Back of protein page Flashcards
1
Q
Protein conformations
A
Several levels on protein structure
2
Q
Levels of protein structures
A
Primary, Secondary, Tertiary, Quaternary
3
Q
1°(Primary) description
A
- Rarely have a function
- A chain of more than 50 amino aids linked by peptide linkages
- sequence and type of amino acid present varies
4
Q
1°(Primary) Chemical bonding
A
- peptide linkage between the NH2 of one amino acid and the carboxylic acid group of the next amino acid
- No R-group interactions
5
Q
2° (secondary) description
A
- One or more polypeptide chains individually coiled into a helix (called an alpha helix) or a beta-pleated sheet
- Ex. some parts of hemoglobin
6
Q
2° (secondary) chemical bonding
A
Hydrogen bonding and peptide links between the carbonyl and nitrogen of Aino acids that are 5 A.A. units apart
7
Q
Ex. Spiders webs
A
Pleated sheet
8
Q
Ex. Keratin
A
Alpha helix
9
Q
3° (tertiary) Description
A
- The folding of a coiled (helical or folded sheet) polypeptide chain
- curn on a curl
- Ex. hemoglobin
10
Q
3° (tertiary) chemical bonding
A
- hydrophilic and hydrophobic R-groups (ex OH with OH)
- Hydrogen bonding between distance amino acids
- disulfide bridges
- Prosthetic groups
11
Q
Prosthetic groups
A
- Inorganic attachments
- Ex. Heme
12
Q
4° (Quaternary) Description
A
- The assembly of 2 or more folded helical sub-units
- ie. 2 or more different peptide molecules
13
Q
4° (Quaternary) chemical bonding
A
- Hydrophobic interactions
- Hydrogen bonding
- R-group interactions
- Van der waal’s forces (intermolecular forces)
14
Q
Protein Denaturing
A
- Does not necessarily affect peptide bonds
- The unraveling of a portion which could ultimately alter the proteins function
15
Q
Factors that cause denaturing
A
Temperature, pH, Ion Concentration, Presence of other reactive chemicals
