C H A P T E R 6
PROTEINS:
THREE-DIMENSIONAL
STRUCTURE
1.
SECONDARY STRUCTURE
A.
The Peptide Group
B.
Regular Secondary Structure: The ␣ Helix and the
 Sheet
C.
Fibrous Proteins
D.
Nonrepetitive Protein Structure
2.
TERTIARY STRUCTURE
A.
Determining...
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C H A P T E R 6
PROTEINS:
THREE-DIMENSIONAL
STRUCTURE
1.
SECONDARY STRUCTURE
A.
The Peptide Group
B.
Regular Secondary Structure: The ␣ Helix and the
 Sheet
C.
Fibrous Proteins
D.
Nonrepetitive Protein Structure
2.
TERTIARY STRUCTURE
A.
Determining Protein Structure
B.
Motifs (Supersecondary Structures) and Domains
C.
Protein Families
3.
QUATERNARY STRUCTURE AND SYMMETRY
4.
PROTEIN FOLDING AND STABILITY
A.
Forces That Stabilize Protein Structure
B.
Protein Denaturation and Renaturation
C.
Protein Folding Pathways
D.
Protein Dynamics
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The atomic structure of myoglobin, an oxygen binding protein, is drawn here as a stick model.
The overall conformation of a
protein such as myoglobin is a function of its amino acid sequence.
How do noncovalent forces act on a polypeptide chain to
stabilize its unique three-dimensional arrangement of atoms? [Figure copyrighted © by Irving Geis.
]
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