BCH210H1 Study Guide - Midterm Guide: Tyrosine, Phenylalanine, Tryptophan

97 views1 pages

pearmule246

18 Oct 2016

School

UTSG

Department

Biochemistry

Course

BCH210H1

Professor

Stavroula Andreopoulos

For unlimited access to Study Guides, a Grade+ subscription is required.

thaanya10 and 40172 others unlocked

BCH210H1 Full Course Notes

Verified Note

49 documents

Document Summary

The 20 amino acids are drawn here with their short form and important characteristics listed at the sides of the diagram. It may not be necessary to know how they are drawn but identi cation is really straight forward. The skeletal formula is used here to draw out the back bone of the amino acid. The alpha carbon is at the middle of the amide and carboxyl group. Alpha helix: this means that the amino acid is a very good former of the secondary protein structure, alpha helix. Beta sheet: this means that the amino acid is a very good former of the secondary protein structure, beta pleated sheets. Good/bad turn: this states how high or low the odds are of nding the amino acid at a beta turn. Beta branched: this occurs when a carbon is connected to 2 or more substituents that are not hydrogen or a proton. Acronyms are listed to help for easy memory of subgroups.

Related Questions

1. A sequence of amino acids in a certain protein is found to be â Ser â Gly â Pro â Gly â

The sequence is most probably part of a(n):

a. beta turn

b. antiparallel beta sheet

c. alpha-helix

d. parallel beta-sheet

e. alapha-sheet

2. Which statement about peptides bonds is NOT TRUE?

There is perfectly free rotation about the peptide bond.

The peptide bond has partial double-bond character.

The peptide bond is shorter than a normal carbon-nitrogen single bond.

The peptide bond usually has a trans configuration with respect to the alpha-carbons of the two amino acids involved in the peptide bond.

Peptide bonds are made via condensation of an amine and a carboxylic acid with loss of water.

3. Which of the following statements about proteins is FALSE?

	Active proteins are generally very loosely structured.
	In water-soluble proteins, hydrophobic amino acid residues are generally buried and not exposed to water.
	Primary structure determines tertiary structure.
	Secondary structure is regular, recurring arrangements in space of nearby amino acid residues in a polypeptide.
	Quaternary structure involves the interaction of subunits in a protein with more than one polypeptide chain.

maroonwallaby335

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

BCH210H1 Study Guide - Midterm Guide: Tyrosine, Phenylalanine, Tryptophan

BCH210H1 Full Course Notes

Document Summary

Get access

Related textbook solutions

Chemistry: Structure and Properties

Basic Chemistry

Principles of Chemistry Molecular Approach

Chemistry: Structure and Properties

Principles of Chemistry Molecular Approach

Chemistry: A Molecular Approach

Chemistry: A Molecular Approach

Principles of Chemistry: A Molecular Approach

Chemistry: The Central Science

Related Documents

BCH210H1 Lecture Notes - Lecture 3: Hemoglobin, Globular Protein, Quaternary

BCH210H1 Lecture 25: L25

BCH210H1 Lecture Notes - Lecture 2: Alpha Helix, Beta Sheet, Glutamine

Related Questions