Chapter 2- Chemistry of Life Flashcards

1
Q

Matter

A

any material that takes up space

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2
Q

Energy

A

the ability to do work. In this context, work means moving matter.

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3
Q

Element

A

A pure substance that cannot be broken down by chemical means into other substances

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4
Q

Periodic table

A

Table the arranges the elements in such a way that their chemical properties repeat in each vertical column

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5
Q

Bulk elements

A

elements that are needed in the largest amounts because they make up majority of every living cell

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6
Q

Trace elements

A

elements that needed in small amounts

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7
Q

Atom

A

the smallest possible “piece” of an element, that retains the characteristics of the element

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8
Q

Three types of particles

A

Protons: carry a positive charge
Neutrons: uncharged
(Protons+Neutrons create the central nucleus)
Electrons: carry a negative charge

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9
Q

Atomic number

A

the number of protons in the nucleus

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10
Q

Ion

A

An atom (or group of atoms) that has gained or lost electrons and therefore has a net negative or positive charge. They also form ionic bonds

If # of protons= # of electrons, then atom of electrically neutral; no net charge

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11
Q

Mass number

A

The total number of protons and neutrons in its nucleus

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12
Q

Isotope

A

Any different forms of a single element

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13
Q

Atomic weight

A

Average mass of all atoms of an element; typically, close to the mass number of the most abundant isotope

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14
Q

Radioactive isotopes

A

Emit energy as ray or particles when they break down into more stable forms. Have a half-life, which is the time it takes for half of the atoms to emit radiation, or “decay” to a different, more stable form.

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15
Q

Compound

A

a molecule composed of two or more different elements. Written in terms of a molecular formula, where the constituent elements are written with subscripts of the number of atoms of each elements ex. H20

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16
Q

Orbitals

A

describes the most likely location for an electron relative to its nucleus

17
Q

Energy shells

A

Octet rule: 2 electrons in the closest shell, and 8 electrons fill the other shells. Outermost shell is called a valence shell.

18
Q

Electronegativity

A

the ability of an atom to attract electrons on a scale of 0 to 4

19
Q

Chemical bond

A

transfer of electrons from one atom to another which creates an attractice force, which holds atoms together

20
Q

Ion

A

an atom that has lost or gained electrons

21
Q

Ionic bond

A

one atom donates one or more electrons to another atom because electronegativity is very large (>1.7). Opposite charged ions attract each other.

22
Q

Covalent bond

A

two atoms share electrons (ex. one bond, two bonds, three bonds)

Polar covalent bond: electrons are shared unequally because electronegativity difference is moderate or large (0.4 to 1.7)

Nonpolar covalent bond: Electrons are shared equally because electronegativity difference is small (<0.4)

Hydrogen bond: An atom with a partial negative charge attracts an atom with a partial positive charge (Weak bond; breaks easily)

23
Q

Properities of water

A

Cohesion: the tendency of water molecules to stick together
Adhesion: the tendency to form hydrogen bonds with substances other than water
Evaporation: conversion of liquid into vapour

Water is a solvent, meaning its a chemical in which other substances called solutes can dissolve. A *solution *consists of one or more solutes in a solvent.

24
Q

Hydrophillic

A

readily dissolve in water (“water-loving”); substances are either polar or charged

25
Q

Hydrophobic

A

do not dissolve in water (aka. form bonds with hydrogen bonds) (“water-fearing”); nonpolar molecules

26
Q

Chemical reaction

A

two or more molecules “swap” their atoms to make different molecules; equation is marked with reactacts (left) that create products (right)

*have same number of atoms of both sides of the equation (atoms are simply rearranged; neither created or destroyed)

27
Q

The pH scale

A

A neutral solution has a pH of 7. The higher the concentration of hydrogen ions (H+), the more acidic the solution (pH less than 7). The lower the concentration of (H+), and more (OH-) ions, the more basic the solution (pH greater than 7).

28
Q

Organic molecules

A

chemical compounds that contain both carbon and hydrogen

Four main types of organic molecules: carbohydrates, proteins, nucleic acids, and lipids

Organic molecules have small groups of atoms, with four most common: hydroxyl, carboxyl, amino, and phosphate groups

29
Q

Proteins, nucleic acids, and some carbohydrates share a common property of being polymers

A

Polymers are chains of small molecular subunits called monomers. A polymer is made of monomers that are linked together (like a train with individual railcards).

30
Q

Dehydration synthesis

A

Water is removed and a new covalent bond forms between two monomers (where a hydrogen atom and a -OH hydroxyl group was removed by enzyme from each molecule to form water)

31
Q

Hydrolysis

A

Water breaks the bond between monomers ( enzyme use atoms from water to make a hydrozyl group -OH in one molecule and a hydrogen atom in the other molecule).

32
Q

Protein

A

chain of monomers called amino acids. Each amino acid has a central carbon atom bonded to four other atoms or groups of atoms. One is a hydrogen atom; another is a carboyl group; a third is an amino group (nitrogen atom single-bonded to two hydrogen atoms (-NH2); and the fourth is a side chain, or R group, which can be any of 20 Amino Acids

33
Q

Pepetide bond

A

A single convalent bond that forms between the carboxyl function group of a amino acid and the amine group of another amino acid (bond is formed by a dehydration/condensation chemical reaction (water produced). Bond is broken via hydrolysis reaction (water required).

34
Q

Four levels of protein structure

A

Primary structure (sequence): Amino acid sequence of a polypeptide (not a functional protein)

Secondary structure (“substructure”): Result of hydrogen bonding between the backbone atoms (not the R groups) of the amino acid, which form alpha helix and/or beta sheets

Tertiary structure (polypepetide shape):overral shape of one polypeptide; result of different types of bonds that form between the R groups of the amino acids

Quaternary structure (protein shape): Overral protein shape, arising from bonding of mutiple polypeptides that make up the functional protein.

*Typically (but not all the time): you need proceeding structures to have the current structure of protein. The structure/shape of protein is essential in determining its function. To denature a protein is to change its shape so it can no longer carry out its function.

35
Q

How does a cell know which amino acids to string together to from a particular protein?

A

Each protein’s primary structure is encoded in a sequence of nucleic acid, a polymer consisting of monomers called nucleotides (cells contain two types of nucleic acids: DNA (deoxyribonucleic acid) and RNA (ribonucleic acid)

36
Q

What do nucleotide monomers consist of?

A

Three components: At the center is a pentose sugar(five-carbon)- ribose in RNA and deoxyribose in DNA. Attached to the sugar’s carbon atoms is one or more phosphate group. Attached to the opposite side of sugar is a nitrogenous base: adenine (A), thymine (T), guanine (G), cytosine (C), or uracil (U). DNA contains A,T, G, C while RNA contains A,U,G,C