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Chapters 1 & 2_214
bio 214
Question | Answer |
---|---|
What are some tripeptides that would most likely to be soluble in an organic (hydrophobic) solvent like benzene? | N - proline - phenylalanine - leucine - C |
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. |
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. |
The low-molecular-weight building blocks of polymers are called? | Monomers |
Which amino acid is most likely to be found in the core of a protein? | methionine |
What is the maximum number of 100 amino acid long polypeptides that could be made? | 20^100 |
True or False? Eukaryotes have membrane-bound organelles; prokaryotes do not. | True |
True or false? Prokaryotes have relatively little DNA; eukaryotes generally have much more. | True |
True or false? Eukaryotic chromosomes are linear; prokaryotic chromosomes are circular. | True |
True or false? Prokaryotic DNA is naked or nearly naked; eukaryotic DNA is usually heavily associated with protein | True |
What is now thought to have been the genetic material in the first living organisms on Earth? | RNA. |
From what is the lipid-containing outer envelope surrounding the viral capsid of many animal viruses derived? | The cells (plasma) membrane |
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. |
The process by which a relatively unspecialized cell becomes highly specialized is called _______. | Differentiation |
A molecule that is capable of releasing or donating a hydrogen ion is termed a(n) _______. | Acid. |
The most stable atoms and thus those that are typically nonreactive are the atoms that have _______. | full outer shells |
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. |
What type of protein secondary structure is characterized as being highly extensible because of its coiled structure? | Alpha-Helix |
What are the Key secondary Structures? | Alpha-helix and Beta-Helix. |
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. |
Who was the first person to describe living single cells? | Leeuwenhoek |
Where are hydrophobic interactions most likely to occur? | the core of a water-soluble protein |
In a living organism, where are ionic bonds most likely to be the strongest? | deep in a protein's core where water is excluded |
DNA strands are held together by what type of bond? | Hydrogen bond. |
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. |
What level of structure in proteins is held together by intermolecular R group interactions? | quaternary structure. |
What do Primary structures describe? | the specific order of amino acids in a polypeptide, written from N- to C- terminus. |
What do Secondary structures describe? | The three-dimensional arrangement of amino acids ("conformation") of a *portion* of a polypeptide |
What do Tertiary structures describe? | The three-dimensional arrangement of amino acids ("conformation") of an entire polypeptide. |
What do Quaternary structures describe? | The molecular interaction between two or more polypeptides. |