Protein Structure and Protein Folding Flashcards
This is formed when elements of secondary structure are connected by turns or regions of less ordered structure called loops or coils.
Supersecondary structure
What are the 4 common motifs of supersecondary structures?
helix-turn-helix, strand-helix-strand
, beta hairpin, Greek hairpin
Supersecondary structure elements combine to form..
domains
There are independently folded regions that often possess a specific function within the protein.
Domains
What aspect of a domain helps to make it stable?
Hydrophobic core
This domain family is mostly amphipathic helices with side chains packed closely together within a hydrophobic core.
a-domain family
What domain family can pack between non-adjacent helices?
a-domain family
What domain family does a horseshoe fold belong in?
a/B family
What domain family would usually fold to form a basket or barrel shaped proteins?
Antiparallel B family
What domain family does a retinol binding protein belong to?
Antiparallel B family
This domain is a small polypeptide chain of 53 amino acids and usually known as an epidermal growth factor
EGF
This domain has 245 amino acids arranged in 2 domains.
Chymotrypsin
These domains have a characteristic pattern of 3 internal disulfide bridges within a region of about 85 amino acid residues.
Kringle domains
Where are proteins made?
Ribosome
Where are the instructions for protein folding embedded in?
Primary amino acid sequence
These interactions are individually weak in proteins, but collectively make a significant contribution to protein conformational stability.
Non covalent interactions
These are proteins that assist other proteins to fold properly during or after protein synthesis.
Chaperone proteins
These are proteins that have misfolded and can cause other proteins to change shape to form aggregates that can cause brain damage.
Prion proteins (proteins infectious agent)
This is the term for an abnormally folded protein.
Amyloid
Alzheimer’s disease and type 2 diabetes are caused by:
Misfolding/aggregation of proteins
Protein folding is directed largely by what?
Internal hydrophobic residues (aka the hydrophobic core) - these residues end up aggregating to form the hydrophobic core.
What is the sequence of events in folding a potein?
1) formation of secondary structures
2) subdomains/supersecondary structures form
3) subdomains come together to form partly folded domain aka a molten globule (which can still rearrange)
4) final domain structure emerges, and small conformational adjustments
