Question 1

How does a protein's amino acid sequence influence the tertiary structure?

Accepted Answer

A protein will spontaneously fold into a three-dimensional structure determined by the amino acid sequence.

Question 2

A protein whose peptide backbone is mostly extended and hydrogen bonded to different strands of the protein is composed mostly of the _______________ secondary structure.

Accepted Answer

β-sheet

Question 3

Describe some of the features of an α helix.

Accepted Answer

The α helix is a coil stabilized by intrachain hydrogen bonds between the carbonyl oxygen of a residue and the amide hydrogen of the fourth residue away. There are 3.6 amino acids per turn. The hydrogen bonds are between amino acid residues that have two intervening residues. Thus, these amino acid residues are found on the same side of the coil. The helix is almost always right-handed, although left-handed helices are, in theory, possible.

Question 4

Choose the correct answer from the list below. Not all of the answers will be used.
-Two amino acids undergo oxidation to form a dimer called ____________.

Accepted Answer

A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine 
A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine

Question 5

Which of the following protein(s) contain examples of α-helical character?

Accepted Answer

A)  keratin 
B)  ferritin 
C)  myosin 
D)  tropomyosin 
E)  All of the above. 
A)  keratin 
B)  ferritin 
C)  myosin 
D)  tropomyosin 
E)  All of the above.

Question 6

What structure(s) did Pauling and Corey predict in 1951?

Accepted Answer

A)  α helix 
B)  β sheet 
C)  β turn 
D)  A, B, and C 
E)  A and B 
A)  α helix 
B)  β sheet 
C)  β turn 
D)  A, B, and C 
E)  A and B

Question 7

What is the advantage of having certain regions of partially correct folded regions?

Accepted Answer

If some regions interact prefe

Question 8

Due to the side group steric clash, almost all peptide bonds are _______________ in their configuration.

Accepted Answer

The answer of Due to the side group steric clash,...

Question 9

Disulfide bonds in proteins can be reduced to free sulfhydryl groups by reagents such as _______________.

Accepted Answer

The answer of Disulfide bonds in proteins can be reduced...

Question 10

Choose the correct answer from the list below. Not all of the answers will be used.
-The overall structure of a protein is referred to as ____________.

Accepted Answer

A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine 
A) amino 
B) water 
C) protons 
D) DNA 
E) secondary structure
F)tertiary structure
G)Ramachandran
H)RNA
I)domain
J)cystine
K)proline
L)Sanger
M)D amino acids
N)cysteine

Question 11

What is the sequence of amino acids found in collagen? What is the significance of the sequence and what is the complication of scurvy?

Accepted Answer

Gly-Pro-Pro. The small side group of the

Question 12

Peptides differ from proteins in _______________.

Accepted Answer

the number

Question 13

What is the "hydrophobic effect" as it relates to protein structure?

Accepted Answer

The three-dimensional structur

Question 14

Why are all the theoretical combinations of phi and psi not possible?

Accepted Answer

Steric hindrances of

Question 15

What are the key characterisics that make the peptide bond important to protein folding/structure?

Accepted Answer

The resonance of the amide bond create a

Question 16

In the ribonuclease experiments performed by Anfinsen, what was the significance of the presence of the reducing agent β-mercaptoethanol?

Accepted Answer

The reducing agent reduced inc

Question 17

_______________ is the major fibrous protein present in skin, bone, tendon, cartilage, and teeth.

Accepted Answer

The answer of _______________ is the major fibrous protein present...

Question 18

How does the protein backbone add to structural stability?

Accepted Answer

The protein backbone contains the peptid

Question 19

_______________ refers to the spatial arrangement of subunits and the nature of their interactions.

Accepted Answer

Quaternary

Question 20

Compact, globular proteins are typically water _______________ and consist mostly of _______________ secondary structure.

Accepted Answer

soluble; a

Exam 4: Protein Three-Dimensional Structure

How does a protein's amino acid sequence influence the tertiary structure?

A protein whose peptide backbone is mostly extended and hydrogen bonded to different strands of the protein is composed mostly of the _______________ secondary structure.

Describe some of the features of an α helix.

Choose the correct answer from the list below. Not all of the answers will be used. -Two amino acids undergo oxidation to form a dimer called ____________.

Which of the following protein(s) contain examples of α-helical character?

What structure(s) did Pauling and Corey predict in 1951?

What is the advantage of having certain regions of partially correct folded regions?

Due to the side group steric clash, almost all peptide bonds are _______________ in their configuration.

Disulfide bonds in proteins can be reduced to free sulfhydryl groups by reagents such as _______________.

Choose the correct answer from the list below. Not all of the answers will be used. -The overall structure of a protein is referred to as ____________.

What is the sequence of amino acids found in collagen? What is the significance of the sequence and what is the complication of scurvy?

Peptides differ from proteins in _______________.

What is the "hydrophobic effect" as it relates to protein structure?

Why are all the theoretical combinations of phi and psi not possible?

What are the key characterisics that make the peptide bond important to protein folding/structure?

In the ribonuclease experiments performed by Anfinsen, what was the significance of the presence of the reducing agent β-mercaptoethanol?

_______________ is the major fibrous protein present in skin, bone, tendon, cartilage, and teeth.

How does the protein backbone add to structural stability?

_______________ refers to the spatial arrangement of subunits and the nature of their interactions.

Compact, globular proteins are typically water _______________ and consist mostly of _______________ secondary structure.

Biochemistry and the Unity of Life

Water, Weak Bonds, and the Generation of Order Out of Chaos

Amino Acids

Techniques in Protein Biochemistry

Basic Concepts of Enzyme Action

Kinetics and Regulation

Mechanisms and Inhibitors

Hemoglobin: an Allosteric Protein

Carbohydrates

Lipids

Membrane Structure and Function

Signal Transduction Pathways

Digestion: Turning a Meal Into Cellular Biochemicals

Metabolism: Basic Concepts and Design

Glycolysis

Gluconeogenesis

Preparation for the Cycle

Harvesting Electrons From the Cycle

The Electron Transport Chain

The Proton-Motive Force

The Light Reactions

The Calvin Cycle

Glycogen Degradation

Glycogen Synthesis

The Pentose Phosphate Pathway

Fatty Acid Degredation

Fatty Acid Synthesis

Lipid Synthesis

Amino Acid Degradation and the Urea Cycle

Amino Acids Synthesis

Nucleotide Metabolism

The Structure of Informational Macromolecules: Dna and Rna

DNA Replication

DNA Repair and Recombination

RNA Synthesis and Regulation in Prokaryotes

Gene Expression in Eukaryotes

RNA Processing in Eukaryotes

The Genetic Code

The Mechanism of Protein Synthesis

Recombinant DNA Techniques

Filters

Compact, globular proteins are typically water _ and consist mostly of _ secondary structure.