Lec 5 - Fibrous Proteins Flashcards
fibrous proteins are the building blocks of blank
ct
enzymes and adaptor proteins that are generally soluble or amphipathic
globular proteins
massive structural proteins
fibrous proteins
fibrous proteins are insolube and composed of blank units
repeating
globular proteins have crosslinks that are all blank
disulfide bonds
fibrous proteins have blank cross links
unique
mutations in coding of collagen, elastin, and keratin causes blank
ct defects
tendons, cartilage, dentin, bone has a lot of
collagen
ligaments and artery walls have a lot of this fibrous protein
elastin
hair, nails, and skin have this type of fibrous protein
keratin
collagen makes up blank of the total protein in mammals
25-35%
each chain of collagen has about blank amino acids
1000
1/3 of all amino acids in collagen
glycine
hemoglobin is globular and only has blank percent glycine
5
percent of collagen that is proline
25%
insuficient vitamin c
scurvy
proline is typically in the blank conformation
trans
proline blank movement
restricts
collagens basic building block is the blank
polyproline helix
proline is what geometrically imposes the shape of the blank
polyproline helix
polyproline helix does not have any blank, instead shape is maintained by steric constraints
hydrogen bonds
higher order structures of collagen does have blank even though it is made of polyproline helices
hydrogen bonding
vitamin c is aka
ascorbic acid
posttranslational modification must take place before formation of blank so the lysine and proline can be accessed by enzymes
triple helix
triple helix formation needs blank to maximize hydrogen bonding
alignment
after secretion, the propeptide sequences at the ends get in the way of blank
getting close together
procollagen peptidases are used to blank
cleave off propeptide ends
after a bunch of triple helix bundles are formed, they should be blank in order to form collagen cross links
staggered
lysyl oxidase is a blank enzyme
copper
cross links involve modification of 1 or 2 blank
lysines
cross links can still be formed if lysine isnt there because there are blank mechanisms
several
elastin structure looks kind of like this kind of globular protein structure
beta turn
repeating units of blank forms the elastin spring
ValProGlyVal
valine contributes to the blank of elastin
insolubility
valine also limits the number of blank to make it easier to stretch out
hydrogen
keratin is mainly for mechanical blank
stability
keratin structure is blank
alpha helix
keratin alpha helices are cross linked by blank and these are blank bonds and can be broken by blank
disulfide, covalent, reduction
10% of residues in keratin may be blank
cysteine
close packing of the helices also make it difficult for blank with reagents
breaking
primary structure differences dictate differences in these structures and functions
secondary, quaternary