Cell & Molecular Biology Test 1 Save Groups
Prade
Terms in this set (89)
4.3 What are the four weak non-covalent Ionic bonds
interactions that determine the conformation Hydrophobic interactions
of a protein? Hydrogen bonds
Van Der Waals forces (dispersion attractions, dipole
moments).
4.4 What are the major properties that Their R groups.
distinguish different amino acids from one Some are basic, acidic, hydrophobic, hydrophilic, and polar.
another? What roles do these differences play These groups interact in many different ways with each other
in the structure and function of protein? chemically and twist and fold the polypeptide structure into
a mature protein. Form dictates function in proteins.
4.5 When proteins denature and renatured, When a protein is denatured (by pH, temp) it loses its side
some fully recover its original conformation chain conformation. When it is renatured, the protein will
and function, and others partially renature and fold back to its original shape. If it renatures and is
remain functionally inactive. Why is this functionally inactive, it is because that protein uses a special
happening? group (heme, iron, copper, manganese) in its binding site
which will not return when the protein is renatured.
4.6 What is a molecular chaperone? Why are Proteins that assist the non-covalent folding or unfolding
they important in the crowded cytoplasm? and the assembly or disassembly of other macromolecular
structures.
Crowding can accelerate the folding process. Also can
reduce the yield of correctly-folded protein by increasing
protein aggregation. Crowding could increase the
effectiveness of the chaperone protein.
4.7 Protein structure is dictated by the amino Will not have the same structure.
acid sequence. Should a protein, in which the Polarity of the molecule changes because the N and C
order of all amino acids is reversed, (ABC- terminus changes. So the protein will be read differently.
>CBA) have the same structure as the original
protein? Explain with supporting information.
, 4.8 Explain how it is possible that living cells There are an enormous amount of amino acids and
contain such an enormously diverse, but combinations of them.
structurally stable, set of proteins? How is Function and specificity: structure. amino acid sequence.
function and specificity determined in
proteins?
4.9 Use a rough diagram to compare the
structure of a protein a-helix and an anti-
parallel B-sheet. For simplicity, show only the
backbone atoms of the protein.
4.10 What common feature of alpha helices The makeup of backbone structure makes it possible for the
and beta sheets makes them universal building protein to fold and form hydrogen bonds with other parts of
blocks for proteins? the backbone structure, causing it to form a-helixes and B-
sheets. Since the backbone atoms are universal throughout
proteins, this makes them always form these structures.
4.11 Why do you suppose that only L-amino L-amino acids are more stable.
acids and not a random mixture of L- and D- D-amino acids are toxic because they have the H is in the
amino acids are used to make proteins? wrong positions.
L and D have opposite stereochemistry.
4.12 Explain the coiled coil protein structure. Repeated pattern of hydrophobic and charged amino acid
residues.
4.13 What do we mean by primary, secondary, Primary: amino acid sequence of the polypeptide chain. Held
tertiary, and quaternary structure of proteins? together by covalent and peptide bonds.
•Secondary: highly regular local sub-structures. (alpha helix
and beta strand). Patterns of hydrogen bonds between the
main-chain peptide groups.
•Tertiary: 3-dimensional structure of a single protein
molecule. the folding of the protein driven by the
hydrophobic interactions.
•Quaternary: larger assembly of several protein molecules.
Polypeptide chains.
4.14 The protein structure in the Figure below
contains four a-helices arranged in a bundle.
Label each helix by number (1 to 4) starting
going from the N terminus to the C terminus.
Prade
Terms in this set (89)
4.3 What are the four weak non-covalent Ionic bonds
interactions that determine the conformation Hydrophobic interactions
of a protein? Hydrogen bonds
Van Der Waals forces (dispersion attractions, dipole
moments).
4.4 What are the major properties that Their R groups.
distinguish different amino acids from one Some are basic, acidic, hydrophobic, hydrophilic, and polar.
another? What roles do these differences play These groups interact in many different ways with each other
in the structure and function of protein? chemically and twist and fold the polypeptide structure into
a mature protein. Form dictates function in proteins.
4.5 When proteins denature and renatured, When a protein is denatured (by pH, temp) it loses its side
some fully recover its original conformation chain conformation. When it is renatured, the protein will
and function, and others partially renature and fold back to its original shape. If it renatures and is
remain functionally inactive. Why is this functionally inactive, it is because that protein uses a special
happening? group (heme, iron, copper, manganese) in its binding site
which will not return when the protein is renatured.
4.6 What is a molecular chaperone? Why are Proteins that assist the non-covalent folding or unfolding
they important in the crowded cytoplasm? and the assembly or disassembly of other macromolecular
structures.
Crowding can accelerate the folding process. Also can
reduce the yield of correctly-folded protein by increasing
protein aggregation. Crowding could increase the
effectiveness of the chaperone protein.
4.7 Protein structure is dictated by the amino Will not have the same structure.
acid sequence. Should a protein, in which the Polarity of the molecule changes because the N and C
order of all amino acids is reversed, (ABC- terminus changes. So the protein will be read differently.
>CBA) have the same structure as the original
protein? Explain with supporting information.
, 4.8 Explain how it is possible that living cells There are an enormous amount of amino acids and
contain such an enormously diverse, but combinations of them.
structurally stable, set of proteins? How is Function and specificity: structure. amino acid sequence.
function and specificity determined in
proteins?
4.9 Use a rough diagram to compare the
structure of a protein a-helix and an anti-
parallel B-sheet. For simplicity, show only the
backbone atoms of the protein.
4.10 What common feature of alpha helices The makeup of backbone structure makes it possible for the
and beta sheets makes them universal building protein to fold and form hydrogen bonds with other parts of
blocks for proteins? the backbone structure, causing it to form a-helixes and B-
sheets. Since the backbone atoms are universal throughout
proteins, this makes them always form these structures.
4.11 Why do you suppose that only L-amino L-amino acids are more stable.
acids and not a random mixture of L- and D- D-amino acids are toxic because they have the H is in the
amino acids are used to make proteins? wrong positions.
L and D have opposite stereochemistry.
4.12 Explain the coiled coil protein structure. Repeated pattern of hydrophobic and charged amino acid
residues.
4.13 What do we mean by primary, secondary, Primary: amino acid sequence of the polypeptide chain. Held
tertiary, and quaternary structure of proteins? together by covalent and peptide bonds.
•Secondary: highly regular local sub-structures. (alpha helix
and beta strand). Patterns of hydrogen bonds between the
main-chain peptide groups.
•Tertiary: 3-dimensional structure of a single protein
molecule. the folding of the protein driven by the
hydrophobic interactions.
•Quaternary: larger assembly of several protein molecules.
Polypeptide chains.
4.14 The protein structure in the Figure below
contains four a-helices arranged in a bundle.
Label each helix by number (1 to 4) starting
going from the N terminus to the C terminus.
