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WorksheetsBiochem (Lec)
Total questions: 51
Worksheet time: 1hrs 5mins
the continual degradation and synthesizing of protein
Protein Synthesis
Protein Digestion
Protein turnover
Results from a severe deficiency in kilocalories
Marasmus
Amino Acid Metabolism
Marasmic Kwashiorkor
Consuming too much protein from animal sources increase saturated fat intake
True
False
PEM is not caused by inadequate protein and/or kilocalorie intake
True
False
Severe protein deficiency
Marasmus
Kwashiorkor
distinct in structure compared to other amino acids because its amino group is cyclical
central carbon atom
carboxyl group
Proline
Indole ring side chain, aromatic
Trp
Phe
Met
hydrocarbon aromatic ring
Trp
Phe
Met
Sulfur atom in side chain
Trp
Phe
Met
The side chain imidazole group of histidine is a Heterocyclic aromatic amine
Guanidine Group
Imidazole Group
carboxyl group
In amino acid, carboxyl group (-) and amino group (+) are charged at neutral pH.
True
False
The three-dimensional form of the antiparallel b-pleated sheet arrangement. The chains do fold back on each other but are in a fully extended conformation
True
False
a repetitive supersecondary structure formed when an antiparallel sheet doubles back on itself
ᵦ-meander
ᵦαᵦ unit
Greek key
created when ᵦ-sheets are extensive enough to fold back on themselves
Greek key
ᵦ-barrel
ᵦ-meander
an antiparallel sheet formed by a series of tight reverse turns connecting stretches of a polypeptide chain
ᵦ-meander
Greek key
ᵦαᵦ unit
the polypeptide backbone coils around an imaginary helix axis in clockwise direction
Alpha helix
Secondary structure
Disulfide (-S-S-) bonds between side chains of cysteines
Supersecondary Structures
Covalent interactions
Secondary structure
Hydrogen bonding between polar side chains (e.g., Ser and Thr)
Noncovalent interactions
Tertiary (3°) structure
The Triple Helix of collagen
the association of polypepetide monomers into multisubunit proteins. Some common multi-subunits include:
(a)
proteins which are folded to a more or less spherical shape
Fibrous Proteins
Globular proteins
Proteins that do not fold correctly may interact with other proteins in an undesired manner and aggregates may result.
True
False
In the protein-dense environment of a cell, proteins may not begin to fold incorrectly or may associate with other proteins before folding is completed
True
False
Hydrophobic interactions are major factors in protein folding
True
False
contain polypeptide chains organized approximately parallel along a single axis
Globular proteins
Fibrous Proteins
the arrangement in space of all atoms in a polypeptide chain
Tertiary (3°) structure
Quaternary 4˚ structure
arrangement of monomer subunits with respect to each other
Tertiary (3°) structure
Quaternary 4˚ structure
the sequence of amino acids in a polypeptide chain, read from the N-terminal end to the C-terminal end
1 st structure
2 structure
the polypeptide backbone is nearly fully extended
Beta sheet secondary structure
Supersecondary structures
2 structure
Isoelectric pH (pl) is the pH at which the majority of molecules of a compound in solution have no net charge
False
True
side chain is a guanidino group
Arg
His
Lys
side chain NH3 group is attached to an aliphatic hydrocarbon chain
Arg
His
Lys
side chain is an imidazole group
Arg
His
Lys
Thyroxine is found only in the thyroid gland
True
False
Hydroxylysine and Hydroxyproline are found only in a few connective tissues such as protein
True
False
For 19 of the 20, the α-amino group is primary; for proline, it is secondary
True
False
a compound that contains both an amino group and a carboxyl group
Amino acid
Protein
Structure Analysis
Deficiency of Protein may lead to: (give three)
(a)
When the amino acid pool reaches capacity the amino acids are broken down to their component parts for other uses
Amino Acid Absorption
Deamination
Amino Acid Metabolism
Amino acids are transported to the liver from the intestines via the portal vein
Amino Acid Absorption
Amino Acid Metabolism
Deamination
Liver metabolizes amino acids, depending on bodily needs
Amino Acid Absorption
Amino Acid Metabolism
Deamination
Four levels of structure
Structure of Proteins
Functions of Proteins (give three)
the association of polypepetide monomers into multisubunit proteins. Some common multi-subunits include:
Example of Fibrous Protein
Two steroisomers of amino acids
Proteins are abundant in:
Adults should consume ______ of protein
Premature infants lack sufficient ______ needed to create ______
The sequence of amino acids is determined by:
Functions of Proteins (give three)
