Lipids
Amino Acids
Protein Structure and Function
Biomolecules
Enzymes and Activation Energy
100

What is a lipid? What are the functions? What are the types of lipids?

Large non-polar molecule that is insoluble in water

Long-term energy storage, Protection/insulation, Structural components

Triglycerides, Phospholipids, Steroids

100

Where are amino acids found?

20 different ones found in proteins in body, but 8 have to come from diet

100

When can a protein not function properly? What is this called?

unless they fold into their proper shape

loses shape- denatured (destroys protein function)

100

Define Biomolecules and the 4 goups that they are categorized into

most molecules that make up the body

groups- Carbohydrates, Proteins, Nucleic Acids, Lipids

100

What has to be present for a reaction to occur?

Activation Energy

200

Define Tryglycerides. List the Functions. What is the composition of a triglyceride?

Fats and oils

Long-term energy storage and insulation

1 glycerol molecule linked to 3 fatty acids

200

Why do 8 amino acids have to come from diet?

Humans cannot synthesize

200

What disrupts protein structure?

Exposure of proteins to certain chemicals, change in pH, or high temperature

200

Describe polymers and monomers

Polymers- long chaina of repeated units

Monomers- individual units that make up polymers

200

What do enzymes end with and what is an example?

end in "-ase" (ex. sucrase- breaks sucrase down into glucose and fructose)

300

What is the difference between unsaturated, saturated, and trans fat?

Unsaturated- double bonds between carbons in fatty acid tails (Liquid at room temp., pack looser: Plant oils)

Saturated- no double bonds between carbons in fatty acid tails (solido at room temp, pack dense: Butter)

Trans Fat- lab converted cis-fatty acid to trans-fatty acid so it is better for cooking, have longer shelpf life. Problem- enzymes don't break down trans-fat quickly so leads to more plaque in arteries

300

How do amino acids differ?

By their R (radical) Groups

300

What are the 4 levels of proteins?

Primary, Secondary, Tertiary, Quaternary

300

Describe Dehydration Synthesis and Hydrolysis.

Dehydration Synthesis- formation of a covalent bond; Hydroxal group and H from another bond break away to form water (connects monomers to make polymers)


Hydrolysis- breaking of a covalent bond, water molecule is used (breaks polymers to make monomers)

300

What are enzymes? 

proteins that speed up reactions by holding substrates and stressing certain chemical bonds; not used up in a reaction and reused

400

What is the structure and function of a phospholipid?

Structure- similar to triglycerides (1 glycerol molecule, 2 fatty acids, 1 modified phosphate group), Fatty acids are nonpolar and hydrophobic, modified phosphate group is polar and hydrophylic

Function- form plasma membranes, in water form lipid bilayer (heads toward water and tails away from water)

400

Are R groups hydrophobic or hydrophilic? 

Some are hydrophobic and some are hydrophilic

400

Describe the 4 levels of proteins?

Primary- The sequence of amino acids

Secondary- Characterizes by the presence of alpha felices and beta (pleated) sheets held with hydrogen bonds

Tertiary- Final overall 3-D shape of a single polypeptide; Stabilized by covalent, ionic, & hydrogen bonding and Van der Waals attractions between different areas of the polypeptide; Some reversible changes possible here...important!!

Quaternary- A unique shape formed by the coming together of several different polypeptides

400

Differentiate between monosaccharides, disaccharides, and polysaccharides

Monosaccharides- single sugar molecule

Disaccharide- 2 monosaccharides joined together by dehydration synthesis (ex. lactose is componed of 1 galactose and 1 glucose)

Polysaccharide- long chains of monosaccharides linked together; excellent energy storage because it is too big and tightly coiled and don't leak through membranas as quickly

400

What is an active site? What is induced fit?

Unique pocket that only fits one substrate; binds with substrate (reactants) to form enzyme-substrate complex

After substrate binds, active site "closes down" around it (handshake)

500

Describe Steroids and Cholesterol.

Composed of 4 fused carbon rings; functional groups define different esteroides (ex. testosterone, estrogen, progesterone, cortisol)

Cholesterol- precursor molécula for many steroids

500

How do you categorize an R group?

It can be polar, non-polar, really polar, really non-polar

500

What are the 6 Functions of proteins and examples

Structure- keratin, collagen

Communication- some hormones, receptors

Membrane Transport- Channel proteins, carrier proteins

Recognition- Glycoproteins

Movement- Actin/ Myosin, Flagella, Cilia

Enzymes

500

Define and describe a protein

Definition- polymers of amino acids linked together by peptide bonds (long chains are called polypeptides)

Description-polypeptide that has folded into a particular shape and has a función

500

What are multienzyme complexes?

Each type of enzyme only does one thing so different enzymes group together to make the product easily pass to the active site of the next

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