What is the major organ of the integumentary system? Approximately how much surface area does this organ cover?
What are the 3 layers within this organ?
List 4 accessory structures found within this system.
What are the main functions of this system?
pls don't copy and paste all words

All living organisms are composed of a. only one cell. b. at least 100 cells. c. at least three cells. d. one or more cells.

With the description of the different cell walls, membranes, and associated proteins set in the students' minds, you now need to introduce them to the idea that the cell wall can also act as a foundation to build things upon. bacterial appendages require a strong foundation that will offer the support needed to move and function in a dynamic world. for example, flagella are long, whiplike protein structures that are used by many gram-positive and gram-negative bacteria for locomotion. in order to function effectively, a flagellum must be firmly anchored to the cell wall. how will you be able to get across the idea that the peptidoglycan cell wall is strong enough to support such a mechanism? with a protein rod that passes through the cell wall and protein rings used to anchor it in the membranes, these basal bodies are the rudimentary biological motors that use atp power to spin the hook and the flagella attached to it. bacterial flagella have a biological motor that spins within the cell wall and is powered by atp. this allows the flagella to spin in a whiplike motion to propel the bacterium.

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