Proteins-Higher Orders of structure Flashcards
a-helix
H bonds nearby. Between amide and carbonyl groups.
Disrupted by proline, bulky, like charges
3.6 per turn, 5.4 ang. 6 ang diameter
b-sheet
H bonds NOT nearby.
Parallel (bent,weak)
Antiparallel (straight H bonds, stronger)
Random coil
Irregular arrangement of polypeptide chain
Strong helix formers
Ala and Val
Helix breakers
Pro and Gly
B-turns
180 degrees over 4 AAs.
H bind from carbonyl oxygen to amide proton 3 residues down.
Proline forces turns, glycine present at position 3 often
Domain
Sufficient to perform a chemical or physical task. Tertiary structure
Tertiary and Quarternary structure stabilized by
Hydrophobic, hydrophilic, salt bridges, hydrogen bonds, disulfide bonds
X-ray crystallography
Determine secondary and tertiary structure.
Pros: no size limit
Cons: difficult for membrane proteins, can’t see hydrogen’s
NMR
Determine secondary and tertiary structures.
Pros: can see many hydrogen’s and don’t have to crystallize.
Cons: difficult for insoluble proteins, works best with small proteins
Endosome -lysosomes pathway
Degrades extracellular and surface proteins
Uniquitin-proteasome pathway
Degrades proteins from cytoplasm, nucleus, and ER
Collagen
Fibrous in ECM, holds cells together, provides thermal stability and strength. Adhesion.
Gly-X-Y
Hydroxypro and Lys occur post translation
Adds hydroxyl groups to Pro and Lys in collagen
Metal containing enzymes, happens post translationally
Facilitates intrachain H bonds and stabilizes
Lysyl Oxidase
Catalyze formation of covalent cross links between collagen and elastin. Uses Cu2+