polypeptides Flashcards
(38 cards)
is amide linkage formed by the reaction between α-carboxyl group of one amino acid and α-amino group of another amino acid with the elimination of water molecule
Peptide (peptide bond)
two amino acids are combined
Dipeptide
3 to 10 amino acids combined
Oligopeptide
> 10 amino acids combined
Polypeptide
300-1000 amino acids combined
Proteins
There are four levels of protein structure:
primary
secondary
tertiary
quarternary
linear sequence of amino acids
primary
regular patterns formed by primary structure folding
secondary
completely folded polypeptide with one or more domains
tertiary
association of multiple polypeptides; not found in all proteins
quaternary
The simplest level of protein structure is simply the amino acid sequence within a polypeptide chain.
the primary structure
Understanding the ??? is important because many genetic diseases results in protein with abnormal amino acid sequences
primary structure of proteins
is local interactions between stretches of a polypeptide chain and includes α-helix and β-pleated sheets structures.
Secondary structure
is primarily due to interactions between the R groups of amino acid which make up the protein.
The tertiary structure
R group interactions (4)
§ hydrogen bonding
§ ionic bonding
§ dipole-dipole interactions
§ London dispersion forces
are also important for the tertiary structure, in which amino acids with non-polar, hydrophobic R groups cluster together within the protein, leaving hydrophilic amino acids outside to interact with surrounding water molecules.
Hydrophobic interactions
One specific form of covalent bond may contribute to tertiary structure: the
disulfide bond
Many proteins however consist of several polypeptide chains, also known as ???
subunits
They give the protein its quaternary form, as these subunits come together.
subunits
One example of a ???
is hemoglobin.
quaternary-structured protein
In general, the same types of interactions that lead to tertiary structure also hold the
subunits together to give ???
quaternary structure
interactions that lead to tertiary structures are mostly ???
weak interactions,
such as hydrogen bonding and dispersion forces in London
??? protein structure;
??? bonding of the peptide backbone causes amino acids to fold into a ??? pattern
secondary;
hydrogen;
repeating
tertiary protein structure:
3-D folding pattern of a protein due to ??? interactions
side chain interactions