BIO CHEM I Flashcards
A reaction with a delta G of zero:
Requires energy
Is at equilibrium
Is spontaneous
None of the above
Is at equilibrium
A solution with a pH of 5 is:
Acidic
Basic
Neutral
None of the above
Acidic
Alcohols contain a _________ group.
Hydroxyl
Sulfur
Phenol
None of the above
Hydroxyl
Biologically important noncovalent bonds include:
Van der Waals interactions
Hydrogen bonds
Electrostatic interactions
All of the above
All of the above
Entropy is ______________.
The degree of disorder of a system
The degree of energy of a system
A type of noncovalent bond
A type of covalent bond
The degree of disorder of a system
The DNA of a eukaryotic cell is stored within the _____________.
Lysosome
Nucleus
Ribosome
Endoplasmic Reticulum
Nucleus
The term “kinetics” refers to:
The energy required for a reaction
The disorder of a system
The speed at which a reaction will occur
The pH of a solution
The speed at which a reaction will occur
______ is the process by which the information in DNA is transferred to RNA.
Translation
Replication
Transcription
Ubiquitination
Transcription
The strongest bonds that are present in biochemical compounds are ______________.
Ionic bonds
Covalent bonds
Hydrogen bonds
Van der Waals interactions
Covalent bonds
A chiral compound _________________.
Is non-superimposable on its mirror image
Is the same as its mirror image
Is inorganic
Contains a sulfur atom
Is non-superimposable on its mirror image
A zwitterion ________________.
Has a positive charge
Has a negative charge
Overall, has no charge
All of the above
All of the above
All amino acids contain both a(n) ______ and a(n) ________ group.
Hydrogen, carbohydrate
Amine, carboxylic acid
Sulfur, amine
None of the above
Amine, carboxylic acid
Essential amino acids:
Are made by organisms
Must be obtained from dietary sources
Are made from DNA
Include proline
Must be obtained from dietary sources
The first reaction of amino acid degradation is?
Deamination
Decarboxylation
Cyclization
None of the above
Deamination
The only amino acid without a chiral center is _____________.
Proline
Methionine
Alanine
Glycine
Glycine
There are ______ common amino acids.
15
25
20
10
20
______ is the initiating amino acid of most newly synthesized proteins.
Proline
Alanine
Glycine
Methionine
Methionine
_____________ is an example of a hydrophilic amino acid.
Lysine
Leucine
Methionine
Tryptophan
Lysine
_____________ is an example of a hydrophobic amino acid.
Glutamic acid
Lysine
Arginine
Leucine
Leucine
Nonessential amino acids are:
Provided in the diet
Synthesized by mammals
Both A and B
None of the above
Both A and B
Provided in the diet
Synthesized by mammals
A(n) _________ is a short protein tag that attaches to and targets proteins for degradation.
Peptide
Ubiquitin
Alanine
Urea
Ubiquitin
Protein secondary structures include:
Loops
alpha helices
beta sheets
All of the above
All of the above
Protein synthesis is carried out by __________.
Mitochondria
Chromosomes
Ribosomes
Lysosomes
Ribosomes
The amino acid _______ places certain constraints on the protein backbone.
Leucine
Alanine
Proline
Glycine
Proline
The difference between a peptide and a protein is ____________.
Length
Bond formation
Subunits
All of the above
Length
The formation of a dimer refers to a protein’s ___________.
Primary structure
Tertiary structure
Secondary structure
None of the above
None of the above
The tertiary structure of a protein refers to its __________.
Overall 3D shape
Multisubunit composition
Amino acid sequence
None of the above
Overall 3D shape
The ______ carries out protein degradation.
Proteosome
Lysosome
Ribosome
Chromosome
Proteosome
________ aid in protein folding.
Chromosomes
Chaperones
Proteosome
None of the above
Chaperones
Amino acids are linked by a(n) _______ bond to form a protein.
Hydrophobic
Peptide
Ionic
All of the above
Peptide
Each of the following is one of the six classes of enzyme catalysts, except:
Ligases
Kinases
Transferases
Isomerases
Kinases
Enzymes within metabolic pathways can be regulated by ____________.
Allosteric enzymes
Post translational modifications
Localization
All of the above
All of the above
n competitive inhibition, the competitor binds to ________________.
The substrate
The substrate binding site
Distant to the substrate binding site
None of the above
The substrate binding site
The maximum rate at which an enzyme can convert substrate to product
The maximum amount of product produced in a reaction
The free energy of a reaction
None of the above
The maximum rate at which an enzyme can convert substrate to product
Kinases are enzymes that add a(n) _____ group to proteins.
Hydrogen
Nitrogen
Phosphoryl
Alcohol
Phosphoryl
The rate of an enzymatic reaction can be regulated by __________.
pH
Temperature
Concentration
All of the above
All of the above
_______ are derived from vitamins and are necessary for the function of some enzymes.
Helicases
Cofactors
Carbohydrates
None of the above
None of the above
________ is an example of a post translational modification of a protein.
Acetylation
Phosphorylation
Ubiquitination
All of the above
All of the above
Enzymes act as catalysts to ___________________.
Decrease the activation energy of a reaction
Increase the rate of a reaction
Mediate the conversion of substrate to product
All of the above
All of the above
An important product of glycolysis is ____________.
Glucose
ATP
Lectins
Both A and B
ATP