30 Questions
What are proteins primarily composed of?
Amino acids
How many standard amino acids are proteins composed of?
20
What determines the specific function of each protein?
Its unique structure
From how many L-α-amino acids are proteins synthesized?
20
Which biomolecules are regarded as the 'building blocks of proteins'?
Amino acids
What elements are amino acids composed of?
Carbon, Hydrogen, Oxygen, Nitrogen
Which condition results from a child being weaned onto a starchy diet poor in protein in certain regions of West Africa?
Kwashiorkor
What is a characteristic of Marasmus?
Lack of calories and general nutrients
Which amino acids are considered hydrophobic?
Glycine and Alanine
In which part of a protein are hydrophobic amino acids most likely to be found?
Core/Interior
What is the main reason why hydrophobic amino acids are not soluble in water?
Their R groups lack charged atoms to form hydrogen bonds
What is a key characteristic of Kwashiorkor?
Swollen ankles and belly due to edema
How many amino acids are typically linked together in proteins?
100 to 10,000
What type of glycosylation involves the attachment of sugar to a nitrogen atom of an Asparagine residue?
N-linked glycosylation
What is the classification based on the number of amino acids in a chain for dipeptides?
2 amino acids
Which type of amino acid is always in the L-conformation in proteogenic amino acids?
L-amino acids
Which amino acids contain a polar -OH group that can serve as a phosphorylation site?
Ser, Thr, & Tyr
In which type of glycosylation is the sugar molecule attached to an oxygen atom of a Serine or Threonine residue?
O-linked glycosylation
What is the term used for the two non-superimposable/mirror images of molecules with four different groups arranged around the central atom?
Enantiomers
What is the primary role of Ser, Thr, & Tyr amino acids in biological processes?
Phosphorylation sites
Which amino acids are considered nutritionally essential?
Histidine, Leucine, Methionine, Threonine, Valine
Where are D-amino acids found naturally?
Brain tissue and cell walls of some bacteria
Which amino acids are important components of the active sites of enzymes like Chymotrypsin?
Ser, Thr, Tyr
What is the 3-letter abbreviation for Glutamic acid/Glutamate?
Glu
What is the main reason why Glycine is considered very unreactive when incorporated into proteins?
The multiple possible angles of rotation due to its 'fake' R group
Which amino acid contributes greatly to the sharp bends or kinks in the peptide chain of a protein?
Proline
Why is Proline important for the structure of collagen?
Its peculiar structure contributes to the final structure of the protein
Which amino acids are hydrophobic, nutritionally essential, and have a branched hydrocarbon R group?
Leucine & Isoleucine
What is the role of Glycine in the biosynthesis of Ser and heme?
Contributes to the biosynthesis of Ser and heme
Why is Glycine unfavorable in some protein structures?
Because of its optically inactive nature
Learn about the malnutrition conditions in certain regions of West Africa, including Kwashiorkor and Marasmus. Understand the causes, symptoms, and differences between these two conditions.
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