Biochem Flashcards
(443 cards)
Denaturation
Disruption of a protein’s shape without breaking peptide bonds. Proteins are denatured by urea (which disrupts hydrogen bonding interactions), by extremes of pH, by extremes of temperature, and changes in salt conc (tonicity)
Primary Structure
-Order of amino acids bonded to each other in the polypeptide chain. The bond which determines this structure is the peptide bond
Secondary Structure
- Refers to initial folding of a polypeptide chain into shapes stabilized by hydrogen bonds between backbone NH and CO groups
- Motifs: alpha helix and beta pleated sheet
Alpha helices
- Right handed
- 5 angstoms in width with each subsequent amino acid rising 1.5 angstroms
- alpha helix is favorable for hydrophobic transmembrane region because all polar NH and CO groups in the backbone are hydrogen bonded to each other on the inside of the helix and so dont interact with the hydrophobic membrane interior
- They also have hydrophobic R groups which radiate out from the helix interacting with hydrophobic interior of membrane
Beta pleated sheets
- Stabilized by hydrogen bonding between NH and Co groups in the polypeptide backbone
- Hydrogen bonding occurs between residues distant from each other or in separate polypeptide chains
- two types: one with adjacent polypeptide strands running in same direction (parallel beta pleated sheet) and another in which the polypeptide strands run in opposite directions (antiparallel)
Tertiary Structure
Interactions between amino acid residues located more distant from each other in polypeptide chain including: van der waals forces between nonpolar side chains, hydrogen bond bw polar side chains, disulfide bond, electrostatic interactions bw acidic and basic side chains
Hydrophobic Effect
- Folding of secondary structures into tertiary is driven by interactions of R-groups with each other and with solvent (water)
- Hydrophobic R groups tend to fold into interior of protein away from solvent and hydrophilic R-groups tend to be exposed to water on the surface of the protein
- Under right condition, the polypeptide will be spontaneously folded into lowest energy conformation
Quaternary Structure
- Describes interactions between polypeptide subunits; arrangement of subunits in a multisubunit complex
- Forces are the same as tertiary structure but peptide bond is not involved
Subunit
Single polypeptide chain that is part of a large complex containing many subunits
Hydrolase
Hydrolyzes chemical bonds (ATPases, proteases, and others)
Isomerase
rearranges bonds within a molecule to form an isomer
Ligase
forms a chemical bond
Lyase
breaks chemical bond not using oxidation or hydrolysis
Kinase
transfers a phosphate group to a molecule from a high energy carrier such as ATp
oxidoreductase
runs redox reactions
Polymerase
polymerization (addition of nucleotides to leading strand of DNA)
Phosphatase
Removes phosphate group
Phosphorylase
transfers phosphate group to a molecule from inorganic phosphate
Proteasee
Hydrolyzes peptide bonds
Reaction coupling
Thermodynamically unfavorable reactions in cell are driven forward this way. One very favorable reaction is used to drive an unfavorable one
How does ATP hydrolysis drive unfavorable reaction?
Causing a conformational change in a protein. In this way, ATP hydrolysis can be used to power energy-costly events like transmembrane transport. Another example is by transfer of a phosphate group from ATP to a substrate
Enzyme structure
Most enzymes are proteins that must fold into specific 3D structures to act as catalysts. An enzyme may consist of a single polypeptide chain or several polypeptide subunits held together in a quaternary structure to form proper active site
Active site
region in an enzyme’s 3D structure that is directly involved in catalysis
Enzymes more likely to have what shape
Globular