P1 Maced Biochem

Front 1

Characteristics of water molecules that are believed to be responsible for its
anomalous "behavior."

Back 1

High boiling point
High freezing point
High heat capacity
Have a dipolar character, which leads to hydrogen bonding
Solid water (ice) is less dense than liquid water, floats

Front 2

Name the chemical species represented by the formula H3O+.

Back 2

Hydronium ion

Front 3

Define the equilibrium constant.

Back 3

K’eq = [H+][A-]
[HA]

An expression that indicates the extent of dissociation of the compound AH into A- and H+. It relates the individual ion concentrations to the aqueous compound.

Front 4

List the ways in which [H+] can influence biological systems.

Back 4

-Rates of enzyme-catalyzed reactions
-Permeability of membranes to many molecules
-Stability and “native conformation” of proteins and other macromolecules
-Rates of transport of molecules, both charged and uncharged, through membranes
-Absorption, transport and metabolism of drugs
-Hydrophobicity or hydrophilicity of a compound

Front 5

two most important buffer systems in the body. more important?

Back 5

Phosphate buffer system: has a pK’ closer to the desired pH of the body, BUT
Bicarbonate buffer system: manages most of the buffering of the blood because of its abundance;

Front 6

pK's of the bicarbonate and phosphate systems?

Back 6

Note: the pK’ is the –logK’eq

Phosphate pK’ ≈ 6.7
Bicarbonate pK’ ≈ 6.1

Remember, a compound buffers best at a pH near its pK’

Front 7

Define "acid" and "base" as usually used in biological systems.

Back 7

Acid: proton donor
Base: proton acceptor

Mnemonic: BAD (Base Accepts; Acid Donates)

Front 8

Write the Henderson-Hasselbalch equation, and describe its utility

Back 8

pH = pK’ + log[base]
[acid]

Relates the concentrations of the components of conjugate pairs to the pH of their environment.

It allows physicians to calculate acid/base balances in the body.

Front 9

What are the relative concentrations of conjugate acid/base when pH equals pK?

Back 9

When the pH equals the pK, the components of the system are present in equal amounts (the concentrations of each conjugate pair are equal).

Front 10

structure of a molecule, and the pK's of its ionizable groups, molecule's titration curve?.

Back 10

Look for neutral atom

Front 11

What defines a lipid?

Back 11

not water soluble; oily, greasy, waxy. extracted from organisms by organic solvents

Front 12

classes of lipids

Back 12

 Fatty acids
 Triacylglycerols
 Phospholipids (and related sphingolipids)
 Steroids
 Eicosanoids
 Vitamins

Front 13

7. Why are fatty acids named fatty acids? What is “fatty” about them? What is acidic about them?

Back 13

 Unbranched hydrocarbon chain (hydrophobic), fatty part
 Ionizable carboxyl group (acidic part)

Front 14

9. Why do triacylglycerols make such a good form of energy storage

Back 14

Triacylglycerols are also stored in an anhydrous form, whereas carbohydrates are stored with water.

Front 15

10. What are the roles of glycosphingolipids in humans?

Back 15

They are responsible for blood groups (including the ABO blood group).

Front 16

12. Do you expect to find fatty acids or lipid hormones free in the blood? Why?

Back 16

No; because they are hydrophobic. They must be transported as large complexes with proteins.

Front 17

13. Describe the lipid bilayer membrane. Name the three classes of lipids of which it is composed.

Back 17

 Glycerophospholipids
 Sphingolipids
 Steroids

Front 18

How do you name lipids?

Back 18

2 ways, omega and p

Front 19

2 cells types with lots shingolipids?

Back 19

nerve and RBC

Front 20

4 roles of steroids? aka cholestorol

Back 20

D H V M
digestion, hormones, vitamins, membrane

Front 21

mech of aspirin action?

Back 21

inhibits cyclogenase

Front 22

ATP ideal storage form cuz?

Back 22

needs enzyme to break bond, stable

Front 23

what role do cAMP and cGMP have?

Back 23

regulators

Front 24

Purpose phosphorlation of enzyme

Back 24

cell growth

Front 25

3 nucleotide components

Back 25

Phosphate
Nitrogen bases
Sugar

Front 26

Purines?
Pyrimidines?
Structure?

Back 26

A,G
C, U, T
Py is single

Front 27

ribonucleotide or deoxyribonucleotide

Back 27

ribo has O on 2'

Front 28

nucleotide?
nucleoside?

