Biomolecules Flashcards

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1
Q

fundamental particles that make up all matter

A

Atoms

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2
Q

any material that takes up space; this includes stars, planets, rocks, and living organisms

A

Matter

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3
Q

Each atom is composed of three subatomic particles, these are?

A

protons, neutrons, and electrons

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4
Q

The nucleus of an atom is composed of?

A

positively charged protons and uncharged neutrons, which are surrounded by negatively charged electrons.

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5
Q

pure substances composed of only one kind of atom. They are the simplest form of matter to have unique chemical properties.

A

Elements

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6
Q

elements are determined through this. This is the number of protons an element has in an atom

A

Atomic Number

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7
Q

When the number of protons of an atom is equal to its number of electrons, the atom is?

A

Electrically Neutral

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8
Q

are atoms that have lost or gained electrons, making them either positively (a cation) or negatively (an anion) charged, respectively

A

Ions

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9
Q

are usually composed of two or more atoms (with the exception of noble gases, which can consist of only one atom).

A

Molecules

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10
Q

Each element has a specific number of electrons occupying a distinct region around the nucleus. These regions are called?

A

Orbitals

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11
Q

The outermost energy shell of an atom is called its?

A

Valence shell

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12
Q

These atoms may ‘donate, steal, or share’ electrons with one another in order to fill up their valence shell, specifically the transfer of electrons from one atom to another

A

chemical bonding

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13
Q

When molecules of at least two atoms of different elements form chemical bonds, the resulting molecule is called a?

A

Compound

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14
Q

refer to compounds that contain carbon, especially carbon-hydrogen and carbon-carbon bonds.

A

Organic compounds

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15
Q

are compounds that do not form carbon-hydrogen bonds

A

Inorganic Compounds

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16
Q

are formed between two ions of opposite charges (a cation and an anion). This large gap of electronegativity allows atoms to ‘donate’ electrons to another atom.

A

Ionic Bonds

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17
Q

the tendency of an atom to attract a bonding pair of electrons)

A

Electronegativity

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18
Q

Atoms can also ‘share’ electrons in order to fill their valence shells. This is what occurs in?

A

covalent bonds

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19
Q

However, this sharing may not always be equal. occurs when one nucleus exerts a stronger pull of electrons than the other atoms. This produces an unequal distribution of electrons, resulting in one end of a molecule having a slightly positive charge while another end has a slightly negative charge.

A

polar covalent bond

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20
Q

occur when atoms exert an almost equal amount of pull on the electrons, resulting in a molecule with no differences in charge across its structure.

A

Non-polar Covalent Bonds

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21
Q

Complex macromolecules are? meaning that they are formed from many similar individual units bonded together by chemical bonds (usually covalent bonds).

A

Polymers

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22
Q

The units themselves are called?

A

Monomers

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23
Q

There are four types of macromolecules in biological systems

A

carbohydrates, lipids, proteins, and nucleic acids

24
Q

-Are basically your sugar molecules. They occur as compounds of carbon, hydrogen, and oxygen, in a 1:2:1, ratio.
-mainly act main energy sources and structural elements for the cell

A

Carbohydrates

25
Q

-the simplest form of carbohydrates
-monomers of disaccharides and polysaccharides, meaning they are the building blocks to create more complex carbohydrates.

A

Monosaccharides

26
Q

Two monosaccharides are joined by a type of covalent bond known as a glycosidic bond to form a?

A

Disaccharide

27
Q

-When many sugar units are joined together by glycosidic bonds to create a large carbohydrate, a ? is formed.
-act as energy reserves such as starch and glycogen (both have long chain branching sugar units).
-act as structural material for organisms

A

polysaccharide

28
Q

-are fatty, oily, or waxy compounds dominated by non-polar carbon-carbon and carbon-hydrogen bonds.
- hydrophobic.
-do not form polymers.

A

Lipids

29
Q

insoluble to water

A

Hydrophobic

30
Q

There are four main kinds of lipids:

A

triglycerides, phospholipids, steroids, and waxes.

31
Q

-commonly found in fats and oils.
- regarded as a major fuel source of animals in the form of fats.
-composed of a glycerol molecule attached with three fatty acid chains. The types of fatty acids in these give it different properties.

