Which part of the brain is responsible for coordinating muscle movements and maintaining balance?

The kobe habor wharfs where the center of japanese exports to other countries. it had 200 wharfs before the earthquake. how many wharfs remained undamaged after the earthquake? a. 130 wharfts b. 3 wharfs c. 30 wharfs

You have been asked to lead a demonstration for the undergraduate microbiology lab course about the uses of negative staining when studying bacteria. a "negative" stain does not stain the bacterial cell itself but stains the space between cells. under magnification, the acidic (negativelycharged) nature of the stain will be repelled by the negatively charged bacterial cell wall and willleave the cell colorless in a stained background. negative stains are used primarily to reveal the presence of negatively charged bacterial capsules; therefore, they are also called capsule stains. encapsulated cells appear to have a halo surrounding them. the negative stain procedure does not require heat fixation, which limits any chances of alteration in bacterial cell shape and size. the bacterial suspension is added to a drop of stain, such as nigrosin or eosin, and drawn across the glass slide using a coverslip.nigrosin staining-not safranin staining-of klebsiella pneumoniae will allow for the visualization of the cell shape and the determination of the presence of a capsule.true/false

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