Chapter 3 part 1 Flashcards
What are the characteristics of an amino acid structure?
Has an amino group at the first end, an alpha carbon, an R group, & an alpha carboxyl group
All 20 aa share the same ________________ backbone
Nitrogen-carbon-carbon backbone
What are the two types of covalent bonds between amino acids in proteins?
- Peptide bonds
- Disulfide bonds
Peptide bonds
Links amino acids together into polypeptides chains
Disulfide bridges
Bridges between cysteine R groups
Polypeptides are formed by linking amino acids together in __________ bonds
Peptide
A peptide bond is formed between the ___________ group of one amino acid & the alpha-amino group with the loss of ________
Carboxyl group, water
In a polypeptide chain the ___________ pattern from the amino acid is known as the backbone of the polypeptide
N-C-C-N-C-C (A single amino acid is known as a reisdue)
The ________________ is the 1st end made during polypeptide synthesis& the carboxyl terminus last
Amino acid terminus
The ________________ residues is always written first
Amino terminal
Proteolysis (Proteolytic cleavage)
Hydrolysis of a protein by another protein
Proteolytic enzyme (Protease)
Hydrolysis of a protein by another protein
____________ can form disulfide bonds (sulfur-sulfur bonds) with each other
Cysteines
When cysteine becomes disulfide-bonded to one another its called ___________ instead of cysteine
Cystine
Proteins fold into a unique 3D structure so that it can _____________ properly
function
Denatured proteins
Improperly folded that are non-functional
Denaturation
Refers to the disruption of a protein’s shape without breaking peptide bonds
Proteins are denatured by what conditions?
- Urea- which disrupts hydrogen bonding interactions
- Extreme pH
- Extreme temperature
- Changing salt concentration (tonicity)
Primary (1) structure
Linear sequence of amino acid residues( & peptide bonds determines its structure)
Secondary (2) structure
Contains hydrogen bonds between backbone groups
Secondary structure is the initial folding of a polypeptide chain into shapes stabilized by ____________ bonds between backbone NH & CO groups
Hydrogen bonds
Secondary structure contains what 2 types of motifs?
- Alpha helix
- Beta pleated sheets
Parallel beta pleated sheets
Have adjacent polypeptides strands running in the same direction
Anti-Parallel beta-pleated sheets
Polypeptides strands running in opposite directions
If a single polypeptide folds once & forms a beta-pleated sheet with itself it would be _________________
Antiparallel
Tertiary (3) structures are stabilized by _________________ interactions
hydrophobic/hydrophilic
Secondary structures such as ___________ fold into 3 structures driven by the interation of the R groups with eaxh toeher & water
Alpha helices
In forming the 3 structures the hydrophobic R groups fold into the interior of the protein & the hydrophilic R groups tend to be exposed to water or the surface of the protein and this process is known as what?
Hydrophobic effect
Quaternary (4) structure involves the interactions between polypeptide _________
Subunits