Protein Structure- Lecture 8/24/21 Flashcards
R-group
20 unique R-groups that all correlate to an amino acid
Molten globule states
Somewhere in between primary structure and final form, tend to be not water soluble and form aggravates
Specific activity
The amount of activity (As defined by protein function) per amount of protein
Amino acids that absorb at 280 nm
Tyrosine and tryptophan
Alpha helix
Primary structure defined by the helical nature formed by the H-bonds within the backbone, proline is a helix breaker
Helix breaker aa
Proline
Amphipathic
Having both hydrophilic and hydrophobic parts (such as in an alpha helix)
Beta sheet
Secondary structure that orient a.a R groups 180 degrees from each other via H-bonds, can be parallel or anti-parallel
Water solvable protein orientation
Hydrophilic R-groups towards the environment, hydrophobic R-groups toward the center of the protein
CFTR
2 transmembrane domains, 2 nucleotide binding domains, an R domain, allow passage of chloride ions through the plasma membrane
Properties of glycine
Smallest R-group, only a hydrogen. Can fit in small spaces
CFTR mutations
75% had deltaF508, missing phenylalanine, which leads to defective protein and degradation
4-5% have G551D, has less function of the protein
Alkalosis
When your blood pH is too high
Acidosis
When you’re blood pH is too low
Buffers
Conjugat acid/base pairs that resist pH changes
