Open the US Energy Mapping System and select your home state. To sort through the energy types and pipelines on the map, select Layers/Legend from the map's menu at the top right. Choose one specific type of energy to view at a time
using the Views dropdown menu. Select each type of energy (biomass, coal, fossil fuels, etc.) to see how and where it is
produced within your state. You can see additional information about each source by expanding the selected boxes
within the Layers/Legends dropdown menu. You can also click the locations on the map to view more information. Click
the blue header to collapse the Layers/Legend window at any time.
Cycle through each type of energy to compare how prevalent each type is in your state. Which energy source appears to
produce the most energy in your state, based on the number of facilities? (Keep this web page open to answer the
questions in parts Fand G.)

Natalie had random hand movements when she was two months old. when she was six months old, she used to grab a block with her whole hand. now at the age of ten months, she can grasp the same block with her thumb and forefinger. this sequence of growth in her hand and finger movements is according to the pattern.

Match the descriptions / definitions with the term they best describe 1. three dimensional relationship of the different polypeptide chains in a multisubunit protein or protein complex 2. common folding pattern in proteins in which a linear sequence of amino acids folds into a right-handed coil stabilized by internal hydrogen-bonding between polypeptide backbone atoms. 3. the amino acid sequence of a protein 4. a region on the surface of a protein that can interact with another molecule through noncovalent bonding. 5. three-dimensional arrangement of alpha-helices and beta-sheets within a single polypeptide, typically stabilized by a variety of noncovalent bonds, including ionic and hydrogen bonds, and nonpolar interactions / hydrophobic force. 6. the chain of repeating carbon and nitrogen atoms, linked by peptide bonds, in a protein. 7. common structural motif in proteins in which different sections of the polypeptide chain run alongside each other and are joined together by hydrogen bonding between atoms of the polypeptide backbone. 8. portion of a polypeptide chain that has a discrete tertiary structure of its own and can often fold independently of the rest of the chain 9. regular local folding patterns in a protein, including alpha-helix and beta-sheet a. primary structure b. beta-sheet c. protein d. coiled-coil e. polypeptide backbone f. secondary structure g. side chain h. tertiary structure i. binding site j. alpha-helix k. quaternary structure l. protein domain

Which scientific design has both practical limitations and limitations due to scale? studying the effect of bleach on the growth of mold spores exposing cultures of duckweed to different intensities of light observing the replication of dna molecules with a hand lens using colored marbles to model a cross between two colors of rabbits