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Week 2 notes

by: Vanessa Notetaker

Week 2 notes BSC 2010

Vanessa Notetaker
GPA 3.55

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These notes cover material from week 2
Biology 1
Dr. George Bates
Class Notes
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This 6 page Class Notes was uploaded by Vanessa Notetaker on Saturday January 23, 2016. The Class Notes belongs to BSC 2010 at Florida State University taught by Dr. George Bates in Winter 2016. Since its upload, it has received 16 views. For similar materials see Biology 1 in Biology at Florida State University.

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Date Created: 01/23/16
WEEK 2 NOTES Macromolecules  Carbohydrates  Proteins  Nucleic acids Polymer  Long molecule consisting of many similar identical building blocks held together by Covalent bonds Monomers  Building blocks of polymers o Can have a function of their own Enzymes  Specialized macromolecules  Speed up chemical reactions Dehydration reaction  When monomers are connected via covalent bonds with the loss of a water molecule A polymer is created when a monomer is linked with another monomer via a covalent bond. When a covalent bond is created, a dehydration reaction occurs, which is the loss of a water molecule. A water molecule is made up of OH- and H+. One monomer will provide the OH- and the other will provide an H-. When this reaction continues, more and more monomers are bonded via covalent bonds and this creates a polymer. Hydrolysis  How polymers are unassociated with monomers  Reverse of dehydration reaction  Bond is broken by an addition of a water molecule Carbohydrates  Sugars and polymers of sugar  Monosaccharides o Classified as:  Aldose – Carbonyl group at the end of a carbon skeleton  Ketose – Carbonyl group within the carbon skeleton  Hexose – sugars that have six carbons (same for trioses and pentoses)  Depends on the structure of the carbon skeleton as well.  In aqueous solutions, rings are formed  Disaccharide o Two monosaccharides joined by a glycosidic linkage – a covalent bond between two monosaccharides by a dehydration reaction  Polysaccharides o Polymers with many monosaccharides joined by glycosidic linkages o Provide sugar for cells o Building material for structures that protect the organism  Glycogen – polymer of glucose that acts as a sugar in the body that must be replenished by eating carbohydrates  Cellulose – the tough walls that enclose plant cells  Chitin – used by arthropods to builds their exoskeleton Fat  Constructed from glycerol and fatty acids o Glycerol is an alcohol; each of its three carbons bear a hydroxyl group (Hydroxyl group are the component in alcohol) Fatty acid  Has a long carbon skeleton  One end of the carbon skeleton has a carboxyl group (carboxyl is an ACID, thus the name “fatty acid”  The other end has hydrocarbon chains (which is why it is hydrophobic, the hydrogen molecules will hydrogen bond to each other and exclude the fat) Triacylglycerol  A lipid consisting of three fatty acids linked to one glycerol molecule (a fat) The molecular building blocks of fat are one molecule of glycerol and three molecules of fatty acids. One water molecule is removed from each fatty acid and then joined to the glycerol. Another name for fat is triglyceride. Saturated fatty acid  Fatty acid where each carbon in the hydrocarbon tail are connected by single bonds. This will maximize the number of hydrogen atoms in the carbon skeleton Unsaturated fatty acid  Has one or more double bonds between carbons in the hydrocarbon tail. This will reduce the amount of hydrogen atoms in the carbon skeleton.  Usually all of the double bonds in fatty acids are cis double bonds Trans isomer – opposite sides of double bond Cis isomer – locked on the same side of the double bond Animal fats are usually saturated and their lack of double bonds allows the fats to be flexible which allows them to pack tightly together. Solid. Plants and fish fats are unsaturated and the cis double bonds cause kinks which prevent them from packing tightly together. Liquid. Trans fats  Unsaturated fats that has been formed artificially by adding hydrogen to break the cis double bonds that contains one or more trans double bonds. Phospholipid  Made up of glycerol joined to two fatty acids and a phosphate group  The hydrocarbon chains are nonpolar (hydrophobic)  The rest of the molecule is polar (hydrophilic)  They form the bilayers that function as biological membranes  Composed of a hydrophilic (polar) head and two hydrophobic (nonpolar) tails Steroids  A lipid that has a carbon skeleton consisting of four fused rings with different chemical groups attached Cholesterol  A type of steroid  A precursor molecule for the synthesis of many different human hormones Enzymatic proteins  Regulate metabolism o Catalyst – increases the rate of the reaction Proteins are all constructed of the same 20 amino acids, linked in unbranched polymers. Polypeptide  A polymer of many amino acids linked by a peptide bond o Peptide bond – bond between amino acids o Has a structure ending in an amino group, N, and a carboxyl group, C Proteins are made up of one or more polypeptides. Amino acid  An organic molecule with an amino group and a carboxyl group.  alpha (a) carbon – at the center of an amino acid  The R group differs with each amino acid and is also known as the side chain. O-H Hydroxyl group (alcohol component) O=C Carbonyl group COOH Carboxyl group H-N-H Amino group S-H Sulfhydryl group NONPOLAR – HYDROPHOBIC (same) POLAR – HYDROPHILIC (different) Acidic amino acids have a carboxyl group and are negative in charge. Basic amino acids are positive in charge. Peptide bond  A covalent bond between the carboxyl group on one amino acid and the amino group on another by a dehydration reaction Primary structure of protein  Sequence of amino acids (linear chain of amino acids)  Determined by inherited genetic information Secondary structure  Repetitive coiling or folding of the polypeptide backbone (not the chains) of a protein  Due to hydrogen bonding o a helix – a coil held together by hydrogen bonding between every fourth amino acid o B bleated sheet – folds back and forth, two regions lie parallel to each other and are held together by hydrogen bonds (on the polypeptide backbone, not the side chains) Tertiary structure  Overall shape due to the interactions of amino acid side chains  One type of interaction: o Hydrophobic interaction – a type of weak chemical reaction caused when molecules that do not mix with water coalesce (one mass or whole) to exclude water o Disulfide bridges – sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer Quaternary structure  Association of two or more polypeptides Sickle-cell disease  Changed red blood cell shape Denaturation  Protein loses its native shape due to disruption of weak chemical bonds  Occurs under extreme conditions of pH, salt concentration, or temperature Chaperonins  Assist in proper folding of other proteins X-ray crystallography  Determines the 3D structure of many other proteins. Gene  A certain sequencing of DNA Nucleic acids  Polymer consisting of many nucleotide monomers  Blueprint for proteins o DNA o RNA Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA) Gene expression  DNA directs the synthesis of proteins, RNAs Each gene along a DNA molecule directs synthesis of a type of RNA called messenger RNA (mRNA) mRNA interacts with the cell’s protein-synthesizing machinery to direct production of a polypeptide DNA  RNA  protein Polynucleotides  A polymer that has many nucleotide monomers in a chain, DNA or RNA Nucleotides  Building block of nucleic acid  Has five-carbon sugar covalently bonded to a nitrogenous base and one or more phosphate groups Pyrimidine  One of two nitrogenous bases found in nucleotides  6 membered ring  Cytosine (C ), Thymine (T), uracil (U) Purines  One of two nitrogenous bases found in nucleotides  6 member ring fused to a 5 membered ring  Adenine (A), guanine (G) DNA and RNA: adenine, guanine, cytosine DNA: Thymine RNA: Uracil Deoxyribose  DNAs sugar  Lacks an oxygen on the second carbon ring Ribose  RNAs sugar


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