The primary structure of a protein refers to the specific sequence of amino acids in the protein chain linked together by peptide bonds. The unique amino acid sequence determines how the protein folds into its 3D structure and performs its function. While different sequences can result in very different protein shapes and functions, the sequence is precisely determined by the mRNA template which is transcribed from DNA.
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Test Bank for Lehninger Principles of Biochemistry 6e NelsonLauriewest24
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The new sixth edition of this best-selling introduction to biochemistry maintains the clarity and coherence that so appeals to students whilst incorporating the very latest advances in the field, new worked examples and end of chapter problems and an improved artwork programme to highlight key processes and important lessons.
ISBN-13: 978-1429234146
ISBN-10: 1429234148
Describes the structural organisation of proteins with example and its determination, interrelationship b/w structure and function of proteins, also biologically important peptides is covered.
by Dr. N. Sivaranjani, MD
Test Bank for Lehninger Principles of Biochemistry 6e NelsonLauriewest24
This is the Test Bank for Lehninger Principles of Biochemistry 6e Nelson. Email lauriewest24@gmail.com for full access.
The new sixth edition of this best-selling introduction to biochemistry maintains the clarity and coherence that so appeals to students whilst incorporating the very latest advances in the field, new worked examples and end of chapter problems and an improved artwork programme to highlight key processes and important lessons.
ISBN-13: 978-1429234146
ISBN-10: 1429234148
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The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
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The slides explain the structures of proteins, the bond stabilizing the structure of amino acids, the different types of protein structures, the applied aspects and the newer advances in the protein structure.
Solid-phase peptide synthesis (SPPS), pioneered by Robert Bruce Merrifield,[1] caused a paradigm shift within the peptide synthesis community, and it is now the standard method for synthesizing peptides and proteins in the lab.
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- These are slides of the talk given at IEEE International Conference on Software Testing Verification and Validation Workshop, ICSTW 2022.
2. PRIMARY STRUCTURE
Sequence of amino acids in protein linked by
covalent amide (peptide) bonds
3. CONDENSATION AMINO ACIDS: AMIDES OR
PEPTIDE BONDS
O O O
H2N C + H2N C + H2N C Amino acids condense
HC OH CH OH
CH2 OH
to form amides – or
CH3 alanine glycine glutamine CH2
H2C peptide bonds
Peptide or amide bond C
H2N O
O
+ O Protein chain made up
H3N C H O
HC N C of amino acids
H HC N C - covalently bonded by
CH3 CH O
CH3
CH2
amide bonds
H2C
C
H2N O
4. SEQUENCE MATTERS
Functioning proteins have
O O
O
unique primary structure –
H2N C + H2N C + H2N C
sequence of amino acids
HC OH CH2 OH CH OH
CH3 alanine glycine glutamine CH2
in the chain
H2C
This primary sequence
Peptide or amide bond C determines how the
H2N O
O protein folds into 3-D
O
H3N
+
C H O shape required for protein
HC N C
H HC N C -
function
CH3 CH O
CH3 Sequence has a free
N-terminal amino acid CH2 C-terminal amino acid
H2C amino end (N-terminal
alanine (free amino end) glutamine (free carboxyl end)
C
amino acid)
H2N O
Sequence has free
carboxyl end (C-terminal
amino acid
5. SEQUENCE MATTERS
O O O
H2N C + + H2N When 3 amino acids
H2N C C
HC OH CH2 OH CH OH reacted together, 6
CH3 alanine glycine glutamine CH2 possible different
H2C
tripeptides result
C
H2N O
Possible sequences
Sequence of amino acids
in proteins determined by
ala-gly-gln
sequence of nucleotides
ala-gln-gly on m-RNA, which is
gly-ala-gln transcribed from DNA
gly-gln-ala
gln-ala-gly
gln-gly-ala
6. Vasopressin (antidiuretic
hormone
• 9 amino acid polypeptide
forms cyclic structure
• N terminal amino acid:
glycine
• No C terminal amino acid
(due to ring structure)
• Conserves body fluids
, reduces loss of water in
urine
• Leads to constriction of
blood vessels, increase in
blood pressure
POLYPEPTIDE HORMONES
7. Oxytocin
• 9 amino acid polypeptide with
cyclic structure
• N-terminal amino acid: glycine
• No C-terminal amino acid
• Well studied effects:
• Stimulates milk production
• Stimulates muscle contraction
for birth
• Promotes maternal behavior
• Possible association with
development of human
bonding an interpersonal
relationships
• Compare structure to
vasopressin: 2 amino acids
different – very different
physiological effects!
POLYPEPTIDE HORMONES
8. Lysozyme
• Enzyme breaks down
bacterial cell walls
• Found in egg
whites, human tears
• Single polypeptide chain
of 129 amino acids
• N-terminal amino acid is
lysine
• C-terminal amino acid is
leucine
Disulfide bonds considered
to be part of tertiary
structure.
PROTEIN PRIMARY STRUCTURE