Unit 6: Protein; Amino Acids Flashcards
Define Amino Acid
The nitrogen atoms give the name amino (nitrogen containing) to the amino acids–links in the chains of proteins
Describe the basic structure of an amino acid
- Central carbon with a Hydrogen atom
- Amino group (NH2)
- Acid group (COOH)
- Unique R-side group
What distinguishes one amino acid from the next? Makes proteins more complex than lipids or carbohydrates.
Unique R-side group
Define Protein
Cells link amino acids end-to-end in a variety of sequences to form thousands of different proteins.
Approximately how many amino acids make up a protein?
20
What links amino acids together to form a protein?
Peptide bonds
Describe a Peptide bond
-Condensation reaction (produces H2O)
Two amino acids bonded form a?
Dipeptide
3 amino acids bonded together form a?
Tripeptide
More than 3 amino acids bonded together form a?
Polypeptide
Amino Acid Sequence–Primary structure is determined how?
By the sequence of amino acids, to form a chain
Polypeptide Shapes-Secondary Structure is determined how?
By the weak electrical attractions within the polypeptide chain. Positively charged hydrogens attract negatively charged oxygens and the chain twists to a helix or a pleated sheet
What does secondary structure (helix/pleated sheet) do for protein?
Provides strength and rigidity
Polypeptide Tangles-Tertiary Structure are determined how?
Occurs has long polypeptide chains twist/fold into complex tangled shapes. Unique side groups give characteristics that attract or replenish from surrounding fluids and other amino acids
Hydrophobic
Hydrophilic
Disulphides bridges
For shapes such as globular/spherical or linear structures
What does the tertiary structure do for protein?
- Enable them to perform various tasks
- Give maximum stability and shape must be retained to remain functional
Define Hydrophillic
Attracted to water
Define Hydrophobic
Repelled by water
Multiple Polypeptide Interactions-Quaternary Structure is determined by what?
Involves interactions between 2 or more polypeptides. Form a functional protein
Define Denaturation
Protein subject to heat, acid, (other conditions to disturb stability) uncoil and lose their shape. Therefore, their ability to function. Past a certain point denaturation is irreversible. Proteins are denatured when exposed to stomach acid allowing them to be digestible
Nonessential (Dispensable) Amino Acids: can be synthesized by the body. What are they?
Alanine Asparagine Aspartic Acid Glutamic Acid Serine
Essential (Indispensable) Amino Acids: (9) must be supplied by the diet, as the body cannot synthesize/adequately synthesize them. What are they?
Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Threonine Tryptophan Valine
Conditionally Essential Amino Acids: are sometimes nonessential but become essential under special circumstances. What are they?
Arginine Cysteine Glutamine Glycine Proline Tyrosine
Protein digestion in the mouth
Chewing and crushing moisten protein-rich foods and mix them with saliva
Protein Digestion in the Stomach
Hydrochloric acid (HCl) uncoils protein strands and activates stomach enzymes
Protein –> Pepsin, HCl –> Smaller polypeptides
Protein digestion in the Small Intestine
Pancreatic and small intestinal enzymes split polypeptides further
Polypeptides –> Pancreatic/Intestinal Protease –> Tripeptides, dipeptides and amino acids
Enzymes on the surface of the small intestinal cells hydrolyze these peptides and the cells absorb them
Peptides –> Intestinal tripeptidases/Dipeptidases –> Amino Acids (absorbed)
Only free amino acids enter the general blood circulation at the portal vein. What is an exception to this?
Newborn infants receive immunity from mother’s when intact protein antibodies present in human colostrum enter the mucosa. A few days after birth the mucosal cells are closed to whole proteins
Digestive enzymes in the stomach are? (2)
Hydrochloric Acid (HCl): denatures protein structure, activates Pepsinogen to pepsin
Pepsin: C;eaves proteins to smaller polypeptides and some free amino acids. Inhibits pepsinogen synthesis
A proenzyme (or zymogen) is the inactive form of an enzyme. What is the inactive form of pepsin?
Pepsinogen
A string of 4-9 amino acids is known as a?
Oligopeptide
Pepsin works best in the low pH of the stomach. When it enters to small intestine (higher pH) what happens?
Becomes inactive and is digested
Once inside intestinal cells amino acids are used for? If they are not used for this what happens?
-Energy
-Synthesize needed compounds
If not used for this:
-Transported across cell membrane into surrounding fluid where they enter the capillaries on their way to the liver