CHAPTER 2 - PROTEIN STRUCTURE
B: PROBING COMPOSITION, SEQUENCE, AND CONFORMATION
BIOCHEMISTRY - DR. JAKUBOWSKI
2/28/16
Learning Goals/Objectives for Chapter 2B: After class and
this reading, students will be able to
describe in general terms the procedures and chemical steps in the
determinations of the following for proteins:
- molecular weight
- presence of certain specific amino acids
- amino acid composition
- N and C terminal amino acid
- specific amino acid necessary for binding and activity
- amino acid sequence
- secondary structure
- 3D structure
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B3. Levels of Protein Structure
A protein can be considered to have primary, secondary, tertiary, and
quaternary structures.
- primary structure: the linear amino acid sequence of a protein
- secondary structure: regular repeating structures arising when
hydrogen bonds between the peptide backbone amide hydrogens and carbonyl
oxygens occur at regular intervals within a given linear sequence
(strand) of a protein (as in the alpha helix) or between two adjacent
strands (as in beta sheets and reverse turns)
Figure:
Secondary Structure (purple -alpha helices, yellow - beta
strands. Image made with
VMD)
- tertiary structure: the overall three dimensional shape of a
protein, often represented by a backbone trace
Figure: tertiary structure (calmodulin - image made with
VMD)
- quaternary structure: oligomeric structure of a multisubunit
protein in which separate proteins chains associate to form dimers,
trimers, tetramers, and other oligomers. The different chains in the
oligomers may be the same protein (homooligomers) or a combination of
different protein chains (heteroliogomers). The different chains within
the oligomer may be held together by noncovalent intermolecular forces
or may also contain covalent interchain disulfides.
Figure: Quaternary structure (4 chains of hemoglobin - Image made with
VMD)
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Chapter 2B:
Probing Composition, Sequence and Conformation
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