Back 28

tide is complete,
side no phosphate

Front 29

DNA, RNA bases

Back 29

come on tard

Front 30

H bonds for pairs

Back 30

AT--> 2
CG-->3
tea for 2

Front 31

antiparallel

Back 31

3' to 5' and other is 5' to 3'

Front 32

DNA at 94 degrees

Back 32

denatured

Front 33

mod of base affect gene expression? nucleotide not in genes that affects metabolism?
mod on mRNA?

Back 33

Cytosine methylation,
caffeine?,
Methylated G's

Front 34

Aliphatic Aminos

Back 34

G A V L P I
Glycine, alanine, valine, leucine, proline, isoleucine

Front 35

Aromatic Aminos

Back 35

T P T
Tyrosine, Phenolalanine, Tryptophan

Front 36

Basic Aminos

Back 36

H L A
Histadine, lysine, Arginine

Front 37

Acidic Aminos

Back 37

G A G A
glutamic, aspartic, glutamine, aspartine

Front 38

Maple Syrup Disease?

Back 38

V L I
Valine, Leucine, Isoleucine

Front 39

Disorders from tyrosine, phenolalanine

Back 39

tyr: albinism, tyrosis, alcapturia
P: PKU

Front 40

Cause Pellegra

Back 40

Tryptophan deficientcy

Front 41

OH groups?
S groups?
reactions they undergo?

Back 41

OH: Serine, Thrionine
S: Cytesine, Methionine
S--> disulfide bridges
both like phosphorlation

Front 42

Essential Amino acids

Back 42

Pvt. Tim Hall
no G's, no tryrosine, no proline, no serine

Front 43

4 compounds aminos are precursors

Back 43

alanine = glucose
glycine = heme, purine
tryosine = thyriod
arginine = NO2

Front 44

what are proteins made of? unique about their bond?

Back 44

amino acids, peptide bonds, strong from taotomerization

Front 45

functions of proteins

Back 45

enzymes, structural, transport, contractile structures

Front 46

solubility of proteins

Back 46

Fibrous and insoluble: i.e. collagen, elastin, and keratin
Globular and soluble: i.e. albumin and hemoglobin
Fibrous and soluble: i.e. fibrinogen

Front 47

different structures of proteins

Back 47

primary, secondary, tertiary, quaternary (shapes?)

Front 48

what are some common mods for proteins?

Back 48

Acetylation: N-terminal residue of the protein is acetylated, more resistant to degradation
Carboxylation: addition of COOH
Hydroxylation: addition of OH
Glycosylation: addition of glucose
Phosphorylation: addition of phosphate
Disulfide linkages: links parts of the polypeptide chain

Front 49

Which aminos are commonly phosphoralated

Back 49

Serine, Threonine, Tyrosine

Front 50

alpha helix, beta sheet, beta turns?

Back 50

b sheet--> antiparallel most stable
turns from H bonds

Front 51

what stabilizes higher order protein structures

Back 51

H bonding, hydrophobic effects, disulfide bonds, van der walls forces

Front 52

aminos likely to have charge at neutral pH

Back 52

Aspartic, glutamic, cytetine, tyrosine (neg)
lysine, argenine, histadine, (pos)

Front 53

proteins denatured how

Back 53

heat, pH, detergents, chaotropic agents, organic solvents

Front 54

Hydrophobic Effect

Back 54

entropy driven, bring shit together

Front 55

What is Enyzme>

Back 55

catalyze reaction, not get used up

Front 56

enzyme: what does it affect, what not?

Back 56

activation energy,
not G Keq

Front 57

Two models how they work and describe, for enyzmes

Back 57

lock and key--> specificity
induced fit--> catalytic and spec
3 point attachement (ensure steriospecificity)

Front 58

Prosthetic group, ex?

Back 58

small nonprotein bound to active sites, complex called holoenzyme
heme, biotin, flavin

Front 59

6 classes proteins?

Back 59

T L H O I L
transferases, lyases, hydrolases, oxidativereducatases, isomerases, ligases

Front 60

Michaelis menten equation

Back 60

V = Vmax [S]
Km + [S]

Front 61

on michialis menten plot where Vmax and Km

Back 61

Vmax top
Km half Vmax on X

Front 62

Lineweaver burk plot also called, what are intercepts?

Back 62

double reciprocal, X -1/Km
Y 1/Vmax

Front 63

Eadie Hofstee

Back 63

spread out data

Front 64

Competitive inhibitor is different from other inhibitors how?

Back 64

binds to active site

Front 65

What different for different inhibitors on lineweaverburk

Back 65

comp--> Km diff
non-->Vmax diff
un-->both different

Front 66

what does inhibitor react with for each type?

Back 66

you know this, unthreesome!

Front 67

Sigmoid shape in L-B graph shows what (didnt really go over)

Back 67

positive coopertivity

Front 68

What are carbohydrates? Aldoses? Ketoses?

