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University of Toronto Scarborough
Biological Sciences
Aarti Ashok

Cell Bio Lec 2 Slide 5: Most biological chemicals made of C-C bonds. Ethylene is one such example, and is used for fruit ripening. Slide 7: the oxygen in water is the electronegative atom. Other examples include N, S, P. Macromolecules can have different properties depending on the groups at each end. Covalent bonds are strong, while noncovalent bonds are weak. Ionic bond: Interaction between two different types of macromolecules. ex: DNA- negative from the sugar phosphate backbone, protein- positive from amino acid (argenine) the rungs of the DNA are bound by H-bonds Slide 17: Hydrophobic- nonpolar molecules are strongly attracted to each other when they are surrounded by polar water. Slide 18: Van der Waal: temporary discharges; weak. But they are strong when there are multiple bonds of them. Table 2.2: Functional Groups. The more polar the molecules, the more soluble they are in water (water= polar) Slide 26: Carbohydrate: Cell walls and membranes are made up of them, and they are also used for storage. Organelles are widely distributed in the cell, except for the nucleus. The position of the C=O bonds in a carbohydrate determines what it’s called. This is a ketose (C=O within body)  fructose This is an aldehyde (C=O at the end)  glucose Slide 27: Make sure you know the difference between glucose alpha and beta Slide 29: ‘Oligo’= a few. Oligosaccharide are added to another protein/lipid to determine their function Slide 31: Starch: polymer of alpha glucose Slide 32: Cotton and ligning are made of cellulose. Slide 33: Chitin- has acytil amino groups instead of OH groups (picture) Slide 36: Lipid : nonpolar biomolecule, so it’s not soluble. Fatty Acid Made of carboxyl groups A glycerol and three fatty acids Slide 37: Unsaturated fatty acid (C=C) have distorted molecules, because of the break (see picture to the right) , and they can therefore not stack on top of another properly.  liquid Slide 38: Adipocyte- source of chemical energy, but can also add up Slide 39: Steroids have a ring structure and are built to chemical messengers (hormones) Slide 40: Phospholipid= (phosphate and polar head group)+ glycerol+ two fatty acids The fatty acid chains are hydrophobic and the head is hydrophilic ampiphatic Slide 43: RNA are used for protein synthesis, gene regulation, and are genes of some viruses Slide 44: The nucleotide are composed of sugar, a nitrogenous base, and a phosphate. RNA has a ribose sugar, while DNA has a deoxyribose sugar. The nucleotides are linked together by phosphodiester bonds that move from 3’ to 5’. PAY ATTENTION TO THE DIRECTION! Slide 46: Purines (two H-bonds): guanine, adenine. Pyrimidine (three H-bonds): cytosine, thymine, uracil Slide 48: The DNA sequences run antiparallel (one side 3’5’, other side 5’3’), so that the bases can bind accordingly. Slide 50: Everything in the cell is run by proteins (enzymes, hormones, signals, etc.) We have 20 amino acid types and many carboxyl groups. It is the R side chains that differentiate the a.a. (Fig 22.4) R-GROUPS 1) Polar charged – Histidine can be polar charged depending on the environment. Arginine coils around and interacts with the negative charged backbone of DNA by using its positive charge. 2) Polar uncharged- H-bonds 3) Nonpolar- hydrophobic, ring structure 4) Other- unique properties. Glycine- smallest R group. Used for protein groups to interact in close contact. Proline- usually nonpolar, but kinks when added with a protein and then interferes with other secondary structures. Cysteine- disulfide bond between two cysteines (Slide 57) Slide 58: peptide bond- bond that keeps amino groups together. There is a nitrogen terminus and the end is carbon. Slide 60: Primary structure is the simple amino acid sequence. There are 20 types, but they can be continuous with infinite amount of sequences (n). The structure defines its property, so when the structure changes, its function changes as well. (ex sickle cells slide 61) Slide 63: enzyme is unfolded when a denaturing agent is added (ex. Urea), but when the agent is removed, the protein naturally defolds and returns to its original state Slide 64: Co-translational- as the protein synthesizes, it al
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