CT 3 part 2 Flashcards
tf Ehlers-Danlos Syndrome, has inc crossliking of collagen
F
lowered
Poor wound healing
and Musculoskeletal deformities
Ehler danslos
Hyp
CANNOT be incorporated into a growing polypeptide chain so addition of [14C] Hyp will not result in formation of [14C] collagen
Proline and hydroxyproline are both radioactive but
Hyp CANNOT be incorporated into a growing polypeptide chain
Unique to collagens;
Unique to collagens; glycosylated hydroxylysyl residues
2 types of O linked glycosylations
serine and 5 hydroxylysine
asparagine
N glycosyl Linkage
glycosylations of
glucose and galactose
After post-translational modification, the 3 polypeptides associate to form the procollagen molecule.
After post-translational modification, the 3 polypeptides associate to form the procollagen (Type I procollagen) molecule.
where is procollagen made
in the ER lumen
Extension peptides
help guide the formation of the triple helix.
Each polypeptide is —- through a large portion of the molecule and stabilized partly by —— of the pyrrolidone rings of proline.
Each polypeptide is helical through a large portion of the molecule and stabilized partly by steric repulsion of the pyrrolidone rings of proline.
3 polypeptides (Pro α Chains) wind around each other to form a —- —–, with —— bonds between individual chains
3 polypeptides (Pro α Chains) wind around each other to form a —- —–, with —— bonds between individual chains
procollagen
Residues in each chain are —— staggered such that a gly, an X and a Y from ——chains are on the same level along the helix axis.
Residues in each chain are vertically staggered such that a gly, an X and a Y from different chains are on the same level along the helix axis.
procollagen
stiff cable
H-bonds form between —- and —- in procollagen
H-bonds form between the N-H of Gly and O in procollagen
procollagen C terminal
disulfide linkage
cooperative interactions
determines stability of collagen molecules
-NH of Gly and the C=O of second residue in triplet of neighboring chain
have a h bond
Gly as every third amino acid
Hyp content
Total imino acid content
determine stability of collagen molecule
inc temp
collagen loses its rodlike shape, the viscosity of the solution drops
helical structure destroyed
after TM
collagen is a random coil
Tm is the temperature at
temperature at which 1/2 of the helical structure is lost
