BIOL107 Lecture Notes - Lecture 10: Untranslated Region, Transcription Bubble, Entertainment Uk

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fuchsiawalrus158

12 Jul 2016

School

University of Alberta

Department

Biology (Biological Sciences)

Course

BIOL107

Professor

Frank Nargang

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BIOL107 Full Course Notes

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Dna determines every characteristic of a cell or organism. It is the properties of the specific proteins in a cell/organism that directly determine its characteristics. Each protein has a distinct sequence of amino acids that determine the proteins shape and activity. These allow a given protein to perform very specific functions. Proteins are linear polymers of amino acids (aas) joined by peptide bonds ( called polypeptides) Different proteins consist of different numbers and different sequences of aas. This determines the shape and properties of a given protein ii. Most proteins have certain segments of the aa chain existing in coiled or folded patterns. Results from h-bonds between atoms in the polypeptide backbone. This aspect of protein structure/shape depends on interactions between aa r-groups. Covalent bonds between s atoms in r groups of two cysteine aas. Tertiary structure interactions cause protein to assume its characteristic shape iv. Some proteins consist of two or more polypeptide chains.

Related Questions

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

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BIOL107 Lecture Notes - Lecture 10: Untranslated Region, Transcription Bubble, Entertainment Uk

BIOL107 Full Course Notes

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