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BIOL 1020 Exam Questions And 100% Correct Answers

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BIOL 1020 Exam Questions And 100% Correct Answers...

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  • November 9, 2024
  • 8
  • 2024/2025
  • Exam (elaborations)
  • Questions & answers
  • BIOL 1020
  • BIOL 1020
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Stetson
BIOL 1020 Exam Questions And 100% Correct Answers



How does a protein's tertiary structure depend on its primary structure? - ANSWER A
protein's tertiary structure is dependant on its primary structure as the position, order,
spatial arrangement and chemical qualities (ei. polar, non-polar, electromagnetic force,
able to hydrogen bond etc) of the polypeptides contained in the primary structure
influence the bonds able to be made at the tertiary level.



Prokaryote - ANSWER An organism without cells that contain a nucleus. Pro = before



Eukaryote - ANSWER An organism with cells containing a nucleus.



Where does DNA reside in a prokaryote cell? - ANSWER In the cytoplasm of the cell. <-
Review, be more specific



Where can DNA reside in a eukaryote cell? - ANSWER The nucleus, the mitochondria
and chloroplasts (plant and algal cells).



What does an amino acid consist of? - ANSWER An amino group (-NH3+), a side chain-or
R-Group, an alpha carbon-middle carbon, a hydrogen atom and a carboxyl group-
-COO+ <- Review.



Alpha Helix - ANSWER A secondary level of protein structure, formed by the coiling of a
polypeptide held together by hydrogen bonds between carbonyl oxygen and amino
hydrogen atoms in the peptide backbone.



Beta Pleated Sheet - ANSWER A secondary level of protein structure; formed when one
or more strands of a polypeptide align parallel to one another and hydrogen bonds
between carbonyl oxygen and amino hydrogen atoms in the peptide backbone form
between the strands.

, Catalyst - ANSWER A substance that speeds up a reaction (generally by lowering the
activation energy) without being consumed.



Denaturation - ANSWER The disruption of secondary and tertiary conformation of a
protein, with resultant loss of function, brought about by exposure to environmental
stresses.



Di-sulphide Bridge - ANSWER Covalent bond between sulfur atoms of two cysteines;
important in tertiary and quaternary levels of protein structure.



Hydrophobic effect - ANSWER The tendency of nonpolar side chains of a polypeptide to
cluster and group together in order to minimize contact with water; important in tertiary
and quaternary levels of protein structure.



Peptide Bond - ANSWER Chemical bond between carbon and nitrogen that results when
two amino acids combine in a dehydration reaction.



Polypeptide - ANSWER Chain of amino acids linked together by peptide bonds.



Quarternary Structure ANSWER The fourth level of structure; involves two or more
polypeptides (which may or may not be identical) that have folded into their tertiary
structure(s) and interact to form a single functional unit.



Secondary Structure - ANSWER The second level of structure; coils and folds along the
peptide backbone due to hydrogen bonding between atoms of the peptide backbone;
distinguished from tertiary structure that involves interactions of R-groups.



X-Ray Crystallography - ANSWER Technique that can determine the structure of
molecules, including biological macromolecules, by measuring angle and intensity of
diffraction of X-rays as they pass through a crystalline structure.



Ribozyme - ANSWER Enzyme composed of RNA

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