Term
| What nonvoalent interaction stabilize the higher levels of protein structures? |
|
Definition
hb
hydrophobic inter
electrostatic bond
vander walls |
|
|
Term
| how Hydrogens bonds related to protein structure |
|
Definition
peptide backbone tend to form hydrogen bonds with one another
like C-->NH
H bond stabalizes protein |
|
|
Term
side chains capable of forming H bonds usually located where? |
|
Definition
water solvent or within surface residues
interior provides increased stabilization |
|
|
Term
| describe Hydrophobic reactions to protein |
|
Definition
| Hydrophib interactions DRIVE protein folding- formation of hydrophpib c bonds" minimizes the interaction of nonpolar residues with water and is HIGHLY favorable" |
|
|
Term
| ioni interaction (electriconic interaction) usually occurs where on protein? |
|
Definition
protein surfaces- it is energetically unfavorable for an ionized residue to be located in the hydrophobic core of the protein
|
|
|
Term
| functions of vander walls in protein |
|
Definition
| through increased number it plays a powerful role in stabalizaiton of protein |
|
|
Term
|
Definition
|
|
Term
| how are proteins classed? |
|
Definition
|
|
Term
| 4 levels of protein sructure |
|
Definition
primary
secondary- H bonds
teriary- 3D
Quaternary- true protein |
|
|
Term
|
Definition
globular/ or fibrous
fat guy or skinny guy= glob or fibr |
|
|
Term
| describe fibrous shape of protein |
|
Definition
relatively simple, regular linear, tend to have structural roles in cells
"house made of hay" |
|
|
Term
describe globular proteins shapes
functions characteristics |
|
Definition
spherical in shape
usually hydrophobic interior, hydrophillic exterior |
|
|
Term
descbe characteristics of primary structure of proteins in its amino acid sequence numbered from its N terminus
|
|
Definition
| linear array of AA in its amino acid sequence numbered from its N terminusto C terminus |
|
|
Term
| how are primary proteins numbered |
|
Definition
| in its amino acid sequence numbered from its N terminus |
|
|
Term
characteristic of secondary structure (2)
what is the force being secondary how does it function in secondary proteins, |
|
Definition
| secondary structures are formed through Hydrogen bonding interactions between adjacent amino acid residues |
|
|
Term
secondary proteins polypeptide chains can arrange itself into what 2 forms
secondary for 2, meaning 2 forms |
|
Definition
| helical or pleaded segments |
|
|
Term
| characteristics of tertiary structure, how does it's form in tertiary help its structure |
|
Definition
| globular shape, minimizes the proteins interactions with enviroment, inorder to take on its quat shape |
|
|
Term
| characteristics of quarternery structure, what provides its form |
|
Definition
a aggregation of multiple polypeptides- aggreations of these structures are called subunits
last hierarchy
known as "PROTEIN" |
|
|
Term
|
Definition
| aggregation of more than one polypeptide that has aggregated together |
|
|
Term
| what drives the formation of higher order protein sturcture |
|
Definition
NON-covalent forces drive formation of higher order proteins
- vander walls
-electrostatic
- hydrogen bonding
-hydrophobic interactions
not just hydrophobic |
|
|
Term
| all the information necessary for a protein molecule to achieve its intracte form is contained in which of the 4 phases? |
|
Definition
|
|
