Proteins II Flashcards
______ allows folding of long polypeptide chains onto themselves. What fraction of globular protein’s residues does this structure make up?
- Reverse turns
- 1/3
Fibroin in silk has two stacked sheets of interdigitating ___ residues as well as ____/____ residues
- Glycine
- Serine/Alanine
In an alpha-helix:
n= ____ (residues/turn)
p= ____ (anxtrums)
- 3.6
- 5.4
What is the number of rises/residue in an alpha helix?
1.5 Anxtrums
What are the components of a heme group? (2)
- protoporphyrin IX ring
- Iron (Fe2+)
Name the 3 globin folded proteins
- hemoglobin
- myoglobin
- lysozyme
Retinol must be transported via _____ from the liver to peripheral tissues because it is hydrophobic. What structure does this transporter have?
- RBP (Retinol binding protein)
- Beta-Barrel
Disease may occur from ______ replacement of amino acids in a sequence.
Nonconservative
Which protein structure forms when all of the Phi and Psi dihedral angles of a polypeptide adopt the same set of values?
Secondary
Compared to alpha helices, ______ are not stable by themselves, but only when incorporated into sheets. What is their length compared to an alpha helix?
- Beta strands
- longer (more extended)
Name 3 ways Beta-strands can align:
1) Parallel
2) Anti-parallel
3) Mixed
In Beta sheets, how do the side chains project -Above and below the plane of the sheet in order to _________. This allows the sheets to stack.
-minimize steric clash
Reverse turn types I and II differ in the orientation of the ______ linking residues ___ & ___.
- peptide unit
- 2 & 3
______ are located on the surface of proteins and participate in reactions with other molecules. They don’t have regular repeating structure but are well defined structurally.
Loops
Tertiary structure is the folding of secondary elements into a specific, unique 3D structure. Tertiary structure schemes include ______, _______, and _______.
- alpha
- beta
- alpha/beta