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Terms in this set (30)
Describe the properties of Carbon- how many bonds can it form? What types of bonds can it form? What shape structures can it form?
Forms 4 covalent bonds with other atoms. The bonds can be single, double, or triple bonds. Carbon bonds can occur in configurations that are linear, ring-like, or highly branched. Can form polar or non-polar bonds
Define an Organic molecule
Most contain carbon, Most contain carbon-carbon or carbon-hydrogen bonds
Distinguish between condensation, dehydration, and hydrolysis reactions
Dehydration- A water molecule is released when the monomers are linked together (polymers are broken into monomers by the addition of water)
Hydrolysis- Water molecule is used to break, or lyse, the linkage that holds monomers together.
Condensation- 2 or more molecules combine
Describe the properties of Carbohydrates and Lipids
Simple carbohydrates are broken down to make ATP, which is used as a source of energy. Larger carbohydrates store energy or may play structural roles. Some carbohydrates function as molecular tags, allowing recognition of specific cells and molecules.
Lipids are non polar molecules that are primarily composed of carbon and hydrogen, with some oxygen. They are a key part of cell membranes and function as hormones in energy storage. They act as insulators and shock absorbers.
Identify which functional groups are found in carbohydrates and lipids
Carbohydrates: Monosaccharides, Disaccharides, Polysaccharides, Cellulose, Glycosaminoglycans
Lipids: Triglycerides (fats and oils), phospholipids, Steroids, and waxes
Define an isomer.
Molecules with identical formulas but different structures
Identify the type of bond formed when a disaccharide is formed
The linkage of monosaccharides by dehydration reaction. The linking involves the removal of an -OH group from one monosaccharide and a hydrogen atom from the other, giving rise to a molecule of H2O and covalently bonding the two sugars together through an oxygen atom. This bond is called a glycosidic bond
Relate the functions of plant and animal polysaccharides to their structure. (think about branching)
Starch and glycogen are used to store energy in cells. The high degree of branching in glycogen contributes to the many hydrophilic groups. Starch is less branched making it less soluble. Cellulose, peptidoglycan, chitin and glycosaminoglycans play a structural rather than energy-storing role. Cellulose has a linear arrangement that allows vast numbers of hydrogen bonds to form between cellulose molecules which stack together in sheets & provides great strength. Peptidglycans are found in cell walls of certain bacteria, and are arranged in lattice-like arrangement that gives strength and rigidity to the cell. Chitin is tough, structural polysaccharide. Glycosaminoglycans are found in cartilage and abundant in in the extracellular matrix. The nitrogen in these polysaccharides allows for additional hydrogen bonding leading to more strength.
Describe how lipids play a role in membranes, energy storage and signaling
Many phospholipids create a bilayer on the cell membrane. Steroids typically serve as a precursor for the synthesis of steroid hormones. The hydrolysis of of triglycerides releases their fatty acids, which can be metabolized to provide energy to make ATP.
List the different types of lipid molecules important for living organisms.
Triglycerides- important for storing energy (creates an ATP when it gets hydrolisized)
Phospholipids- critical for determining the structure of cell membranes
Steroids- Contributes to membrane structure and function & serves as a precursor for the synthesis of steroid hormones.
Waxes- exclude water, providing a barrier to water loss, can also serve as structural elements.
Explain why some fats are solid at room temperature and others are liquid
Unsaturated fats are liquids are room temperature and typically have a low melting point. Saturated fatty acids can pack together more tightly because they don't have any kinks in their hydro-carbon tails. As a result, it takes a greater amount of energy to melt them.
Diagram the structure of a triglyceride and explain how it is formed and how its structure is affected by the presence of saturated and unsaturated fatty acids
Consists of a glycerol molecule linked to three fatty acids. Saturated fatty acids- those in which all of the carbons in the hydrocarbon chain form single bonds. Monounsaturated- contain one C-C double bond. Polyunsaturated fatty acids- Contain two or more C-C double bonds.
Explain why phospholipids form a bilayer when dissolved in water
Their polar heads interact with the H20 molecules and their non polar tails facing the interior , where they avoid contact with water.
Describe the chemical structure of steroids and give an example of their biological importance.
Four fused rings of carbon atoms form the general structure of all steroids. Steroids with an -OH attached are called sterols, and they are found in fungi, plants and animals. Ex. Cholesterol- found in the cell membranes of animals where it contributes to membrane structure and function, also serves as a precursor for the synthesis of steroid hormones. The steroid hormones are necessary for animal reproduction.
What type of organic molecules are waxes? Identify 2 different functions of waxes.
