Cell Block 3 flag concepts

Types of amino acids

nonpolar, uncharged polar, acidic, basic

Examples of nonpolar a.a.

Glycine and proline

Examples of uncharged polar a.a.

Serine, threonine, tyrosine, asparagine, glutamine, cysteine

Examples of acidic a.a.

Aspartic acid and Glutamic acid

Examples of basic a.a

lysine, arginine, histidine

Which a.a. participate in H-bonding?

Uncharged polar a.a.

Important physiological peptides and functions

Oxytocin- hormone in contractions,
Bradykinin- vasodilator,
Angiotensin III- vasoconstrictor,
ANP- blood volume and pressure
ADH- water retention
Creatine- energy in muscle,
Melanin- skin pigment,
Gastrin- stimulate HCL and pepsinogen,
Glucagon- keeps BG lvl

Where does protein digestion begin?

In the stomach with HCl (parietal cells) and pepsin (chief cells)

how can proteins be used for energy production?

TCA, glycolysis, GNG, ketogenesis

Protein splicing vs alternative splicing

Intron removal vs generating more protein variability

Protein synthesis location and steps

In cytosol,

1. Activation: aminoacyl-tRNA synthetase
2. Initiation: form ribosome complex
3. Elongation: A-P-E
4. Termination: disassemble complex and free polypep chain

Role of ER and Golgi Apparatus in protein post-translational modification

Protein misfolding correction and modification, protein targeting and sorting

types of post-translational modifications

phosphorylation, glycosylation, methylation, acetylation, hydroxylation, lipidation, trimming

Example of frame shift mutation

Dwarfism in Fleckvieh cattle

Example of splice-site mutation

Golden retriever muscular dystrophy

Causes of protein mutation

Mutagens, heat

Bonds in tertiary structure

hydrogen bonds, ionic bonds, disulfide bonds, hydrophobic interactions

Types of structural proteins and examples

Fibrous (collagen), globular (hemoglobin), intermediate (blood clotting proteins)

Types of composition of proteins

Simple (only a.a.), and conjugated (with non-a.a: prosthetic group)

Fates of newly synthesized protein

Cytosol, vesicle export, organelles

Main physiological functions of enzymes

1. Direct metabolism (enzyme)

2. Permit movement (contractile)

3. Move molecules (transport)

4. Fight infections (antibody)

tryptophan derivative

Serotonin

Taurine derivative

Bile acid

Glutamate derivate

GABA

Histidine derivate

Histamine

Lysine derivative

Carnitine

Tyrosine derivate

T3 & T4, dopamine

example of alpha helix molecule

Alpha keratin- rigid from disulfide bonds

Example of beta sheet molecule

Fibroin (silk)

Storage proteins and examples

Store metal ions and A.A. in cells, ex: ferritin/iron, casein

Amino acid catabolism: what happens to amine part?

1. Transamination: separate amine from carbon skeleton forming glutamate

2. Deamination: glutamate to ammonia - enters urea cycle

Amino acid catabolism: what happens to the carbon skeleton?

Converted into common intermediate for TCA, ketogenesis, GNG

What are proteins produced by cytosolic ribosomes destined for?

Cytosol, nucleus, peroxisomes, mitochondria

ER role in protein folding and maturation

Folding, glycosylation, proteolytic cleavage, lipidation (SRP)

Golgi apparatus role in protein folding and maturation

Folding, glycosylation, transport vesicle formation, package/store proteins, perform PTM

Cis (phosphorylation), medial (O-glycol), trans (package&ship to lysosome, plasma mem, secretion)