lecture 21 - fibrous proteins & alpha keratin Flashcards
explain the structure of fibrous proteins
- usually composed of one type of secondary structure that doesn’t fold up
- thus, secondary structure = tertiary structure
- which results in an extended shape
fibrous proteins are usually composed of many hydrophobic residues, T or F? why?
- true
- allows for the formation of quaternary structure
how does the tertiary structure of fibrous proteins form?
- multiple polypeptide chains pack together to form an ordered array (bc hydrophobic)
- this results in the formation of larger supramolecular structures
are fibrous proteins rigid or flexible?
- can be either
- depends on function
what are the primary functions of fibrous proteins?
- support (CT)
- provide force/shape (muscle)
- protection (skin/nails/horns)
define alpha keratin
- family of proteins that are a component of hair, nails and horns
- differentiated to these areas by the sequence and structural features
explain the primary structure of alpha keratin
- heptad repeat (a-b-c-d-e-f-g)n
- where ‘a’ and ‘d’ are typically hydrophobic
explain the secondary structure of alpha keratin
slightly distorted alpha helix:
-normal = 3.6 res/turn and 5.4 A pitch
-keratin = 3.5 res/turn and 5.1 A pitch
(causes a slight turn in the helix)
explain the tertiary structure of alpha keratin
single alpha helix
explain the quaternary structure of alpha keratin
- 2 supertwisted alpha helices intertwined (each one wraps around the other)
- interface of Z helices formed by the ‘a’ and ‘d’ residues of the heptad repeat
- results in the potential to form salt bridges between ‘e’ and ‘g’
- residues ‘b’, ‘c’ and ‘f’ may be more polar and can interact favouably with the solvent
are amino acid sequences different for each member of tha alpha keratin family? what does this mean?
- yes
- hair will have diff aa and structure than nails
- which affects function
if we had an alpha-helical coiled coil with a pitch of 400A, ~88 helical turns and ~300 aa residues, what would be the result?
coiled coils associate to form supramolecular structures
what is a key component to alpha keratin proteins?
their flexibility due to their structure
what are the important features of alpha keratin for hair?
- contains cys residues
- allows u to get a perm which is where you reduce cys-cys bonds to cys-SH bonds resulting in curly hair
- can reoxidize cys to form disulphide bonds
what are the important features of alpha keratin for nails?
it contains aa sequence features that enhance the rigidity of supramolecular structures