BIOL 101 Lecture Notes - Lecture 6: Prometaphase, Phospholipid, Transport Protein

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24 Mar 2018

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Proteins: be able to draw the general structure of an amino acid. The four levels of protein structure are primary, secondary, tertiary, and quaternary structure. Know examples of each type given in class. It is one 3d folding of a polypeptide chain in order to form a globular protein. It is stabilized by bonds between r groups. These bonds might be covalent, ionic, hydrogen, or hydrophobic interactions. May be stabilized by any type of bond covalent, ionic, hydrogen or hydrophobic. It may result in globular proteins or fibrous proteins. Eukaryotes contain a nucleus to contain their dna, prokaryotes do not. Eukaryotes also have membrane bound organelles and are compartmentalized by their function. Eukaryotes have one strand of linear dna, while prokaryotic dna is in a ring shaped formation. Multicellular organisms belong to eukarya: fungi, animals, plants, protists. Know cell structures, their functions, and whether they are found in bacterial, plant and animal cells.

Related Questions

In your own words, write a short paragraph for each level of protein structure
(primary, secondary, tertiary, quaternary) and for each describe the types of
interactions. What parts of the protein are interacting with what other parts of the
protein? What types of bonds are used to hold that level of protein structure
together? Are there any patterns of folding that are found in that level of protein
folding? If so, describe them.

coralhippopotamus551

1. The level of protein structure that is stabilized primarilyby non-covalent interactions between the side chains within asingle polypeptide chain is refered to as its:

A) primary structure

B) secondary structure

C) tertiary structure

D) quaternary structure

E) none of the above

2. Collagen, a strong fibrous protein found in connectivetissue, bone, and the extracellular matrix, has a structure inwhich three left-handed helices wind around each other to form aright-handed triple helix. The primary structure of collagen has arepeat unit of -(Gly-X-Pro)- Which of the following bonds stabilizethe collagen triple helix? (mark all that apply)

A) Hydrogen bonds between hydroxyproline residues

B) Hydrogen bonds between N-H and C=O

C) Ionic bonds between amino acid side chains

D) Hydrogen bonds between charged amino acids

3. The non-covalent forces that stabilize the Beta-strandconformation of peptides include:

A) H-bonds between amide C=O and amide NH

B) Van der Waals packing between the peptide backbone atoms

C) Van der Waals packing due to side chain interdigitation

D) Only A and B above

E) None of the above

4. What is the approximate length difference of a 22-kDasingle-stranded ?-helical protein segment vs. a 22-kDasingle-stranded ?-strand protein segment? Assume a mean residuemass of 110 Da. Show work.

5. Circular dichroism measurements have shown that the peptidebackbone of poly-l-lysine (KKKKKKK) adopts a random coilconformation at pH 7.0, but becomes ?-helical as the pH is raisedabove 10. This observation is known as the

magentaotter572

Is DNA a protein if so what makes up proteins, if not what it is and what are its monomers called? Describe the primary, secondary, tertiary, and quaternary structure of DNA (this sub-question is independent of the answer to the first question).

Describe electrostatic bonds, covalent bonds, van der Waals interactions, and hydrogen bonds and give an example of each.

Which of the four classes of amino acids has side chains with the greatest hydrogen-bond-forming potential?

Which has the greatest potential to form electrostatic interactions?

Which class has the greatest potential for hydrophobic interactions?

Of the following amino acids, (K), (Y), and (F), which side-chains would you expect to be the most soluble in a polar aqueous solution? Which the least?

Would you agree with the statement that many different amino acid sequences can fold into the same basic tertiary structure? What data can you cite as evidence for your position?

BIOL 101 Lecture Notes - Lecture 6: Prometaphase, Phospholipid, Transport Protein

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