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Bio 20 AP > basic biochem > Flashcards

basic biochem Flashcards

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1
Q

What is the test for Carbs

A

Benedicts (reducing sugars - monosaccharides) from blue to red (must be heated)
Starch - Detect the presence of complex carbohydrates if positive iodine creates blue-black

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2
Q

What is an isomer?

A

Same chimcal formula diffrent structure - Glucose, Fructose

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3
Q

What are disaccarides?

A

Formed from two monosaccharides joining into one, sucrose is formed from glucose and fructose

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4
Q

What is a polysaccaride?

A

Formed from many sugar molecules bonded together.

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5
Q

What is starch?

A

Main stroage molecules in plants

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6
Q

What is glycogen?

A

Main storage molecules in animals. The liver produces glycogen (long forms of glucose)

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7
Q

What is cellulose?

A

Structural polysaccharides are made of beta glucose.

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8
Q

What are lipids?

A

A group of organic substances insoluble in water - energy storage molecules like oil/fat

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9
Q

What is a fat molecule consisted of?

A

3 molecules of fatty acid and one glycerol molecule (triglyceride) formed by dehydration synthesis.

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10
Q

What makes a fatty acid saturated?

A

No double bonds

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11
Q

What makes a fatty acid unsaturated?

A

one or more double bonds

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12
Q

What is a test for lipids?

A

Sudan 6 test - lipids dissolve in Sudan 6 indicator turning it from a black to red
Translucence test - lipids cause unglazed brown paper to become translucent

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13
Q

Why is choletral important?

Where is it produced

A

Made in liver
Needed to make cell membranes, insulate nerves, some hormones - a type of steroid

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14
Q

What are proteins?

A

Polymers of amino acids

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15
Q

How many amino acids?

A

20 found in all living tings. All have an amine group and a carboxyl group bonded to a central carbon

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16
Q

What are essential amino acids?

A

Cannot be made by the body and must be consumed in diet - 9 in total

17
Q

How are peptides bonded?

A

Dehydration synthesis reactions occur when an amine group of one A.A is joined to carboxyl group of another

18
Q

What is a long chain of amino acids called?

A

Polypeptide - linear sequences of a.a. is called a primary structure

19
Q

What are three ways proteins are broken down>

A

Hydrolysis - enzymes are used to split peptide bonds, requires addition of water
Denaturation - Changes in pH may destory tertialt structure of a proteins. If this change is permanent its said to have coagulated
Deamination - removal of an amine group by the liver in order to convert a.a. to sugar or lipids since we aare unable to store a.a.

20
Q

What is a test for proteins?

A

Biuret - Positive = purple

21
Q

What is nucleic acid?

A

Building blocks of DNA and RNA

22
Q

What are enzymes

A

Natural catalysts that provide activation energy for breakdown of molecule that it fits

23
Q

What is an active site?

A

Part of enzyme that binds to substrate.

24
Q

What is a substrate?

A

Molecule being broken apart by enzymes

25
Q

What is a cofactor

A

An inorganic substances that help enzymes work correctly

26
Q

What is a co-enzyme?

A

Organic molecule usually made from vitamins

27
Q

What is a vitamin>

A

Organic compounds that an organism needs to function and not an energy source/

28
Q

What is a mineral?

A

Inorganic substances needed to survive

29
Q

What is allosteric activity

A

The change in an enzyme is caused by the binding of a molecule. May prevent or promote enzyme activity.

30
Q

What are factors that effect enzymes

A

Temperature - as increases temperature so does the rate of reaction until a certain point
pH - Each metabolic reaction has an optimum range that is best for reactions
3. Substrate reactions - greater concentration, higher rate
4. Inhibitors - Inhibotrs are molecules that attach to enzymes and reduce their ability to bind to the substrate

31
Q

What is a competitve inhibitor?

A

Attach to active site of enzyme blocking substrate
]

32
Q

What are non-competitve inhibitors?

A

Attach elsewhere to enzyme changing shape of active site preventing binding of substrate.

Bio 20 AP (11 decks)

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