Flashcards in Proteins Deck (43):
4 parts of an amino acid
*all are bonded to common carbon core
1. H - hydrogen atom
2. NH2 - amino functional group
3. COOH - carboxyl functional group
4. a distinctive "R-group"
What happens to amino acids in water?
They ionize due to the pH of 7
What acts as a base in an amino acid?
Amino group (NH2)
What acts as an acid in an amino acid?
Carboxyl group (COOH)
The two highly electronegative oxygens pull the hydrogen away
What makes the amino acids unique?
What happens if an R-group just contains carbon and hydrogen?
They will not participate in many chemical reactions
Polar and electrically charged
Nonpolar R-groups or highly electronegative atoms capable of forming hydrogen bonds with water
Does the R-group have a negative charge?
If yes, it is acidic and will lose a proton
Does the R-group have a positive charge?
If yes, it is basic and will pick up a proton
If the R-group is uncharged, does it have an oxygen atom?
If yes, then the highly electronegative oxygen atom will form a polar covalent bond, thus making it uncharged
also called condensation reactions
newly formed bond results in the loss of water
What type of bond is a peptide bond?
What do peptide bonds occur between?
carboxyl group of one amino acid and the amino group of another amino acid
2 hydrogens from (NH2) react with one oxygen from (COOH) to form the peptide bond
Are peptide bonds stable?
Yes due to the degree of electron sharing
amino acids that are linked together in a chain
R-group orientation in residue
Side chains (R-group) stick out which makes it possible for them to react with eachother and to react with water
What is the directionality of the residue?
N-terminus (amino group) to C-terminus (carboxyl group)
a polymer with fewer than 50 amino acids
a polymer with more than 50 amino acids
refers to the distinct amino acid sequence
R-groups affect chemical reactivity and solubility
distinctively shaped sections that are stabilized by hydrogen bonding that occurs between the oxygen on the C=O group of one amino acid residue and the N-H groups on another
the polypeptide's backbone is coiled
segments of the peptide chain fold in the same plane
rarely found in a-helixes
form using a variety of bonds and interactions between R-groups or between R-groups and the backbone
Types of interactions used for tertiary structures
1. Hydrogen bonding
2. Hydrophobic interactions
3. van de Waals interactions
4. Covalent bonding
5. Ionic bonding
form between polar side chains and opposite partial charges either in the peptide backbone or other R-groups
water molecules force the hydrophobic nonpolar side chains to merge into globular masses
van der Waals interactions
once hydrophobic side chains are close to one another, electrical attractions take place
constant motion of elections produces tiny asymmetry in charge this makes nonpolar molecules slightly attracted to eachother
can form between two cysteines
disulfide bonds create strong links
form between groups that have full and opposing charges
proteins that involve multiple polypeptides
proteins with two polypeptide subunits
groups of multiple proteins that assemble to carry out a particular function
Is folding spontaneous?
It tends to be
How do we know that folding affects function?
Anfinsen studied denatured proteins and found that they could not function
special proteins that can facilitate protein folding
proteins that can be induced to fold into infectious, disease causing agents
shapes are different
Ex: mad cow disease
What are proteins used for?
location where substrates bind to enzyme and react