A

Triglycerides

32
Q

-are an important type of lipid in all organisms as this is what mostly comprises a cell’s plasma membrane.
-structured similarly to triglycerides except that one fatty acid chain is replaced by a water-soluble phosphate molecule
-amphiphatic

A

Phospholipids

33
Q

meaning that the molecule has a water-soluble and a water-insoluble end in the molecule

A

amphiphatic

34
Q

-long chain fatty acids with alcohols or other compounds attached to them.

A

Waxes

35
Q

-are lipids with no fatty acid chains. Instead, these occur in the form of four rings.
-signaling molecules and providing fluidity to cell membranes

A

Steroids

36
Q

acts a precursor molecule to the formation of many important molecules such as bile salts (for digestion), vitamin D, and other steroid hormones.

A

Cholesterol

37
Q

large complex molecules that are polymers of amino acids

A

Proteins

38
Q

are primarily made up of the elements Carbon, Hydrogen, Oxygen, and Nitrogen.

A

Amino Acids

39
Q

amino acids in proteins are joined together by ?, a type of covalent bond.

A

peptide bonds

39
Q

amino acids in proteins are joined together by ?, a type of covalent bond.

A

peptide bonds

40
Q

When two amino acids form a peptide bond

A

Dipeptide Bond

41
Q

More amino acids can form peptide bonds at the end to form a long chain of amino acids called a

A

polypeptide

42
Q

Proteins are highly organized with four structural levels. (1)

A

Primary structure: The sequence of amino acids in a polypeptide chain

43
Q

Proteins are highly organized with four structural levels. (2)

A

Secondary structure: The folding of the polypeptide chain into sheets and helices by hydrogen bonding

44
Q

Proteins are highly organized with four structural levels. (3)

A

Tertiary structure: The complete three-dimensional structure of a polypeptide

45
Q

Proteins are highly organized with four structural levels. (4)

A

Quarternary structure: The combination of two or more polypeptide chains (Only proteins with more than one polypeptide chain can form a quarternary structure.)

46
Q

The immense diversity of complex forms proteins can attain allows them to have numerous functional roles in biological systems. Some of these functions include:

A

-Providing structural elements to cells and the body (g. your hair is made up mostly of a protein called keratin),
-Act as conduits for communication (as hormones, cell receptors, etc.),
-Help transport materials in the body (steroid hormones are carried by transport proteins in the blood)
-Act as catalysts (e. increases the rate of chemical reactions)
-Movement (muscular contraction is done by proteins in muscle tissue)
-Cell adhesion (some proteins hold cells tightly together, providing protection from mechanical stress such as tearing)

47
Q

unfolds proteins from its tertiary/quarternary structure

A

Denaturation

48
Q

regarded as ‘informational macromolecules’ that provides instructions in the layout to creating proteins

A

Nucleic Acids

49
Q

two types of nucleic acids:

A

deoxyribonucleic acid (DNA) and ribonucleic acid (RNA).

50
Q

Nucleic acids are polymers consisting of monomers, these have a sugar, a phosphate, and a nitrogenous base

A

Nucleotides

51
Q

These nitrogenous bases serve as a kind of ‘identity’ to the nucleotide.
There are five kinds of nitrogenous bases:

A

guanine (G),
cytosine (C),
thymine (T),
adenine (A),
and uracil (U).

52
Q

structural differences between DNA and RNA:

A

DNA is composed of two strands of nucleotides whereas RNA only has one strand.
DNA contains the nitrogenous base Thymine whereas RNA replaces this with Uracil.
The sugar base in DNA is a deoxyribose whereas RNA has a ribose sugar.

53
Q

stores genetic information as a string of nucleotides which contains the instructions on how amino acids are arranged in polypeptides

A

DNA (Deoxyribonucleic Acid)

54
Q

enables cells to ‘read’ and convert this information into an amino acid sequence—the primary structure of a protein.

A

RNA (Ribonucleic Acid)

55
Q

formation of RNA from DNA

A

Transcription

56
Q

formation of the amino acid sequence from RNA

A

Translation