Unit 1 - Chemistry of Life

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120 Terms

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Subatomic particles

protons, electrons and neutrons

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Nucleus of an atom

made of protons and neutrons in an orbital

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Valence shell

the last orbital in an atom

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Valence electrons

electrons inside the last orbital

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Atomic mass

the total number of protons and neutrons

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Atomic number

the number of protons

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O, C, H, and N

components of all living matter

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Achieving stability

reason for chemical interactions

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Covalent bonds

sharing electrons to achieve stability

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Pure elements

substances consisting of only one type of atom. (H2 , O2)

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Chemical compound

substances that are formed when two or more different elements chemically bond together

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Electronegativity

the attraction of an atom to another in a covalent bond

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Hydrogen bonds

attraction of a Hydrogen + Electronegative atom with another Hydrogen + Electronegative atom

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Ionic bonds

when atom transfer electrons to satisfy their valence shells

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Cation

a positively charged ion

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Anion

a negatively charged ion

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Adhesion

attraction between water and other molecules (xylem in plants)

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Cohesion

attraction between water molecules (high surface tension, transpiration pull)

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High heat capacity

ability to absorb and release large amounts of heat with only a slight change in temperature (how many C lost per 1 gram).

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Crystalline lattice

structure that contains spaces between molecules.

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Universal solvent

water dissolves all polar and ionic molecules, facilitating chemical reactions and processes in living organisms.

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A mixture

a combination of two or more substances that are PHYSICALLY bonded together

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Solutions

a uniform mixture of a solute and a solvent.

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Solute

dissolvents that melt into the solution

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Solvents

liquids in which solutes dissolve

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Aqueous solution

a solution in which water is the solvent

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Hydration shell

a layer of water molecules surrounding a solute particle, stabilizing it in solution and preventing it from interacting w/ other molecules

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Hydrophilic substances

any substance with affinity (attraction) to water, usually polar or charged.

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Hydrophobic substances

substances that repel water, are nonionic and non-polar, or cannot form hydrogen bonds.

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Hydrophobic tail

made of non-polar fatty acid chain

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Hydrophilic head

made of polar phosphate groups

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pH (power of hydrogen)

measuring the concentration of H+ ions in a solution.

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Buffer

helps maintain the internal pH of substances

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Carbonic acid-Bicarbonate system

buffer system in blood that regulates pH using carbonic acid (H₂CO₃) and bicarbonate (HCO₃⁻)

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pH of blood

7.4 (slightly basic)

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4 bonds elements

carbon

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2 bonds elements

oxygen and sulfer

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Location of Sulfer

in proteins

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Location of Oxygen and Hydrogen

in all types of macromolecules

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3 bond elements

nitrogen and phosphate

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Location of Nitrogen

in nucleic acids and proteins

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Location of Phosphorus

in nucleic acids and some lipids

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Single bond element

hydrogen

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Hydrocarbons

organic molecules that consist of carbon and hydrogen atoms (fuel source in biological processes)

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Isomers

compounds with the same molecular formula but different structural arrangement of atoms

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Structural isomers

same molecular formula but differ in the way atoms are connected or arranged (ex:- straight chain vs a branched chain)

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Geometric isomers (trans-cis)

compounds with same atoms and same connectivity but have different arrangements

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Cis isomers

isomers with similar groups on the same side of a double bond or ring.

<p>isomers with similar groups on the same side of a double bond or ring.</p>
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Trans isomers

isomers with similar groups on opposite sides of a double bond or ring.

<p>isomers with similar groups on opposite sides of a double bond or ring.</p>
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Enantiomers

isomers that are mirror images of each other, caused by a asymmetrical carbon atom that is 4 bonded.

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Estradiol

type of estrogen found in females

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Testosterone

the main sex hormone for males

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Steroids

a carbon skeleton made up of four infused rings (ex:- estradiol and testosterone)

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Chemical groups

groups of atoms that give specific properties and reactions to molecules, (ex:- hydroxyl, carboxyl, amino, and phosphate groups).

