#Question id: 775
#Unit 1. Molecules and their Interaction Relevant to Biology
The formation of microRNA is to:
#Question id: 4972
#Unit 11. Evolution and Behavior
Fossils of Lystrosaurus, a dicynodont therapsid, are most common in parts of modern-day South America, South Africa, Madagascar, India, South Australia, and Antarctica. It apparently lived in arid regions, and was mostly herbivorous. It originated during the mid-Permian period, survived the Permian extinction, and dwindled by the late Triassic, though there is evidence of a relict population in Australia during the Cretaceous. The dicynodonts had two large tusks, extending down from their upper jaws; the tusks were not used for food gathering, and in some species were limited to males. Food was gathered using an otherwise toothless beak. Judging from the fossil record, these pig-sized organisms were the most common mammal-like reptiles of the Permian. Anatomically, what was true of Lystrosaurus?
#Question id: 2753
#Unit 2. Cellular Organization
DNA gyrase and topoisomerase IV are the targets of anti-bacterial drugs. Whereas type I and II are target of:
#Question id: 11992
#Unit 10. Ecological Principles
#Question id: 723
#Unit 1. Molecules and their Interaction Relevant to Biology
Common structural elements in proteins such as α-helices or β-sheets are characterized by uniformly repeating, energetically favorable main chain conformations which additionally exhibit a completely saturated hydrogen-bonding network of the main chain NH and CO groups. Although polyproline or polyglycine type II helices (PPII or PGII ) are frequently found in proteins, they are not considered as equivalent secondary structure elements. Which of the following statements are correct about PP and PGs.
A. PGII -like helices form hexagonal bundles which appear to fulfill the criterion of a (largely) saturated hydrogen-bonding network of the main-chain groups
B. main chain NH and CO groups of the central PGII -helix are saturated by either intra- or intermolecular hydrogen-bonds, resulting in a self-contained hydrogen-bonding network
C. The formation of the right-handed PPI helix is possible only with proline residues because of the required cis conformation.
D. PPII helices seem to be stabilized by main chain-water hydrogen bonds (in the absence of main chain- main chain H-bonds), and tend to have a regular pattern of hydrogen bonds with water. After this, it is not surprising, that PPII helices are found mostly on the protein surface.