| | | A) | endoplastic reticulum | | | B) | microtubules | | | C) | cytoplasm | | | D) | mitochondria | | | | | | Feedback: The cell's chemical processes take place in a semifluid material called the cytoplasm. This material provides an ideal environment for organelles because of its fluidity. | | 7 CORRECT | | This shows an example of endoplasmic reticulum. What is the significance of its structure? | | | A) | provides a location for DNA production | | | B) | helps decrease surface area | | | C) | allows selective permeability of cell membrane | | | D) | facilitates breakdown of chemical bonds | | | | | | Feedback: The pleats and folds of the endoplasmic reticulum provides a large surface area where cellular functions, such as breaking chemical bonds, can take place.
They are attached through myristoylation, palmitoylation, or isoprenylation. What are the lipid rafts? How do they form and what is their function? A lipid raft is a membrane domain which is enriched in sphingolipids and cholesterol (liquid ordered phase). Rafts are postulated to grow by accumulation of cholesterol, sphingolipids, and GPI-anchored proteins.
Your answer: The precipitin line occurs when the antigen and antibody are in optimal proportions and cross-linking occurs forming an insoluble precipitate. 3. Did you think human serum albumin and bovine serum albumin would have epitopes in common? How well did the results compare with your prediction? Your answer: yes;results showed they have partial identity Activity 3: Indirect Enzyme-Linked Immunosorbent Assay (ELISA) Lab Report 1.
Kirstie Javier AP Biology Period 4 November 14, 2011 Proteins Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. Some types of chemical bonds/ interactions are disulfide bonds, hydrogen bonds, ionic bonds, and hydrophobic interactions. Disulfide bonds form when two cytosine molecules join together to form a bond between their two sulfur atoms. Such bonds cross-link polypeptide chains or parts of chains. Because they are nonpolar covalent bonds, they are very strong bonds and not easily broken.
When the chromatin is dispersed and not readily stainable, it is known as euchromatin. Euchromatin is prevalent in cells that are active in the transcription of many of their genes while heterochromatin is most abundant in cells that are less active or not active. The nucleus often contains one or more nucleoli that are spherical or oval bodies composed chiefly of ribonucleoproteins. Nucleoli are usually stained with basic dyes because of their high RNA content and are generally larger in cells that are actively participating in protein synthesis. The endoplasmic reticulum (ER) is a system of interconnected membranous sacs, channels, or cisternae in the cytoplasm.
Analyze the polarity of the different regions of a phospholipid molecule. Use the model of the phospholipid to describe the structure of the cell membrane. How do water, phospholipids, and proteins interact to produce the cell membrane? * Analyze the polarity and water-solubility of the different regions of the globular protein floating in the phospholipid bilayer membrane shown below. The protein molecule is able to float in the membrane – part of it is embedded in the membrane, part of it sticks into the cytoplasm, and part of it sticks out into the aqueous environment of the cell.
This technique is highly used on DNA, RNA, and proteins. This technique is all taken place in a gel electrophoresis chamber. The chamber includes a buffer solution, an Agarose gel, a cathode end, and an anode end. The cathode end of the chamber is negatively charged and will attract molecules that have a positive charge, while the anode end is positively charged and will attract molecules that are negatively charged. The buffer solution is used to keep the pH of the experiment at a constant number while carrying ions that are essential to hold a current.
Out of all the acids that passed through, only one was found to be toxic. By using high performance liquid chromatography, a polar and nonpolar stationary phase that contained the toxin was mixed, and this isolated the toxin by itself. To ensure that that was the isolated toxin, they further broke it down to find its charge, size, and molecular shape. Mass spectrometry was then used to find the weight and formula of the toxin. By finding the formula, it had similar characteristics to an amino acid known as domoic acid.
BIO 5 June 12 essay 10a The importance of shapes fitting together in cells and organisms Plan- • Enzymes - lock and key model, induced fit, specific complementary shapes, digestion of lactose, restriction enzyme in DNA • RuBP binding with CO2 in light dependent reaction of photosynthesis • Muscles - contraction, sliding filament theory • Blood and oxygen - inhibitors blood glucose receptors on cell surface membrane Essay- There are numerous examples of of the importance of shapes fitting together in cells and organisms. For example ; within enzymes, DNA, photosynthesis, muscle contraction, and receptors. Enzymes are used in every aspect of biology to catalysts a reaction. As they bind to substrate molecules which have a specific complementary shape to the enzyme, to form enzyme-substrate complexes and finally the enzyme and the product. There are many models of enzymes, such as the lock and key model, which explores the structure of the enzyme and its ability to bind with a substrate molecule which is specific and complementary.
Experiment 14: Proteins and Denaturing Agents (adapted with permission of Dr. Ann Willbrand, USC-Aiken) Introduction Proteins are polymers of amino acids. A typical protein may be composed of hundreds of amino acids. The side chains of the amino acid residues may contain nonpolar, neutral polar, acidic, or basic groups. The primary structure of a protein is determined by the sequence of amino acids, but the secondary and tertiary structures of proteins define their natural or native states, which are often folded. This is called the native conformation and is usually the state in which the protein is most active and functional.