - 5 cm in diameter of slime. Gently place this piece on top of the newspaper print, then carefully pick it up again.

4. Observe and record in Table 2 whether or not the ink was picked up onto the slime.

5. Break off another small piece of slime. Once the inks from Step 1 have dried, gently place the slime on top of the first spot on the notebook paper, then carefully pick it up.

6. Repeat Step 5 for each of the inks. Observe and record which inks were picked up (dissolved) by the slime in Table 2.

7. Repeat Step 6 ink testing two more times for accuracy.

8. Before performing ink tests on Silly PuttyÂ®, in the Data: Part 2 section hypothesize which inks the silly putty will pick up.

9. Perform ink tests on Silly PuttyÂ® in the same manner as above. Record your results in Table 2.

Part 3: Chromatography of Ink Samples

1. Use a pencil or scissors to poke a small hole in the center of a piece of filter paper disk (see Figure 8).

Figure 8: Chromatography apparatus for Procedure Part 3.

2. Use a rule to spot the filter paper with the two soluble ink sources, and the two insoluble ink sources used in Part 2 (four total). Each spot should be approximately two cm from the center hole, and should be evenly positioned around the circumference of the hole.

3. Cut the rectangular piece of filter paper in half. Fold the paper in half (length-wise) several times to create a narrow wick.

4. Insert the wick into the hole of the filter paper disk so that it the top of the wick is approximately two cm from the disk.

5. Fill a 250 mL beaker ³/₄ full with water (between 100 and 150 mL of water).

6. Set the filter paper disk on top of the beaker so that the bottom of the wick is submerged in the water. The disk should extend passed the circumference of the beaker with the spotted side facing up.

7. Allow water to travel up the wick until it is approximately one cm from filter paper disk. Remove the filter paper set-up from the beaker.

8. Observe which inks moved from where they were originally spotted. Record your observations in the Data: Part 3 section at the end of the procedure.

Data

Part 1

â¢ Slime Observations:

Part 2

â¢ Hypothesis for Silly PuttyÂ® (Procedure Part 2, Step 7) :

Part 3

â¢ Observations of inks following chromatography:

Table 2: Results of Ink Testing for Silly PuttyÂ®
Name of Ink	Picked up (dissolved)	Did not pick up
Name of Ink	Test 1	Test 2	Test 3	Test 1	Test 2	Test 3
Newsprint
Highlighter
Uni-ballÂ® Roller Pen
SharpieÂ® Marker
Dry Erase Marker

Post-Lab Question

1. Did the slime pick up water soluble or water insoluble inks in Part 2? From these results, what can you conclude about the polarity of slime molecules?

2. Explain how you determined your hypothesis about whether or not Silly PuttyÂ® would pick up water soluble inks. What scientific information did you incorporate to formulate the hypothesis? Was your hypothesis correct?

3. Were the inks you used properly classified as soluble and insoluble? Explain your answer.

BIOSC-101 Lecture Notes - Lecture 3: Chemical Energy, Surface Tension, Organic Compound

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