Amino Acids And Protiens Flashcards
What are the types of amino acids?
Amino acid types include standard amino acids, atypical examples, and L configuration amino acids
Standard amino acids are the 20 common amino acids used in protein synthesis.
What determines the primary structure of a protein?
The linear order of residues in the chain determines the primary structure
For example, the sequence GIGAVLKVLTTGLPALPSWIKRKRQQ represents a 26 residue peptide.
What is the relationship between genetic mutation and natural proteins?
The sequence of natural proteins can change due to genetic mutation, allowing for evolution over time.
How does natural selection affect protein evolution?
Natural selection involves biological experimentation with different amino acid residues as caused by DNA base mutation.
What factors influence the selection of new amino acid residues in proteins?
Selection accepts new residues that are conservative of chemical character and preserving of accurate chain folding.
Describe the protein chain folding process.
- Initial formation of sections of secondary structure
- Packing together of secondary structures to form stable domains
- Final docking together of the domains and/or other subunits.
What bond has restricted rotation in protein structure?
Peptide bond has restricted rotation.
What does the Ramachandran Plot represent?
The Ramachandran Plot predicts favored angle combinations of rotation in protein structures.
What stabilizes the α-helix structure?
Hydrogen bonds between amide linkages stabilize α-helix.
What characterizes the β-structure in proteins?
Two antiparallel β strands with hydrogen bonds between peptide linkages.
What influences the choice of helix, sheet, or turn conformation in proteins?
The local sequence of side chains influences the choice of conformation.
Fill in the blank: The preferences for secondary structure types can be computed for all _____ types of amino acid.
20
What is the significance of tertiary structure stabilizing forces?
They maintain a hydrophobic core and involve charged residues, hydrogen bonding, and disulfide bridges.
What role do disulfide bridges play in protein structure?
Disulfide bridges act as covalent ‘staples’ that stabilize tertiary structures.
True or False: Protein structures are static and do not change.
False
What is the quaternary structure of a protein?
The arrangement of multiple subunits in a protein, such as in a transmembrane channel.
What challenges exist in predicting protein 3D structure without experimentation?
Prediction is challenging due to the complexity of protein folding and the expense of experimentation.
What are prosthetic groups?
Molecules required for special chemical properties that amino acid residues cannot deliver, including:
* Metal ions
* Nucleotides
* Flavins
* Phosphates
* Porphyrins
What characterizes the primary structure of collagen?
Collagen has three helical wound chains and modified amino acid residues.
What is the role of zinc in carboxypeptidase A?
Zinc acts as a cofactor required for the enzyme’s function.
What is the significance of the Michaelis-Menten equation?
It describes the rate of enzymatic reactions and the relationship between substrate concentration and reaction velocity.
Fill in the blank: Km is the concentration of substrate at which half maximal _____ is observed.
velocity
What does a low Km indicate about substrate binding?
A low Km indicates tight binding of the substrate.
