What are the most common elements in living things? (Top 8)
Give 2 examples of trace elements and what they are used for.
The dietary elements or essential trace elements are those that are required to perform vital metabolic activities in organisms. Examples of essential trace elements in animals include Fe (hemoglobin), Cu (respiratory pigments), Co (Vitamin B12), Mn and Z
Briefly describe atomic number, atomic mass, ions & isotopes
- atomic number: the number of protons in an atom
- atomic mass: the average mass of an atom, taking into account all its naturally occurring isotopes
- ion: an atom or molecule with a net electric charge due to the loss or gain of one or more electrons
Explain the difference between nonpolar and polar covalent bonds.
Nonpolar covalent bonds are a type of chemical bond where two atoms share a pair of electrons with each other. Polar covalent bonding is a type of chemical bond where a pair of electrons is unequally shared between two atoms.
How are hydrogen bonds formed and how are they different from covalent and ionic bonds?
In a covalent bond, two atoms share one or more electrons. Water is a polar molecule. A hydrogen bond is a relatively weak bond between two oppositely partially charged sides of two or more molecules. ... In an ionic bond, an atom gives away one or more e
Give an example of how the shape of a molecule fits its function. (Don't use endorphins - come up with another one)
List the functional groups and draw their structure
List and briefly describe the 7 properties of water that result from its polarity.
Explain the difference between acids and bases in terms of ion concentration and pH
Acids are substances that, when dissolved in water, increase the concentration of H+ ions (that is, positive hydrogen ions, or protons). Bases are substances that, when dissolved in water, increase the concentration of OH- ions (also known as hydroxide io
What is the role of buffers in human body systems? Give an example.
Buffers help maintain the pH of the blood and other fluids within a narrow range�between pH 7.35 and 7.45. A buffer is a substance that prevents a radical change in fluid pH by absorbing excess hydrogen or hydroxyl ions.
List the four families of organic compounds. For each family, list the following information:
- Functional groups
- Name of bond between monomers
- carbs: monosaccharide- fats: fatty acids & glycerol- proteins: amino acids- nucleic acid: nucleotides
What is the formula for all monosaccharides?
What indicators are used to detect the presence of sugars and starches? What changes are seen in positive tests?
serve as energy for organisms
Describe the 3 types of lipids and their characteristic structures.
- fats- phospholipids- steroids- waxes & oils
Explain each of the levels of protein structure.
The different levels of protein structure are known as primary, secondary, tertiary, and quaternary structure.
- Primary: the sequence of amino acids that make up a polypeptide chain.
- Secondary: the three dimensional form of local segments of proteins.
Compare and contrast the following terms:
- Dehydration synthesis
- Dehydration synthesis:
Write the 2 laws of thermodynamics.
- energy cannot be created or destroyed; the total quantity of energy in the universe stays the same
- the quality of energy. It states that as energy is transferred or transformed, more and more of it is wasted
How could you recognize a molecule of ATP?
- adenosine tri phosphate� energy molecules used to power cellular work� adenine, ribose sugar & 3 phosphate group causes release of free energy� renewable molecule generated by addition of phosphate group ADP (phosphorylation)
What is the function of enzymes? What types of things affect their function?
- Enzymes are biological molecules (typically proteins) that significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They are vital for life and serve a wide range of important functions in the body, such a
Explain the concept of denaturation in terms of level of structure of a protein.
Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains
What is the difference between competitive and noncompetitive inhibition?
The competitive inhibitor binds to the active site and prevents the substrate from binding there. The noncompetitive inhibitor binds to a different site on the enzyme; it doesn't block substrate binding, but it causes other changes in the enzyme so that i
Explain the function or role of the each of the following from the enzyme lab:
- Hydrogen peroxide
- Potassium permanganate
- Sulfuric acid
- Hydrogen peroxide:
- Potassium permanganate:
- Sulfuric acid: