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a confused dna
Proteins (Polypeptides)
• Contain carbon, hydrogen, oxygen, nitrogen, and
sulfur
• Basic building block is the amino acid
• There are 20 different kinds of amino acids
• Amino acids are bonded together by peptide bonds
(polypeptides).
Peptide Bonds
2
Proteins (Polypeptides)
Proteins play a central role in the structure and
metabolism of all living organisms.
All amino acids contain an amino group (-NH2) and a carboxylic acid group (-COOH).
Both of these groups are attached to a central carbon atom, known as the α-carbon.
The backbone of an amino acid contain three atoms C-C-N.
The R group varies between different amino acids. The following chart
shows the different R-groups in the 20 amino acids that make up all of
the proteins in living organisms.
Table: The 20
amino acids
found in all living
things.
Amino acids in solution
The carboxyl group (like all acids) loses a hydrogen ion (H+) to become COO-.
The amino group (like all bases) gains a hydrogen ion to become NH3+. In
solution, therefore, an amino acid carries both positive and negative charges. For
this reason, it is known as a zwitter ion, meaning double ion.
An amino acid can behave as an acid or a base. Any molecule that does this is
described as amphoteric. Amino acids can resist a change in pH and therefore, it
can act as a buffer.
How amino acids form Protein
Proteins form long chains of amino acids that are joined together by peptide
bonds.
All proteins are complex molecules and biochemists look at their structure at four
different levels:
1. Primary Structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure
Structure of proteins
1. Fibrous Protein:
They are physically tough and insoluble in
water.
Collagen and keratin are two such fibrous
proteins.
2. Globular Protein:
Spherical or globular in shape.
Most are soluble in water and they tend to
be functional proteins.
Example: enzymes-are roughly spherical
and soluble.
How stable are proteins?
Proteins are very sensitive to increases in temperature and undergoes
change. Because, the final shape of globular proteins is maintained by
relatively weak molecular interactions such as hydrogen bonds that are easy
to break.
As the temperature rises above 400C, the molecular variation increases to
the point where bonds holding together the tertiary or quaternary structure
break and the shape of the molecule changes. This is known as
Denaturation.
Different proteins are denatured at different temperatures but the lethal
temperature for organisms is reached when the first vital proteins become
denatured, usually at 450C.
Proteins can also be denatured by adverse chemical conditions. Any
chemical that affect the weak bonds tend to alter the overall structure and
even a slight change in protein shape can mean loss of function. Some
proteins are particularly sensitive to changes in pH.
Nucleic acid
Nucleic Acids contain carbon, hydrogen, oxygen, nitrogen and phosphorus.
There are two types of nucleic acid:
a) Deoxyribonucleic acid (DNA)
b) Ribonucleic Acid (RNA)
3. Transfer RNA:
is found in the cytoplasm and is a carrier molecule, bringing amino acids to
the ribosomes for assembly into a new amino acid chain, according to the
order specified on the mRNA code.
DNA: RNA:
A T A U
C G C G
sugar phosphate sugar phosphate sugar phosphate sugar ...
T A C G
¦ ¦ ¦ ¦
A T G C
sugar phosphate sugar phosphate sugar phosphate sugar ...
Transcription DNA
mRNA
Translation
Ribosome
Polypeptide
(protein)
The Central Dogma
The Dogma is: DNA -> RNA ->
Protein
The Central Dogma is:
DNA is transcribed to RNA
which is translated to protein.
Translation
Translation is the process where ribosomes synthesize
proteins using the mature mRNA transcript produced
during transcription.
Gene Expression
GENE
DNA
From gene
to
protein mRNA in nucleus
mRNA in cytoplasm
Polypeptide
ACTIVE
PROTEIN