TBL 1 - Amino acids and structure function relationships in proteins

Question 1

Amino acid configuration found in proteins in the human body

Answer 1

L

Question 2

L-DOPA

Answer 2

Derivative of tyrosine

Used to treat Parkinson’s disease

Question 3

Essential Amino acids

Answer 3

THIK WLF VRM

Threonine
Histidine
Isoleucine
Lysine
Tryptophan
Leucine
Phenylalanine
Valine
Arginine - Essential in growing children
Methionine

Question 4

Gylcine is:

Answer 4

Flexible

Achiral

Question 5

AA which is used as a source of energy for muscles

Answer 5

Alanine

Question 6

SAM

Answer 6

S-adenosyl methionine

Methyl donor

Question 7

BCAA’s

Answer 7

Isoeucine
Leucine
Valine

Question 8

MSUD

Answer 8

Maple syrup urine disease

Deficiency in alpha-ketoacid dehydrogenase complex

Question 9

PKU

Answer 9

Phenylketonuria

Deficiency in phenylalanine hydroxylase

Question 10

Which AA makes tyrosine? and by using which enzyme?

Answer 10

Phenylalanine

Phenylalanine hydroxylase

Question 11

Precursor of DOPA

Answer 11

Tyrosine

Question 12

Ketogenic only AA’s

Answer 12

KiLL

Lysine
Leucine

Question 13

Gucogenic and ketogenic AA’s

Answer 13

Isoleucine, phenylalanine, threonine, tyrosine, tryptophan

Thank You IF u Would

Question 14

Basic AA’s
vs
Acidic AA’s

Answer 14

Arginine
Lysine
Histidine

Aspartic acid
Glutamic acid

Question 15

AA which is neutral at physiological pH:

Answer 15

Histidine

Question 16

2 modified AA’s, how they are made and their biochemical significance:

Answer 16

hydroxyproline hydroxylysine

Hydroxylation reaction which requires Vitamin C as a cofactor

Used in collagen production

Question 17

MSUD causes:

Answer 17

A build up of BCAAs in urine, and blood which are toxic to the brain and cause mental retardation

Question 18

PKU patients can not synthesize which AA?

Answer 18

Tyrosine

Question 19

Melanin is created by which AA

Answer 19

Tyrosine

Question 20

In a PKU patient, phenylalanine is converted to what? and why

Answer 20

it can not be converted to tyrosine due the absence of phenylalanine hydroxylase, so instead it is converted to phenylacetate and phenyllacetate

Question 21

Presentation of PKU patient

Answer 21

Mental retardation
Musty odor to urine
Hypopigmentation to skin

Question 22

Serine and tyrosine unergo _____ reaction at the _____ group

Answer 22

phosphorylation

hydroxyl

Question 23

AA’s that modify the acitivites of many enzymes through phosphorylation

Answer 23

Serine and tyrosine

Question 24

Tyrosine is the precursor for:

Answer 24

Tyrosine Doesn’t Need Everyone To Make Dopamine

DOPA, norepinephrine, epinephrine, thyroxine, melanin, dopamine

Question 25

Tryptophan is the precursor for:

Answer 25

Tryp'n Never helped a Medical Student | niacin (B3), melatonin, serotonin

Question 26

Glutamine carries ______

Answer 26

Ammonia through out the body

Question 27

Methionine is crucial in:

Answer 27

MET - STARTing the polypeptide chain Synthesis of methyl donor SAM (S-adenosyl methionine) Have you ever MET SAM?

Question 28

Glycine's importance:

Answer 28

Heme production | Abundant in collagen

Question 29

Bonding present in secondary structures

Answer 29

``` Hydrogen bonding (intramolecular for alpha-helix intermolecular for beta-sheets) Sometimes disulfide bonding ```

Question 30

Amino acids that are largely apart of alpha helices and why

Answer 30

Glycine- flexibility | Proline- rdigidity

Question 31

3 types of beta sheets:

Answer 31

parallel, antiparallel, mixed

Question 32

How are beta sheets connected?

Answer 32

Beta-turns which consist of proline and glycine

Question 33

Beta turns frequently connect:

Answer 33

antiparallel beta-sheets

Question 34

Motifs aka

Answer 34

super secondary structure

Question 35

What are motifs:

Answer 35

Commonly observed folding motifs comprised of different secondary structures

Question 36

______ have the characteristics of a small compact globular protein that is independent of other ____

Answer 36

Domain(s)

Question 37

Domains can consist of which protein structure type

Answer 37

Tertiary structure

Question 38

4 stabilizing interactions in protein folding

Answer 38

Ionic or electrostatic Hydrogen bonding DIsulfide bonding Hydrophobic interactions

Question 39

Quaternary structures are stabilized by:

Answer 39

non-covalent interactions

Question 40

_____ assist in the proper folding of proteins

Answer 40

Chaperones

Question 41

Mercaptethanol with Urea

Answer 41

Added to protein to break disulfide bonds / unfold protein structure Reversible

Question 42

Abnormal protein in sickle cell anemia

Answer 42

β-globin

Question 43

Abnormal protein in Alzheimers disease

Answer 43

β-amyloid

Question 44

Abnormal protein in CJD/Kuru/Mad cow

Answer 44

Prions

Question 45

Abnormal protein in Huntingtons disease

Answer 45

polyglutamine repeats

Question 46

Abnormal protein in parkinsons disease and Characteristic finding:

Answer 46

α-synuclein | Lewy bodies

Question 47

Abnormal protein in osteogenesis imperfecta

Answer 47

Collagen type I

Question 48

Abnormal protein in Elhers-danlos syndrome

Answer 48

Collagen type III

Question 49

Protein denatruation caused by:

Answer 49

Increasing or decreasing pH Altering ionic strength Increasign temperature Denaturing agents (SDS, Mercaptoethanol, urea)

Question 50

Fibrous protein

Answer 50

Insoluable in water Elongated and ridgid conformation Structural Ex: collagen and elastin

Question 51

Collagen provides ______ strength

Answer 51

Tensile

Question 52

Collagen is comprised of:

Answer 52

Glycine, proline, hydroxyproline and hydroxylysine

Question 53

Parkinsons disease is characterized by a loss of conversion of ________ to ________

Answer 53

DOPA to Dopamine

Question 54

Vitamin C deficiency leads to:

Answer 54

Scurvy - abnormal integrity of connective tissue and skin, leads to easy bruising