LAB: EXP 2 (Isolation of Proteins) Flashcards
Proteins are made up of smaller units called _____
amino acids
They are essential for the structure, function, and regulation of the body tissues and organs
Proteins
Amino acids that have an amino group bonded directly to the alpha-carbon are referred to as _____
alpha amino acids
the polar group is a hydroxyl (-OH) bonded to aliphatic hydrocarbon groups
serine and threonine
the hydroxyl group (phenol) is bonded to an aromatic hydrocarbon group
tyrosine
the polar side chain contains a thiol group (-SH)
cysteine
contain amide groups in their side chains
Glutamine and asparagine
Acidic amino acids
Glutamic acid, aspartic acid
Basic amino acids
Histidine, lysine, and arginine
Classification of amino acids according to polarity
- Uncharged non-polar
- Uncharged polar
- Charge polar
Classification of amino acids according to nutritional availability
- Non-essential
- Essential
Amino acids are linked together by ‘amide groups’ called _____.
peptide bonds
During protein synthesis, the carboxyl group of amino acid at the end of the growing polypeptide chain reacts with the amino group of an incoming amino acid, releasing a molecule of _____
water
Amino acid links to another to form a peptide through _____ and _____
peptide bond, condensation
Identify the structure: Sequence of amino acid residues that serves as the backbone of a peptide chain or protein
Primary
Function of the protein depends on the _____ structure
primary
Identify the structure: Regular, repeating folding patterns
secondary
Identify the structure: the “local” ordered structure brought about via H-bonding mainly
secondary
Identify the structure: α-helix & β-pleated sheets
secondary
Identify whether α-helix or β-pleated sheets: Rod-like structure
α-helix
Identify whether α-helix or β-pleated sheets: N-H to C=O
α-helix
Identify whether α-helix or β-pleated sheets: H-bonds in 4th succeeding amino acids
α-helix
Identify whether α-helix or β-pleated sheets: H-bonds parallel to axis
α-helix
Identify whether α-helix or β-pleated sheets: typically amphiphilic
α-helix
Identify whether α-helix or β-pleated sheets: polypeptide chains are arranged side by side
β-pleated sheets
Identify whether α-helix or β-pleated sheets: H-bonds form between chains
β-pleated sheets
Identify whether α-helix or β-pleated sheets: parallel or antiparallel
β-pleated sheets
Identify whether α-helix or β-pleated sheets: more stable
β-pleated sheets
Identify the structure: The way the segments of the protein fold in 3 dimensions
tertiary
Identify the structure: overall folding of domains
tertiary
Identify the structure: specific overall shape of a protein
tertiary
Identify the structure: cross links between R-groups of amino acids
tertiary
Cross links in tertiary structures happen in:
o Disulfide
o Ionic
o Hydrophobic
Identify the structure: Interaction between different polypeptide chains to produce an oligomeric structure
quaternary
Identify the structure: Aggregates of two or more protein chain connected by weak non-covalent interactions
quaternary
Identify the structure: Proteins with two or more chains
quaternary
Yield only amino acids upon hydrolysis
Simple proteins
Simple proteins + non-protein substances
Conjugated proteins
Catalytic protein example
Enzymes