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Functional group

a specific group of hydrophilic atoms in a molecule that determines its chemical properties and reactions

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Hydroxyl group

(-OH) Alcohol, polar

<p>(-OH) Alcohol, <mark data-color="yellow" style="background-color: yellow; color: inherit">polar</mark></p>
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Carbonyl group

(>C=O) Ketone aldehyde, polar

<p>(&gt;C=O) Ketone aldehyde, <mark data-color="yellow" style="background-color: yellow; color: inherit">polar</mark></p>
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Carboxyl group

(-COOH) Carboxylic acid, or organic acid, polar

<p>(-COOH) Carboxylic acid, or organic acid, <mark data-color="yellow" style="background-color: yellow; color: inherit">polar</mark></p>
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Amino group

(-NH2) Amine, polar

<p>(-NH2) Amine, <mark data-color="yellow" style="background-color: yellow; color: inherit">polar</mark></p>
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Sulfhydryl group

(-SH) Thiol, polar

<p>(-SH) Thiol, <mark data-color="yellow" style="background-color: yellow; color: inherit">polar</mark></p>
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Phosphate group

(-OPO3²-) Organic phosphate, polar

<p>(-OPO3<sup>²-</sup>) Organic phosphate, <mark data-color="yellow" style="background-color: yellow; color: inherit">polar</mark></p>
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Methyl group

(-CH3) Methylated compound, non-polar

<p>(-CH3) Methylated compound, <mark data-color="blue" style="background-color: blue; color: inherit">non-polar</mark></p>
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ATP

the energy currency in cells

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ADP

an energy molecule that converts to ATP

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Polymer

a long molecule made up many monomers (bonded by covalent bonds)

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Carbohydrates

made from monosaccharides

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Proteins

made from amino acids

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Nucleic acids

made from nucleotides

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Lipids

made from fatty acids and glycerol

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Condensation reaction

a reaction where monomers combine to form polymers, releasing a molecule.

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Dehydration reaction

When the condensation reaction releases water

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Hydrolysis

Breaking down of polymers by adding water

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Enzymes

reusable proteins that speed up chemical reactions.

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Defensive proteins

protects against disease

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Storage Proteins

stores amino acids

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Casein

the protein of milk

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Ovalbumin

the protein of the egg white

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Transport proteins

transport of substances

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Hemoglobin

iron-containing protein in blood

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Hormonal proteins

coordinates an organism’s activity

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Insulin

a hormone secreted by the pancreas that regulates blood sugar by forcing tissues to absorb glucose.

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Receptor protein

responds to the cell by chemical stimuli

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Contractile and motor proteins

for movement (actin, myosin, cilia and flagella)

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Structural proteins

gives support and shape to cells and tissues

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Keratin

the protein of hair, horns, feathers and skin appendages

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Collagen and elastin

a fibrous framework in connective tissue

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Protein structure

amino group, carboxyl group and side chain

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Peptide bonds

covalent bonds that link together amino acids, forms when a carboxyl group of one amino acid reacts with an amino group of another

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Polypeptides

a chain of amino acids liked together by peptide bonds

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Amino acid - Nonpolar

side chains are hydrophobic

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Amino acid - Polar neutral

side chains are hydrophilic (slightly charged)

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Amino acid - Polar acidic

side chains are hydrophilic (negatively charged, presence of carboxyl group)

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Amino acid - Polar basic

side chains are hydrophilic (positively charged, presence of amino group)

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Protein - Primary structure

linear sequence liked by peptide bonds

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Protein - Secondary structure

parts of the polypeptide chain interact together through hydrogen bonds between atoms of the backbone

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Protein - Tertiary structure

the overall 3D shape of a polypeptide

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Protein - Quaternary structure

a protein chain made up of two or more polypeptide chain

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Alpha helix

a coiled structure held together by hydrogen bonds

<p>a coiled structure held together by hydrogen bonds</p>
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Beta-pleated sheet

flat structure where the segments of the chain line side by side, held together by hydrogen bonds

<p>flat structure where the segments of the chain line side by side, held together by hydrogen bonds</p>
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Denaturation

when the weak bonds holding the protein together is disturbed, causing it to unravel and lose it shape, therefore its function