Back 68

Carbohydrates: class of compounds which consist of polyhydroxyaldehydes, polyhydroxyketones and compounds which can be hydrolyzed to give polyhydroxyaldehydes or polyhydroxyketones

Aldoses: monosaccharide with an aldehyde group
Ketoses: monosaccharide with a ketone group

Front 69

2. What is the most important monosaccharide, and which polysaccharides are made up of this saccharide?

Back 69

Glucose is the most important monosaccharide. It is a subunit of starch, cellulose and glycogen.

Front 70

3. Pyran and furan are organic compounds for which what sugar structures are named? How many atoms per ring?

Back 70

Furan: a 5-membered cyclic structure
Pyran: a 6-membered cyclic structure

Front 71

4. What is mutarotation, and where does it take place?

Back 71

Mutarotation involves changes in configuration at the anomeric carbon by ring opening and closing.

Front 72

5. What are two conformations of 6 membered rings?

Back 72

chair and boat

Front 73

sugar acids named?

Back 73

If the terminal aldehyde is oxidized to an acid, “-aldonic acid”
If the terminal hydroxyl group is oxidized to an acid, “-uronic acid”
If both terminal groupsare oxidized to acids, “-aldaric acid”

Front 74

7.Name and describe two commonly found modifications of sugars.

Back 74

Amino sugars: formed when a hydroxyl group is replaced by an amine group
Deoxy sugars: formed when a hydroxyl group is replaced by a hydrogen

Front 75

8.What is a glycoside and an aglycone?

Back 75

Glycosides: formed when the anomeric hydroxyl group of a sugar reacts with another hydroxyl compound. The sugar providing the anomeric carbon is the one the compound is named for, the other is known as the aglycone

Front 76

9.Which of the three most important polysaccharides have alpha linked sugars? Beta linked? What is the importance of this?

Back 76

Glycogen: has  linkages; forms a tree-like structure (which allows addition/removal of glucose when it’s needed in the body)
Starch: has  linkages
Cellulose: has B linkages; we cannot digest

Front 77

10.Name three important disaccharides and tell which have alpha or beta linked sugars.

Back 77

Maltose: 2 glucoses connected by an  linkage
Sucrose: 1 glucose and 1 fructose connected by an  linkage
Lactose: 1 glucose and 1 galactose connected by a B linkage

Front 78

11.Tell what glycosaminoglycans are, and name two important ones.

Back 78

Glycosaminoglycans (GAG’s): unbranched polysaccharides made up of repeating disaccharides where one is an amino sugar and the other is a uronic acid
 Hyaluronic acid
 Heparin

Front 79

12. In the A, B, O blood group substances, where is the difference in the structures of the oligosaccharides located? How many sugars are different?

Back 79

Difference due to presence or absence of N-acetyl-galactosamine or galactose linked to the penultimate galactose. 1 sugar difference.

Front 80

Where glycolysis take place?

Back 80

Cytosol

Front 81

Gycolysis: starting substrate and possible ending products?

Back 81

Glucose
Pyruvate, Lactate

Front 82

What musst every cell that metabolizes glucose do first? what enzymes do this?

Back 82

Phosphoralate
kinases ex first step hexokinase

Front 83

Commited step of glycolysis:
what is enzyme, substrate, product? ATP?

Back 83

Phosphofructokinase
Fructose-6-Phosphate
Fructose-1-6-Phosphate
ATP used

Front 84

Control factors of gylcolysis

Back 84

first reaction (hexokinase)
phosphofructokinase (3rd)
last rxn (+) fructose 1-6 biphosphate
(-) ATP

Front 85

In what steps of gylcolysis is ATP generated?

Back 85

7th step and last step
3PG and pyruvate

Front 86

glycolysis steps that cant be reversed for Gluconeogensis?

Back 86

commited step,
last step,
first step
?

Front 87

Types of approaches to get around barriers encountered in reversing glycolytic path?

Back 87

different locations (ex mitochondria and ER)
different enzymes spec for this

Front 88

subcellular organelles involved in gluconeogenesis?

Back 88

ER and mitchondria

Front 89

malate shuttle is? where take place?

Back 89

moves malate from inside mitochondria to outside where its converted back to oxaloacetate

Front 90

how G-6-P convereted to glucose is gluconeogenesis? T1-3 what moves what?

Back 90

dephosphoralated in the ER by phosphatase in lumenal wall

Front 91

which enzyme used in gluconeogenesis in mitochondria and cytosol?

Back 91

malate dehydrogenase

Front 92

what tissues are capable of carrying out all steps of gluconeogenesis?

Back 92

liver, kidney, (intestine but no one cares)