Waxes are a type of lipid. Most waxes are very non-polar so they exclude water, providing a barrier to water loss. Some waxes may also be used for structural elements.
Know what the monomers that make up a polypeptide chain are and how they are linked together
They are linked together in a dehydration reaction that forms a covalent link = peptide. Polypeptides have a N-terminus and a C-terminus (another amino acid would be added here). When they are linked together the N-terminus has a free amino group and has a nitrogen atom. The C-terminus aka the carboxyl end has a carbon atom. Amino acids are joined together by linking the carboxyl group of one amino acid to the amino group of another.
Be able to draw the common core structure that all amino acids share and be able to identify the chemical groups in that structure.
All amino acids contain a carbon atom, that is linked toa an amino group (NH2) and a carboxyl group (COOH). The carbon is also linked to a hydrogen atom and a side chain which is known as the R group.
Know what is meant by the "R" group in a protein
The "R" group is the side chain of the amino acid. The varying structures of "R" group gives amino acid its characteristics.
Given the chemical structure of two amino acids, be able to draw the structure of the dipeptide produced when a peptide bond is formed between them
*Look in textbook
Be able to describe the levels of structure of a protein (primary, secondary, tertiary, and quaternary).
Primary- Sequence of amino acids
Secondary- Certain sequences of amino acids form hydrogen bonds that cause the region to fold into a spiral (Helix) or sheet (Pleated sheet)
Tertiary- polypeptide folds and refolds upon itself to assume a complex 3-D shape. Secondary and random coiled regions fold.
Quaternary- 2 or more polypeptides bond to each other to form a functional protein.
Be able to describe how hydrogen bond formation establishes secondary structure in proteins. Know the two common secondary structural elements seen in many proteins
For the helix, the hydrogen linked to a nitrogen atoms forms a hydrogen bond with an oxygen atom , which in turn is double bonded to a carbon atom. These hydrogen bonds occur at regular intervals along the polypeptide backbone and cause the backbone to twist into a helix. In a B pleated sheet, Hydrogen bonds between a hydrogen linked to a nitrogen atom and a double-bonded oxygen form between theses adjacent, parallel regions. When this occurs, the polypeptide back-bone adopts a repeating zigzag, or pleated, shape.
Know what a disulfide bond is and why they can be important for protein structure
A disulfide is a type of covalent linkage, occurs when both cysteines react
Know what a protein domain is and why a domain type can be found in more than one protein
Functional domains: Independently folded regions of a protein that performs a characteristic function. They usually have the same function across different proteins. The domains have been duplicated during evolution, so the same kind of domain is found in many different proteins.
Be able to recognize the three main parts of a nucleotide (Phosphate group, base, sugar)
*Look in text book
Sugar- five carbon hexagon
Bases- 1 or 2 fused rings
Know the differences between nucleotides found in DNA and RNA
DNA-store genetic info for long term, resides in the cell, copied and passed on from one cell generation to the next, contains regions called genes which encode proteins.
RNA- involved in decoding this information into instructions for linking a specific sequence of amino acids to form a polypeptide.
Know the numbering system for the carbons in the sugar of a nucleotide
Starts from the first right on the ring to the 5th being on the phosphate group.
Be able to describe how nucleotides are linked together to form a nucleic acid
The phosphate groups link the 3' carbon of one nucleotide to the 5' carbon on the next. The linkages between sugars and phosphates form the backbone of a DNA or RNA strand with the bases projecting from the backbone.
Know what is meant by the 5' and 3' ends of a nucleic acid strand
The 3' carbon of one nucleotide is linked to the 5' carbon of the next nucleotide via a phosphate group
Know how the bases of DNA strands associate to form a double-stranded structure. Know what bases pair with each other.
The two strands are held together by hydrogen bonds between a purine base in one strand and a pyrimidine base in the opposite strand. In DNA, an A in one strand is always paired with a T in another strand, and G is paired with a C. For RNA (single stranded), A pairs with U and G pairs with C.
Know what is meant when we say that the two strands in the DNA double-helix are "antiparallel"
DNA strands are antiparallel 5' to 3' and run in opposite ways.
Recommended textbook explanations
Lehninger Principles of Biochemistry
David L Nelson, Michael M. Cox
Campbell Biology (AP Edition)
Cain, Campbell, Minorsky, Reece, Urry, Wasserman
Campbell Biology (AP Edition)
Cain, Jackson, Minorsky, Reece, Urry, Wasserman
Miller and Levine Biology
Joseph S. Levine, Kenneth R. Miller
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