1
2
3
4
5
100
draw an alpha amino acid
what groups ?
this AA has Hydrogen as a R group
100
Two functional groups that are present in all amino acids are the ________ group and the ________ group
carboxyl; amine
100
Which of these amino acids has a thiol group as part of its side chain?
cysteine
100
draw a zwitterion
100
The isoelectric point of an amino acid is
the pH at which it exists in the zwitterion form.
200
Which amino acid is not chiral?
glycine
H as R group
200
The amino acid sequence of a protein is known as its
primary structure.
200
The tripeptide represented as ala-leu-gly is named
alanine-leucine-glycine.
200
The N-terminal amino acid in the peptide ala-leu-gly-his-pro is
alanine
200
The C-terminal amino acid in the peptide ala-leu-gly-his-pro is
proline
300
How many different tripeptides can be formed from one molecule each of the amino acids tyrosine, valine, and alanine?
6
300
he two protein chains in insulin are held together by ________.
disulfide linkages
300
non-covalent interactions important in maintaining the secondary, tertiary, and quaternary aspects of amino acids
(4)
hydrogen bonding along the backbone.
hydrophobic interactions between R groups.
hydrogen bonding between R groups.
salt bridges between R groups.
300
what type of interaction would this amino acid have?
this is arginine
basic (positively charged) and hydrophilic amino acid. Because of the unique structure of its side chain, it can participate in several distinct types of molecular and biochemical interactions
300
examples of fibrous protein
wool
skin
bones
fingernails
----structural...
400
what is a globular proteins, give an example
a type of protein that is roughly spherical or globe-shaped, compact, and generally soluble in water.
albumin
hemoglobin
immunoglobulin
400
Which type of interaction is not directly involved in maintaining tertiary structure?
peptide bonds
400
Proteins that consist of two or more chains assembled into a large 3-dimensional structure are said to display
quaternary structure.
400
When a protein is ________, its primary structure is destroyed, thus destroying the other aspects of its structure.
hydrolyzed
400
When a protein is ________, its primary structure is maintained, but other aspects of its structure are disrupted.
what can cause this?
denatured
heat, pH, mechanical agitation....
500
When a glycoprotein is hydrolyzed, the products would include
amino acids plus carbohydrates
500
a protein that is usually water soluble, having a hydrophilic exterior and hydrophobic interior, and an overall rounded shape
globular protein
500
the form of an amino acid in which both the carboxyl group and the amine group are charged, but the overall molecule remains neutral
zwitterion
500
a carbon atom bonded to four different groups and therefore able to form enantiomers
chiral carbon
500
simple protein vs. native protein
simple: When broken down (hydrolyzed), a simple protein yields only amino acids
native: A native protein is classified by its physical and functional shape. It refers to a protein in its natural, fully folded, and biologically active three-dimensional state as it exists inside a living cell or organism