Macromolecules Flashcards

1
Q

What is a monomer?

A

A molecule that can be bonded to other monomers via covalent bonding.

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2
Q

What is a polymer?

A

Monomers bonded in long chains connected by covalent bonds.

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3
Q

What is hydrolysis and how does it occur?

A

The breaking down of a polymer by adding water to a molecule to break a bond.

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4
Q

What is dehydration and how does it occur?

A

A reaction that occurs during the synthesis of polymers, removing a water molecules from an unlinked monomer that forms a new bond.

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5
Q

What are carbohydrates?

A

Carbohydrates are sugar molecules that form mono, di, and polysaccharides.

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6
Q

What are monosaccharides? How are types of monosaccharides determined?

A

They are made up of monomers, multiples of the unit CH2O. They contain 3 - 7 carbons and all have carbonyl and hydroxyl groups. Placement of these groups determines what type of monosaccharides they are.

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7
Q

Aldoses and Ketoses are both carbohydrate monosaccharide sugars. What are the difference between the two?

A

Aldoses are monosaccharides that contain an aldehyde group, while ketoses are monosaccharides that contain a ketose group.

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8
Q

Why do monosaccharides form rings?

A

Rings are more stable in aqueous solutions than straight molecules.

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9
Q

What are disaccharides? How do they join?

A

They are molecules joined by glycosidic linkage, usually a carbohydrate to another carbohydrate but other groups are possible.

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10
Q

What is glycosidic linkage? How does it happen?

A

It is a covalent bond that connects carbohydrate molecules to other carbohydrate groups or other molecules via a dehydration reaction.

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11
Q

What does sucrose do in plants?

A

Transport form of sugar in plants

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12
Q

What are polysaccharides, what do they do and where are they found?

A

100s - 1000s of monosaccharides joined via glycosidic linkage. They store energy as glucose and are found in plants as starch and cellulose and in animals as glycogen.

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13
Q

What is starch? Can humans digest it? What is it made of and in what form?

A

Polysaccharides in plants. Humans can digest this (unlike cellulose). Made of glucose in the form of amylose or amylopectin with a helical, alpha position.

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14
Q

What is amylose and how is it linked?

A

Unbranched glucose in plants by a 1-4 linkage between glucose molecules.

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15
Q

What is amylopectin and how is it linked?

A

Somewhat branched glucose in plants by a 1-6 linkage at branch points, otherwise 1-4 linkage between glucose molecules.

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16
Q

What is glycose? Why is it so branched?

A

They are the polysaccharides in animals and the stored form of glucose. It is very branched to allow for short term storage of energy because it needs to be broken down faster (more end points = more access points so hydrolysis can occur faster) vs fat which is used for long term storage.

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17
Q

What is chitin, where is it found and how is it made?

A

Modified polysaccharide that contains nitrogen. Synthesized from the beta linkage of glucose with N-attachment. Found in arthropods and fungi.

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18
Q

What is cellulose?

A

Major component of plant cell walls. It is a polymer of glucose with 1-4 glycosidic linkage in the beta position which makes it straight and unbranched that contains free hydroxl groups.

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19
Q

Microfibrils

A

Thin structures in cells, usually described as bundles of cellulose in plant cell walls formed from free hydroxyl groups in cellulose molecules that form H-bonds with other molecules.

20
Q

What is glucose and how is it arranged?

A

Glucose is a carbohydrate polysaccharide sugar that makes up starch (alpha), cellulose (beta), chitin (beta) and glycogen (alpha). It forms either alpha or beta structures. Alpha forms helical, 3D structures and beta forms straight, unbranched structures that lead to microfibrils.

21
Q

What are proteins and how are the linked?

A

They are made of amino acids linked by unbranched peptide bonds. Have an alpha carbon, left side amino group, right side carboxyl group, and side chain R group and hydrogen.

22
Q

Why are R-side chains in amino acid proteins important?

A

R-groups in amino acids change with different types that determine amino acid physical and chemical properties.

23
Q

What are the properties of hydrophobic amino acids?

A

Hydrophobic amino acids try to avoid contact with water. They contain no O or OH in their side chains but can have NH, S, CH(n) and H.

24
Q

What are the different types of acids in protein synthesis?

A

There are 20 types and all have ammonium and carboxylic acid as their amino group and carboxyl group respectively.

25
What are the properties of hydrophilic amino acids with polar side chains?
Hydrophilic amino acids with polar side chains have either OH, SH, or NH2 (or combinations of multiple) in their side chains.
26
What are the properties of hydrophilic amino acids with electrically charged side chains?
Hydrophilic amino acids with electrically charged side chains can be either acidic (negatively charged) with O-, or basic (positively charged) with NH(1,2,3)+
27
What are polypeptides and how are they made?
They are a chain of amino acids formed by fusing amino acids connected with peptide bonds that release H2O when formed and are never branched and always linear.
28
What is the general structure of proteins?
Proteins are usually one or more polypeptides that fold into 3D shapes determined by amino acid sequences.
29
What are primary protein interactions?
Gene sequence; amino acids chain one after another in polypeptide form.
30
What are secondary protein interactions?
H-bonds between polypeptide backbone, with two types. Alpha helixes can form between every 4 amino acids where as beta pleated sheets are beta strands that connect side by side peptides via H-bonds.
31
What are tertiary protein interactions?
Interactions between side chains of amino acids by ionic bonds, hydrogen bonds, a disulphide bridge, or hydrophobic and van der Waals interactions.
32
What are quaternary protein interactions?
Interactions between multiple polypeptide chains.
33
What are denatured proteins and how does denaturing happen?
Denatured proteins are uncoiled, inactive proteins caused by high temperatures (high fevers) and cannot renature easily. (Kinda like boiling an egg).
34
What is the function of enzymatic proteins?
Selective acceleration of chemical reactions. ex) Digestive enzymes catalyze the hydrolysis of bonds in food molecules.
35
What is the function of defensive proteins?
Protection against disease. ex) antibodies inactive and help destroy viruses and bacteria.
36
What is the function of hormonal proteins?
Coordination of an organism's activites. ex) Insulin, a hormone secured by the pancreas, causes other tissues to take up glucose, regulating blood sugar concentration
37
What is the function of receptor proteins?
Response of a cell to chemical stimuli ex) Receptors build into the membrane of a nerve cell detect signaling molecules released by other nerve cells.
38
What is the function of storage proteins?
Storage of amino acids. ex) plants store energy in seeds.
39
What is the function of transport proteins?
Transport of substances ex) hemoglobin transports o2 from lungs to other parts of body.
40
What is the function of contractile and motor proteins?
Movement ex) Responsible for contractions of muscles
41
What is the function of structural proteins?
Support ex) Collage proteins provide a fibrous framework in animal connective tissues.
42
What are genomics?
Study of all person's genes (genomes), concerned with the structure, function, evolution and mapping.
43
What are proteomics?
Study of proteomes and their functions
44
What are proteomes?
Set of proteins produced in a biological context (organism, system).
45
What are peptide bonds and do they occur?
How proteins are linked; release H2O when formed (dehydration = synthetization)