Macromolecules pt 3
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Transcript Macromolecules pt 3
Four Levels of Protein
Structure
Biological activity of protein is determined by
these levels
Primary structure is the sequence of amino
acids in a polypeptide (Usually read N-C)
Secondary structures are localized folds or
helices that form within a region of a
polypeptide
Tertiary structures are larger folding events that
are stabilized by interactions between R groups
Quaternary structure is the interaction of
multiple polypeptides within one active proteins
Primary Structure
Sequence of amino acids within
a single polypeptide
Are often similar among proteins
of similar function
Usually written from amino
terminus to carboxy terminus
Can also provide some insight
into additional structures by the
position of particular groups of
amino acids
Secondary Structure
Localized within regions
of polypeptide
Stabilized by hydrogen
bonding
a helix-stabilized by
frequent polar groups
Right handed helices
b-pleated sheets are
formed by consecutive
polar groups on two
regions of polypeptide
Tertiary Structure
Large folding events that are
stabilized by interactions
between amino acids
Hydrophobic interactions
Disulfide bridge
Very stable bond formed
between two distant cysteine
residues
Ionic interactions
-Hydrogen bonds form
between polar groups
Nonpolar regions generally
internalize in structure
Strong bond between
oppositely charged side groups
Quaternary Structure
Only seen in compound
proteins
Interactions are
maintained between
polypeptide chains by
bonds similar to tertiary
structure
Function is often unique
to quaternary structure
Individual components
are unable to
accomplish task alone
Protein Structure Revisited
Fig. 5-23
Denaturation
Normal protein
Renaturation
Denatured protein
Protein Conformation
The 3D structure in which the protein is
biologically active is called the active conformation
Denatured protein has lost its active conformation
Shape of a protein is consistent under identical
conditions
Proteins will attempt to find the lowest energy form
under conditions
Conditions that affect conformation
Solvent (polar versus non-polar),pH, temperature and
chemical agents (2-mercaptoethanol)
Protein summary
Very important biological macromolecules that
perform a wide array of functions
Polymers of amino acids
20 natural amino acids that have distinct R side
groups
The side groups determines the shape and
function of a polypeptide
There are four levels of structural organization
of proteins
Nucleic Acids
Deoxyribonucleic acid (DNA) and ribonucleic
acid (RNA)
Polymer of nucleotides
Store cellular information
Molecules of inherited information
Basis for genetics
Often large, very complex molecules
Serve as templates for proteins
Help control regulation of cellular functions
Nucleotides
Comprises:
A pentose
sugar
A nitrogen
containing
base
An organic
phosphate
group
Bases
Two kinds of bases
Pyrimidines are
single ring
structures
Purines are double
ring structures
cytosine, thymine
and uracil
adenine and
guanine
In DNA G-C and
A-T interactionss
Pentoses
Deoxyribose in DNA and Ribose in RNA
Only difference is the lack of an Oxygen at carbon 2 in
deoxyribose
Ring structures
Nucleic Acid Structure
Phosphate group is attached
to carbon 5 of pentose
Oxygen of Phosphate forms
a phosphodiester bond with
the OH group on carbon 3
of the pentose
Strands have a 5’ end and a
3’ end
Fig. 5-27ab
5' end
5'C
3'C
Nucleoside
Nitrogenous
base
5'C
Phosphate
group
5'C
3'C
(b) Nucleotide
3' end
(a) Polynucleotide, or nucleic acid
3'C
Sugar
(pentose)
DNA vs RNA
Both are important for cell function
DNA is double stranded and longer-lived
Both can serve as a template for the synthesis of
the other
RNA is single stranded and has shorter life
DNA to RNA is very common (transcription)
RNA to DNA occurs only with retroviruses
(reverse transcription)
Both have 5’-3’ orientations
DNA Double Helix
Structure elucidated by Watson and
Crick
Two strands are anti-parallel
From work of Wilkens and Franklin
5’end of each strand aligns with 3’
end of complementary strand
Bases pair by hydrogen bonding
A-T (2 bonds)and G-C (3 bonds)
Since strands are complementary
they serve as a template for opposite
strand
Strands make Double Helix structure
(twisted ladder)