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BCHM: Exam 2 Jeopardy
Terms in this set (39)
L and D enantiomers can be distinguished experimentally because their solutions can rotate plane polarized light in opposite directions (optically active). Thus all amino acids exist as enantiomers except_______.
The pH at which the numbers of positive and negative charges on an amino acid are equal is referred to as the _____ point.
This amino acid has sidechain pKa close to physiological pH and thus can either accept protons or donate them at this pH.
-positively charged at a pH<6
-neutral at a pH>6
This bond type forms the primary structure of proteins
Covalently linked amino acids with a single amino terminus and a single carboxyl terminus is called a(n)____
The peptide alanylglutamylarginyltyrosyllysylalanine consists of _____amino acids and ____peptide bonds.
6 amino acids:
5 peptide bonds
Individual amino acids when they are polymerized into polypeptides
Two amino acids undergo a ______ reaction to form a peptide bond. This reaction is_____.
Condensation (dehydration) ; unfavorable - must be coupled with ATP hydrolysis
A covalent bond between two nonadjacent cysteines in a polypeptide chain is a _____ bond
A small molecule not made of amino acids that is required for the protein to be active and inherently provides additional stability
A prosthetic group
These three interactions contribute to large negative enthalpy making protein folding thermodynamically favorable
The _____effect helps make the entropy change of the solvent favorable via the burial hydrophobic groups within the protein
The ____ bond is very important in stabilizing secondary and tertiary structure
In beta sheets the ____ of amino acids protrude in opposite directions with respect to the plane of the sheet
The amino acids ____ and ____ do not favor either of the main types of secondary structure but can be found in this left-handed secondary structure
______ proteins consist of predominantly secondary structure
Fibrous proteins are filamentous/elongated because they make use of amino acids that favor a particular ____ structure
True or False: The crosslinking of tropocollagen molecules via disulfide bonds makes them less elastic and more brittle over time.
False. Tropocollagen molecules get linked via modified lysine residues
Disrupting the hydrophobic interactions of a single subunit protein would have the greatest effect on the ____structure of that protein
In Afinsen's RNase A experiment, he _____the protein tertiary structure by adding urea followed by disulfide bond reduction with BME
This compact, locally folded region of tertiary structure. Also called a motif
This protein folding intermediate is compact and has native-like secondary structure and backbone folding topology but lacks defined tertiary structure interactions
A reagent used in electrophoresis to separate polypeptides based on mass
A _____ tag is covalently linked to your gene of interest in protein expression. This linkage can be removed from your protein via purification in this method of chromatography
You are given a bacterial lysate composed of a mixture of proteins with masses 150 kDa for protein A, 100 kDa for protein B and 50 kDa for protein C. In this type of chromatography, Protein B would elute second.
___ ___ chromatography is used to separate proteins on the basis of their surface charge
Myoglobin is to tertiary as hemoglobin is to _____.
HIV-1 protease can only function with 2 identical subunits. It is therefore this type of protein
The GroEL-GroES complex is made up of entirely different protein molecules. Thus, the entire complex is ____
T/F: Quaternary structure proteins can end up as aggregated intermediates or misfolded proteins in the energy landscape model
Cellular agents that assist in protein folding at elevated temperatures
Molecular chaperones/heat shock proteins
The covalently bonded product of the oxidation of two cysteine residues
A native protein is in its functional____
In a protein with sequence NADEFGHIKLMNPQRSTVWYC what are the N-terminal and C-terminal residues?
N and C
A mutation in one of the subunits in this protein causes a sickle phenotype in erythrocytes giving rise to this disease
Hemoglobin/Sickle Cell Anemia
Vitamin C is a cofactor for prolyl hydroxylase which is responsible for the hydroxylation of proline and lysine in collagen. Vitamin C deficiency leads to this disease.
Fibrillin is one of the three main proteins in connective tissue. Mutations in the fibrillin gene give rise to long limbs, fingers, toes, and excessive joint flexibility in this disorder
Alzheimer's, Parkinson's and Huntington's disease are all caused by these types of protein folding intermediates/aggregates
Scrapie in sheep, BSE in cows, Creutzfeldt-Jakob in humans are all caused by this protein/protein mutant
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