PROTEINS PT 1 Flashcards
Greek word of Proteins
Proteus
stabilizing thick filament of your muscles
Titin
proteins in saliva
salivary amylase
building blocks of proteins
alpha amino acids
Alpha amino acids have a _____ carbon, except for ______
chiral, glycine
Oxytocin, the smallest known protein has how many amino acids?
9 AAs
Titin has how many amino acids?
25,000 AAs
Acidic Amino Acids examples
Aspartic Acid, Glutamine
They are negatively charged and release proton
Polar Acidic Amino Acids
positively charged at physiologic pH, accept proton
Polar Basic Amino Acids
3 examples of polar basic AAs
Histidine, Lysine, Arginine
cannot be synthesized by the body, get from diet
Essential Amino acids
is both essential because babies need to eat it and is also non-essential
Arginine
have all essential amino acids in amounts as needed by the human body
complete dietary proteins
very good protein alternative for vegans because it has a complete protein substitute
soy
only eat beans = kulang ng ?
methionine and tryptophan
only eat rice and oats = kulang ng ?
lysine
only eat corn
lysine and tryptophan
only eat peas = kulang ng ?
methionine
almonds and walnuts = kulang ng?
lysine and tryptophan
Dipeptides have how many AAs?
2 AAs
Oligopeptides have how many AAs?
3 - 10 AAs (Tripeptide and T peptide)
How many AAs are there in Polypeptides?
11-100 AAs
In naming Glutamate, it becomes?
Glutamyl
In naming Glutamine, it becomes?
Glutaminyl
In naming valine, it becomes
Valinyl
structure where peptide bonds attach the a-amino group of one to the a-carbonyl group of another
Primary Protein Structure
folding of short (3-30 AA residues) sequences of polypeptides into geometrically ordered units
Secondary Protein Structure
type of Secondary Protein Structure that is the most common (Keratin is made up of 100% of these), spiral in shape, side chains are oriented outwards, and is 3.6 Amino Acids per term
Alpha Helix/ Helices
This type of secondary structure forms a zigzag or pleated pattern, can be parallel or anti-parallel, and are found in antibodies (immunoglobulins)
Beta Sheets
Shape of Tertiary structures and what are they stabilized by?
- 3D structure of the protein
- stablized by:
1. Hydrophobic clustering forces
2. Disulfide bridges (Cystine)
3. Hydrogen bonds
4. Ionic interactions / salt bridges
5. Van der waals forces
Molecular chaperones assist in what?
assist in protein folding but are NOT the determinants of the final structure
this structure has 2 or more polypeptide chains forming one macromolecule
Quaternary Structure
Hemoglobin is an example of a quaternary structure because it has how many polypeptide chains?
Hemoglobin has 4 polypeptide chains:
alpha 1 and 2, beta 1 and 2
any protein that’s composed of more than one polypeptide chain is called?
Multimeric protein
these type of proteins are called ‘enzymes’ because they are the biologic catalysts in the body; one example is Pepsin
Catalysic Proteins
These type of proteins defend organisms against external agents of disease
Proteins with Immune Functions
One example of Transport Proteins that transport ferric/ iron ions
Transferric
What is the function of Messenger Proteins?
they give instructions to parts of the body (not all hormones are proteins)
Examples of Structural proteins
keratin and collagen
examples of movement proteins
myosin and actin
examples of Nutrient Proteins and what food they’re found in
Casein - milk
Albumin - eggs
Examples of Storage Proteins
myoglobin, hemoglobin, and ferritin (iron storage)
these proteins influence transcription from DNA to RNA and can either prevent or activate transcription
Regulatory Proteins