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BIO 219 Final Exam (Questions & Solutions By Expert)
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BIO 219 Final Exam (Questions & Solutions By Expert)
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BIO 219 Final Exam (Questions & Solutions By Expert)Humans are made of Right Ans - nitrogen, carbon, hydrogen, and oxygen
True of False: Nonpolar tend to avoid polar Right Ans - True
What is protein folding driven by? Right Ans - by separating nonpolar parts
of the protein from water
What is true of ionic bonds? Right Ans - They are weak inside cell because
it is made a water, and they are stronger outside of the cell
Hydrophobic Right Ans - covalent bonds can share electrons equally:
nonpolar
Hydrophilic Right Ans - covalent bonds do not share electrons equally:
polar
Hydrophobic interactions Right Ans - when atoms or regions of a molecule
are non-polar, they are also hydrophobic. These regions will stick together out
of their mutual avoidance of water
Monosaccharides, amino acids, nucleotides, and fatty acids are built with non-
covalent bonds. What does this mean? Right Ans - This means they can be
broken and built frequently and easily
Monomer Amino acids go to what macromolecule? Right Ans - proteins
Monomer nucleotides go to what macromolecules? Right Ans - Nucleic
acids
Monomer monosaccharides go to what macromolecules? Right Ans -
polysaccharides
Monomer fatty acids go to what macromolecules? Right Ans - lipids
True or False: All macromolecules have directionality? Right Ans - True
,What bonds are between the bases of nucleic acids? Right Ans - hydrogen
bonds
What bonds are between bases of carbohydrates? Right Ans - hydrophobic
interactions
What bonds make up proteins? Right Ans - ionic bonds for folding
Some proteins are catalyst. Right Ans - These proteins make reactions
faster.
Some proteins are structural. Right Ans - These proteins hold things
together.
Some proteins are motor proteins. Right Ans - These proteins generate
movement in cells or move cells themselves.
Some proteins are storage proteins. Right Ans - These proteins store other
molecules until they are needed.
Some proteins are signalers Right Ans - These proteins signal from cell to
cell
Some proteins are receptors Right Ans - These proteins receive signals and
transmit them across the membrane
Some proteins are regualtors Right Ans - These proteins turn other parts of
proteins on or off.
Primary Structure Right Ans - Amino acids in a linear string held together
by peptide bonds.
Tertiary structure Right Ans - backbone atoms are connected to side
chains. they interact in a couple of common ways to shield hydrophilic atoms
in hydrophobic spaces.
Secondary structure Right Ans - local folding of the polypeptide chain into
helices or sheets
, Quaternary structure Right Ans - proteins consisting of more than one
amino acid chain
Binding affinity Right Ans - measure how fast something falls apart
Allostery Right Ans - molecules have multiple stable conformations, which
are determined by their binding proteins. also known as "induced fit".
Transmembrane Right Ans - all the way through the membrane
Lipid -link Right Ans - lipids interact with hydrophobic parts of the
membrane
Mosaic membrane Right Ans - non-covalently bonded, bonds easily created
and broken
Unsaturated Right Ans - more fluidity because there is more room for more
water to flow through. short chain
Saturated Right Ans - less fluid because there is less room for water to flow
through due to long chain
Simple diffusion Right Ans - when molecules can cross with their
concentration gradient without addition of energy
Facilitated diffusion Right Ans - move with gradient, use proteins to move
faster
Channel proteins Right Ans - very specific holes create permeable spaces in
the membrane
use allostery to move molecules
Active transport Right Ans - molecules move against their gradient using
energy from coupled transport
Direct active transport Right Ans - use chemical reactions
indirect transport Right Ans - uses coupled transport (movement of
molecule with gradient)
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