Home > Flashcards > Print Preview
The flashcards below were created by user
on FreezingBlue Flashcards
. What would you like to do?
Long carbon chains with COOH end
Saturated Fatty Acids vs. Unsaturated Fatty Acids
Saturated = SINGLE double C=C bond
Unsaturated = One or more C=C bonds
- 3C Glycerol backbone + 3 fatty acids chains attached
- Important energy storage molecule
3C Glycerol backbone + 2 fatty acid chains + 1 phosphate group
- Type of lipid that regulates metabolic activities
- Include: hormones, cholesterol, Vit D
- Type of lipid
- Include: Prostaglandins, leukotrienes
How are lipids transported in the blood stream?
- Via lipoproteins & Albumin
- Classification: VLDL(bad) --- HDL (good)
Bonds found in proteins
Bonds found in carbohydrates
Bonds found in nucleis acids
Basic amino acids
Acidic amino acids
- Aspartic acid/Aspartate
- Glutamic Acid/Glutamate
Polar amino acids
- Cysteine (forms covalent disulfide bonds)
Nonpolar amino acids - I saw Lucy methodically probe and feel Alan, then Val tripped glycine
- Methionine (start amino acid)
- Proline (turn-inducing & affects tertiary structure)
How many amino acids are there and of those how many are essential?
20 amino acids total -- 10 of which are essential.
Forces creating tertiary structure
- 1. Disulfide bonds
- 2. Ionic interactions between side chains
- 3. H-bonding
- 4. Van der Waals
- 5. Hydrophobic side chains being pushed away from protein center
- Membrane pumps
- Tubulin - which polymerized to form MTs in flagella & cilia
- Maintain and strengthen cellular matrix
Describe the two anomeric forms of glucose
1. Alpha-glucose: anomeric carbon and methoxy carbon are on opposite ends of the ring
2. Beta-glucose: anomeric and methoxy carbons are on same side of the ring
Types of glucose linkages
1. Alpha: Digested by animals - starch & glycogen
2. Beta: Digested by bacteria - cellulose (bacteria break beta linkages)
Where are the largest amounts of glucose found?
The mucles and liver
How is glucose absorbed into most cells?
- 1. Mostly via facilitated diffusion
- 2. Or by secondary active transport fown the [Na+] gradient
What kind of cells can absorb glucose in the absence of insulin?
Neurons and hepatic cells
Components of a nucleotide
- 1. 5C pentose sugar
- 2. Nitrogenous base
- 3. Phosphate group
How many H-bonds are formed between the nitrogenous bases?
- A&T form 2 H-bonds
- C&G form 3 H-bonds
Directionality in which a nucleic acid is written and read?
5'--->3' (leading strand)
What is ATP?
What about NADH?
What about Mg2+?
- ATP is a nucleotide
- NADH is a coenzyme
- Mg+ is a cofactor (assist in enzyme fxn, minerals)
Non-competitive enzymatic inhibition
- Binds to somewhere other than active site
- Does NOT change enzyme-substrate affinity
- Decreases reaction rate
Competitive enzymatic inhibition
- Binds to the active site and thus, decreases enzyme-substrate affinity
- Does not change reaction rate
- Can be overcome by adding more substrate
Irreversible enzymatic inhibition
Covalently binds to enzymes
Types of enzymatic regulation (4)
- 1. Proteolytic cleavage (zymogen-->active enzyme)
- 2. Covalent modification (phosphorylation)
- 3. Protein subunit regulation (GPCRs)
- 4. Allosteric modulation (positive cooperativity)
- **Allosteric modulation results in a conformational change
Kinases vs. Phosphatases
- Kinases phosphorylate & usually deactivate
- Phosphatases dephosphorylate
Importance of cofactors?
Not all enzymes need cofactors
They are metal ions that activate an exzyme by binding to it
They help out enzyme catalyzed reaction by carrying/delivering electrons and being oxidized or reduced
Include: NADH, FADH2 etc.
What would you like to do?
Home > Flashcards > Print Preview