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BCHM 307 EXAM 1 QUESTIONS WITH ANSWERS

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BCHM 307 EXAM 1 QUESTIONS WITH ANSWERS Secondary structure - Answer-the local 3-dimensional structure of the peptide backbone - there are 4 major classes of secondary structure (alpha helix, beta sheet, turns, and random coil) The alpha helix of the secondary structure - Answer-the alpha heli...

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  • August 30, 2024
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  • 2024/2025
  • Exam (elaborations)
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  • BCHM 307
  • BCHM 307
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BCHM 307 EXAM 1 QUESTIONS
WITH ANSWERS

Secondary structure - Answer-the local 3-dimensional structure of the peptide backbone
- there are 4 major classes of secondary structure (alpha helix, beta sheet, turns, and
random coil)

The alpha helix of the secondary structure - Answer-the alpha helix is a helical region of
the peptide backbone that is stabilized by hydrogen bonding
- carbonyl residue of each amino acid residue is hydrogen bonded to the amide group 4
residues further toward the carboxyl terminus
- R groups stick outward from alpha helices
- bulky or charged residues are unfavorable

the beta sheet of the secondary structure - Answer--planar arrangement of several
peptide backbones that is stabilized by hydrogen bonding
-carbonyl residue of each amino acid residue is hydrogen bonded to an NH group in an
adjacent chain
- R groups stick up and down from beta sheets

in beta sheets adjacent chains can be __ or __ - Answer-parallel or antiparallel

turns are small regions of the peptide backbone that can form small loops - Answer--
often contain glycine (small)
-often contain proline (Causes kinks)

tertiary structure - Answer-the global arrangement of secondary structure, amino acid R
groups and prosthetic groups
- regions of secondary structure interact to give a protein the tertiary structure
-repeats of antiparallel pleated sheet can form a beta barrel
-repeats of beta alpha-beta units can also form beta barrels
-hydrophobic residues are unfavorable on exterior of protein (no H bonds)
- charged residues are unfavorable on interior of a protein
-portions of tertiary structure can define domains
-a beta barrel linked to a beta-alpha-beta domain
-covalently stabilized by disulfide bridges

Phenylalanine - Answer-Absorbs light at 280 nm
hydrophobic
essential aromatic amino acid

, proline - Answer-hydrophobic amino acid

methionine - Answer-hydrophobic amino acid

tyrosine - Answer-absorbs light at 280 nm
a polar uncharged amino acid

glycine - Answer-hydrophobic amino acid
a non-chiral amino acid

lysine - Answer-a basic amino acid

aspartate - Answer-has a negatively charged R group

cysteine - Answer-can make disulfide bonds
a polar uncharged amino acid

The primary structure of a protein is held together by - Answer-peptide bonds

pH= - Answer-pH=-log[H+]

detergents are - Answer-amphiphilic molecules

hydrogen bonds occur between ___ donors and ___ - Answer-occur between polar
donors and acceptors

Glutamate has the following pKa's: 2.2 (alpha-carboxyl group), 4.3 (R group), and 9.7
(alpha amino group). What charge would be present on this molecule at pH 7? -
Answer--1

Water is a dipole because - Answer-oxygen is more electronegative than hydrogen
of it non-linear arrangement of atoms

for a molecule that functions as a buffer - Answer--it's buffering capacity is at the
molecule's pKa +/-1 pH unit
-consists of weak acid and conjugate base pair

Most of the common amino acids are chiral because - Answer-Their alpha carbon has
four different substituents

The primary structure of a protein is held together by - Answer-peptide bonds

Ultimately all levels of protein structure are dependent on - Answer-the amino acid
sequence of the protein

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