WK4 P2 Cell Bio

winniesmith's version from 2017-01-03 21:07

Section 1

Question Answer
Name the types of nucleic acidsDeoxyribonucleic acid(DNA)- the genetic material. Ribonucleic acid(RNA): mRNA carries info from DNA to the ribosomes. Ribosomal/transfer RNA are involved in protein synthesis.
Roles of other RNA moleculesinvolved in regulation of gene expression and processing and transport of RNAs and proteins. RNA can also catalyze a number of chemical reactions. The
What are nucleotides made off purine and pyrimidine bases linked to phosphorylated sugars.
What purines/pyrimidines does DNA containtwo purines (adenine and guanine) and two pyrimidines (cytosine and thymine).
What does RNA contain compared to DNA uracil in place of thymine.

Section 2

Question Answer
Bases are linked to sugars to form what nucleosides.
What sugar does DNA have 2'-deoxyribose
What sugar does RNA haveribose
What links to the 5'carbon on the sugarsone or more phosphate group
What bond links nucleotidesphosphodiester bonds
Where are the phosphodiester bondsbetween the 5' phosphate of one nucleotide and the 3' hydroxyl of another. Condensation reaction
What is the chain sense of direction in a polynucleotideSynthesized in the 5' to 3' direction. one end terminates in a 5′ phosphate group and the other in a 3′ hydroxyl group.

Section 3

Question Answer
what does guanine like with cytosine
what does cytosine link withguanine
what does adenine link withthymine
what does thymine link withadenine
how do they linkhydrogen bonds between complementary base pairs.
What does complementary base pairing allowone strand to act as a template for synthesis of a complementary strand: Self-replication

Section 4

Question Answer
What is the most diverse macromoleculeProteins
What are the functions of proteins Structural components Transport and storage of small molecules (e.g., O2) Transmit information between cells (protein hormones) Defense against infection (antibodies) Enzymes
How many amino acids are there20
Describe the structure of an amino acidα carbon bonded to a carboxyl group (COO−), an amino group (NH3+), a hydrogen, and a distinctive side chain.
What are the AA side chain groupsNonpolar side chains Polar side chains Side chains with charged basic groups Acidic side chains terminating in carboxyl groups
How are AA joinedby peptide bonds, condensation reactions
How do AA polypeptide chains terminateone end terminates in an α amino group (N terminus) and the other in an α carboxyl group (C terminus)

Section 5

Question Answer
Sequence of amino acids codes for..characteristics of protein by determining the order of nucleotide bases in a gene.
How is the 3D structure of a protein analyzedby X-ray crystallography
How does X-ray crystallography workX-rays are directed at the protein; the pattern of X-rays that pass through is detected on X-ray film. The X-rays are scattered in characteristic patterns determined by the arrangement of atoms in the molecule.
What is the primary structure the sequence of amino acids in the polypeptide chain
What is the secondary structureregular arrangement of amino acids within localized regions.
What are the two types of secondary structure α helix and β sheet. Both are held together by hydrogen bonds between the CO and NH groups of peptide bonds.
What is the tertiary structurethe folding of the polypeptide chain due to interactions between side chains of amino acids in different regions of the chain. In most proteins this results in domains, the basic units of tertiary structure. Figure
What is the quaternary structure Interactions between different polypeptide chains in proteins composed of more than one polypeptide
What is a critical determinant of tertiary structurePlacement of hydrophobic amino acids in the interior of the protein and hydrophilic amino acids on the surface, where they interact with water.
What do loop regions connect the elements of secondary structure.
How do loop regions formon the surface of folded proteins, where the polar components of the peptide bonds form hydrogen bonds with water or with the polar side chains of hydrophilic amino acids.