L7 Nitrogen Structures Flashcards
Proteins and nucleic acids are distinguished by the ______ content in their building block molecules
Nitrogen
Small, specific amines, or subunit/ monomers that build proteins are called:
amino acids
Nitrogen-containing ring structures that chelate a metal ion in the center of the ring, specialized to hold the ion in place without bonding it
amino acids
Amino acids contain: (3)
- NH2 amino group
- Carboxyl group
- R- group (aliphatic or aromatic group)
A polypeptide becomes a protein when:
When it develops into its secondary and tertiary structure by folding
What joins two amino acids?
Amide or peptide bond
Amide/ peptide bond is formed by:
Dehydration synthesis
What is the most abundant molecule in the cytoplasm besides water?
Glutathione, an essential tripeptide and antioxidant molecule
What is glutathione composed of?
3 amino acids: glutamic acid, cysteine, glycine
What is the main function of glutathione in the cytoplasm?
Relieve oxidative stress from cellular processes and toxins
What is the active part in glutathione?
thiol (sulfhydryl) group - SH - is the active oxidant scavenger
How many amino acids are used in making proteins in humans
20
How many essential amino acids are there?
8
In animals, only the _-form enantiomer amino acids and only _- chiral amino acids are incorporated into proteins
L- form enantiomer
a-chiral amino acids
What are the 2 classifications of the 20 amino acids?
- Essential and non-essential
2. Hydrophobic and hydrophilic
What are the properties that give multiple, diverse possibilities for protein conformation? (4)
- Disulfide bridges
- Charged or uncharged molecules
- Hydrogen bonds
- Hydrophobic/ hydrophilic
Cysteine and methionine are _____-containing aminos that are important in protein folding and integrity by forming _____ ______
sulfur; disulfide bridges
Roles protein play in biological systems (7)
- Enzymes
- Structure (connective tissue, skin, collagen)
- Messengers/ hormones/ regulatory molecules (metabolism regulation- insulin and glucagon)
- Transport (hemoglobin, plasmalemma transport and channel proteins
- Movement- tendon, muscle (actin, myosin)
- Defense- immunoglobins, or B-cell mediated (humoral) immunity
- Nutrient storage- milk protein, albumin
A polypeptide produced by a ribosome that is a linear, unfolded chain of a.a. linked with peptide bonds
Primary structure
Polypeptide structure formed by hydrogen bonding between specific a.a.
Secondary structure
This structure folds the polypeptide even further, as disulfide bonds, charge attraction/ repulsions and hydrophobic/hydrophilic attractions are lined up. Most proteins are complete at this stage
Tertiary structure
Polypeptide structures created when 2 or more tertiary proteins form similar weak bonds between each other, creating massive, multi-protein molecules
Quaternary structure
Molecules that will be acted upon by the enzyme
Substrate
Splitting or joining molecules and flipping conformations occur in:
active sites
______ and ______ like ATP, vitamins, ions, and porphyrins are part of or introduced into the active site to facilitate reactivity
coenzymes and cofactors
What catabolizes proteins from food in the stomach and intestines?
Proteases
Enzymes that hydrolyze proteins and release a.a. into the bloodstream via small intestine absorption:
Proteases