bio 214
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| What are some tripeptides that would most likely to be soluble in an organic (hydrophobic) solvent like benzene? | N - proline - phenylalanine - leucine - C
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| Describe 5 characteristics that form the basic properties of cells? | 1)Cells are highly complex and Organized
2)Cells posses a genetic code and the means to use it.
3)Cells are capable of producing more of themselves.
4)Cell acquire and utilize energy
5)Cells carry out a variety of Chemical reactions.
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| Describe 4 characteristics that form the basic properties of cells? | 6) Cells engage in Mechanical activies.
7) Cells are able to respond to Stimuli.
8) Cell are capable of self-Regulation.
9) Cells evolve.
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| The low-molecular-weight building blocks of polymers are called? | Monomers
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| Which amino acid is most likely to be found in the core of a protein? | methionine
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| What is the maximum number of 100 amino acid long polypeptides that could be made? | 20^100
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| True or False? Eukaryotes have membrane-bound organelles; prokaryotes do not. | True
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| True or false? Prokaryotes have relatively little DNA; eukaryotes generally have much more. | True
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| True or false? Eukaryotic chromosomes are linear; prokaryotic chromosomes are circular. | True
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| True or false? Prokaryotic DNA is naked or nearly naked; eukaryotic DNA is usually heavily associated with protein | True
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| What is now thought to have been the genetic material in the first living organisms on Earth? | RNA.
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| From what is the lipid-containing outer envelope surrounding the viral capsid of many animal viruses derived? | The cells (plasma) membrane
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| Proteins are often composed of two or more distinct modules that fold up independently of one another. They often represent parts of a protein that function in a semi-independent manner. What are these modules are called ______. | Domains.Domains, in a folded protein, look like independent units in terms of their local folding and because they are observed over and over again in different proteins. Very often each domain has a specific function.
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| The process by which a relatively unspecialized cell becomes highly specialized is called _______. | Differentiation
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| A molecule that is capable of releasing or donating a hydrogen ion is termed a(n) _______. | Acid.
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| The most stable atoms and thus those that are typically nonreactive are the atoms that have _______. | full outer shells
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| Why are free ionic bonds of little importance and relatively unlikely to form in living organisms? | Cells are composed mostly of water, which interferes with ionic bonds between free ions.
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| What type of protein secondary structure is characterized as being highly extensible because of its coiled structure? | Alpha-Helix
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| What are the Key secondary Structures? | Alpha-helix and Beta-Helix.
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| How do amino acids like hydroxylysine and thyroxine, which are not among the 20 amino acids that are inserted into proteins, get into proteins? | They are the result of the alteration of R groups of the 20 amino acids after their incorporation into the polypeptide.
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| Who was the first person to describe living single cells? | Leeuwenhoek
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| Where are hydrophobic interactions most likely to occur? | the core of a water-soluble protein
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| In a living organism, where are ionic bonds most likely to be the strongest? | deep in a protein's core where water is excluded
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| DNA strands are held together by what type of bond? | Hydrogen bond.
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| What kind of noncovalent interaction is typified by interactions between two molecules that are so close together that they can experience weak attractive forces bonding them together? | van der Waals forces.Van der Waals forces are very weak forces between two very close surfaces.
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| What level of structure in proteins is held together by intermolecular R group interactions? | quaternary structure.
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| What do Primary structures describe? | the specific order of amino acids in a polypeptide, written from N- to C- terminus.
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| What do Secondary structures describe? | The three-dimensional arrangement of amino acids ("conformation") of a *portion* of a polypeptide
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| What do Tertiary structures describe? | The three-dimensional arrangement of amino acids ("conformation") of an entire polypeptide.
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| What do Quaternary structures describe? | The molecular interaction between two or more polypeptides.
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