BCH210H1 Lecture Notes - Lecture 3: Hemoglobin, Asparagine, Hydrophile

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BCH210H1 Full Course Notes

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Chain a & chain b: linked through disulphide linkages (within and between chains) ** h-bonds are the key to stabilizing these structures! H-bond forms between amine group"s h and c=o of residue i-4. Side-chains face the outside: minimize steric interactions between r-groups, allow environment to interact w/ r-groups, minimize water"s involvement in the system h-bond competition with water. Amphipathic has 2 faces (hydrophobic & hydrophilic: most common, hydrophobic side: attached to protein, hydrophilic side: exposed & interact with external environment. Glycine: often present in large amounts at the packing sites (b/c of its small size) Extended strands aa"s are as pulled out as possible (3 angstroms) H- bonds b/w the sheets: doesn"t have to be all h-bonds other interactions w/ side groups exist as well. Can bind w/ aa"s close & far away (different from -helix) Side chains alternate sticking up & down: can form hydrophobic & hydrophilic faces.

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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BCH210H1 Lecture Notes - Lecture 3: Hemoglobin, Asparagine, Hydrophile

BCH210H1 Full Course Notes

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