Lecture 4-7 Flashcards
(27 cards)
Essential Amino Acids
Histidine, Isoleucine, Leucine, Lysine, Phenylalanine, Threonine, Tryptophan, Valine
Essential Amino Acids where consumption > production
Arginine, Methionine
Nonessential Amino Acids
Alanine, Asparagine, Aspartic acid, Cysteine, Glutamine, Glutamic acid, Glycine, Proline, Serine
Secondary Synthesis
Tyrosine
What is the only amino acid that can participate in Redox reactions
Cysteine
Proteinogenic Amino Acid
Used to make proteins from the genetic code
Nonproteinogenic Amino Acids
Not decoded from the genome
What is considered the 21st Amino Acid
Selenocysteine
What is Selenocysteine synthesized from
Serine
What is considered the 22nd Amino Acid
Pyrrolysine
What is pyrrolysine synthesized from
Combining 2 lysines
Where is pyrrolysine found
Only in prokaryotes all of which are methanogens
A deficiency in what amino acid causes statin intolerance and how
Selenium- statins inhibit tRNA that form selenocysteine
How are most antibiotics made
Non-ribosomal protein synthesis
Protein Primary structure
A chain of amino acids
Protein Secondary structure
Local folding of the polypeptide chain, connected by hydrogen bonds
Protein Tertiary structure
Folding of the secondary structure, connected by disulfide linkages
Protein Quaternary structure
Interaction of multiple peptides
Non-covalent interactions that govern protein folding stability
Van der Waals- short range repulsion, Hydrogen Bonds, Electrostatic forces
With what elements are Hydrogen bonds possible
Nitrogen, Oxygen, Flourine
What direction turn is more energetically favored in an alpha-helieces
Right-handed or clockwise
How are beta sheets stabilized
Hydrogen bonding between polypeptide strands
What direction can beta sheets run
Parallel and antiparallel
What protein structure serves predominantly in a structural manner
Superhelix
