This document summarizes key concepts from chapters 2 and 4 of a chemistry textbook. It discusses the basic elements that make up living things, types of chemical bonds, properties of water, acids and bases. It also covers carbon-based molecules like carbohydrates, proteins, lipids and nucleic acids. These molecules have diverse structures that allow them to perform important functions in living organisms. The document also defines several important chemistry terms.
This document summarizes key concepts from chapters 2 and 4 of a chemistry textbook. It discusses the basic elements that make up living things, types of chemical bonds, properties of water, acids and bases. It also covers carbon-based molecules like carbohydrates, proteins, lipids and nucleic acids. These molecules have diverse structures that allow them to perform important functions in living organisms. The document also defines several important chemistry terms.
This document summarizes key concepts from chapters 2 and 4 of a chemistry textbook. It discusses the basic elements that make up living things, types of chemical bonds, properties of water, acids and bases. It also covers carbon-based molecules like carbohydrates, proteins, lipids and nucleic acids. These molecules have diverse structures that allow them to perform important functions in living organisms. The document also defines several important chemistry terms.
Electrons o PE directly related to distance from nucleus o Lowest state of PE Strong bonds o Covalent - EN o Dry ionic - complete transfer of electrons Weak bonds - reversible, 3D protein shape o H-bond - b/t partially positive H and negative EN atom o Van der Waals - changing regions of +/- Unequal sharing of electrons in H2O leads to polar bonds, which leads to H bonds between water and other molecules Properties of water - due to H bonds o Cohesion/Adhesion - capillary action, surface tension o Specific heat - resists temp changes; allows life to exist o Evaporative cooling - due to high heat of vaporization - prevents overheating o Expansion upon freezing - crystalline lattice with more space; life underneath floating ice o Versality as solvent - hydration shells around ions, H-bonds around polar molecules Acids o Add H+ o Combine H+ with OH- to form water Bases o Add OH- o Accept H+ o Combine H+ with OH- to form water Acidification o CO2 + H2O = Excess H+ combines with H2CO3 CO32- (carbonate) to form (carbonic bicarbonate. Carbonate is acid) = H+ required for calcification HCO3- (calcium carbonate) by (bicarbonate) marine animals. Loss of calcium carbonate leads to loss of coral reef and loss of biodiversity.
Definitions:
Bonding capacity/valence: # of e- needed to complete octet
Covalent molecule: definite size and # of atoms Ionic compound: ratio of elements Evaporative cooling: surface of liquid cools due to molecules with greatest KE evaporating, so avg KE decreases; molecules must extract heat of vaporization from liquid, so it cools Buffer: accepts excess H+, donates them where needed Temperature: average KE, regardless of volume Thermal energy: total KE, depends on volume Spring turn: ice melts in spring and sinks; O2 returns to bottom and nutrients carried to top
CH. 4 CARBON
Variation of carbon skeleton
o Length o Branching o Double-bond position o Presence of rings Isomers o structural (covalent arrangement) o cis/trans isomer (spatial arrangement) o enantiomers (mirror) Functional groups - directly involved in reactions o Hydroxyl - dissolve o Carbonyl - ketone/aldehyde o Carboxyl - acid o Amino - base o Sulfhydryl - cross link o Phosphate - gives negative charge, ability to react with water; releasing energy o Methyl - tag Monosaccharide classification: o Aldose, ketose o # of C in skeleton o Arrangement around asymmetric carbon Polysaccharides o Storage - starch and glycogen o Structural - cellulose and chitin Protein - diverse structures = diverse functions o Storage o Enzymes o Hormones o Motor and contractile molecules o Defense o Transport o Receptor o Structure Levels of protein structure o Primary - amino acids o Secondary - alpha helix/beta-pleated sheet due to H-bonds between polypeptide backbone o Tertiary - hydrophobicity, disulfide bridges, H-bonds, ionic bonds, Van der Waals between R groups o Quaternary - aggregation of polypeptides Nucleotide sequence - amino sequence - protein structure and function RNA - base pairs with DNA or with itself (tRNA); variable in shape Carbs - CH2O Protein: CHON,S Fats: CHO,P Nucleic acids: CHON,P
Definitions:
Asymmetric carbon: C attached to 4 different elements
Glyosidic linkage: between two monosaccharide Ester linkage: 1 glycerol bonded to 3 fatty acids Unsaturated fats: double bonds, less H atoms Hydrogenated fats: unsaturated fats converted to saturated by adding H Steroids/cholesterol: 4 fused rings with chemical groups attached Polypeptide backbone: contains N terminus and C terminus; R group extends out Sickle cell: abnormal hemoglobin aggregates in chains, deforming RBCs into sickle shape Denaturation: protein loses shape and becomes inactive due to disruption of weak bonds (heat, pH, salinity) X-ray crystallography: diffracts x-ray through crystal to find structure of proteins Intrinsically disordered proteins: must binds with another molecule to see shape Nucleotide: pentose, nitrogenous base, phosphate Phosphodiester linkage: forms polynucleotides o 5' end: phosphate group o 3' end: OH group Chaperone proteins: help protein-folding