Explore the fundamentals of protein structure in the CH4 Biochem Bashar khatib quiz. Assess your understanding of disulfide bonds, collagen properties, protein folding, and more, enhancing your skills in biochemistry and molecular biology.
True
False
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Imidazole
Methine bridges
Ferrous iron
His F8
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In vivo it establishes an equilibrium between two or more active conformations
It has more than fifty amino acids.
The active protein involves the association of two or more polypeptide chains
The proteins has multiple α-helices.
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Strong electrostatic repulsion
Crowding
Presence of proline amino acid
Steric repulsion
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Hydrophobic bonds
Metal ion interactionsÂ
H-bonds
Electrostatic bonds
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Has a single equilibrium constant for oxygen binding
binds more oxygen after the initial proteins first bind oxygen
Shows cooperativity.
Binds up to four molecules of oxygen
All of the above
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Collagen is considered a fibrous protein
30% of the amino acids in the collagen are Pro and Hyp
Every second position in the sequence of amino acids in collagen fiber must be Gly
Each polypeptide chain in collagen fiber is a helix
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B-mercaptoethanol
Detergents by SDS
High or low PH
Urea or guanidine
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Hb F has no affinity to O2.
There is a His amino acid in position 143 in gamma chain in Hb F.
BPG can bind to Hb F.
There is a substitution between His and Ser amino acid in gamma chain in Hb F.
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True
False
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 minimal configuration
Native conformation
Primary structure
Most stable enantiomer
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Domain
Modules
Reverse turn
Electrostatic interaction
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Carbon dioxide.
2,3 BPG
Protons.
All of the above.
A and B above
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Its tertiary structure is likely stabilized by the interactions of amino acid side chains in non-neighboring regions of the polypeptide chain
It could contain α-helices that are stabilized my hydrogen bonding.
It likely has extensive quaternary structure to maintain its globular shape.
Non-covalent forces are the primary source of stability for the secondary and tertiary structure.
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