Protein Chemistry By Dr Pooja For MBBS 1st Proff

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Protein Chemistry -
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Protein chemistry is the study of the structure, function, and properties of proteins, which are essential macromolecules in all living organisms. Proteins perform a wide array of functions, including catalysis, structural support, transport, communication, and defense.

Structure of Proteins -
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Primary Structure -
Sequence of amino acids in a polypeptide chain.
Determined by the genetic code in DNA.
Peptide bonds link amino acids together.

Secondary Structure -
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Local folding of the polypeptide chain into α-helices and β-pleated sheets.
Stabilized by hydrogen bonds between the backbone amide and carbonyl groups.
Examples: α-helix (spiral shape), β-sheet (sheet-like structure).

Tertiary Structure -
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Overall three-dimensional shape of a single polypeptide chain.
Stabilized by various interactions: hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.
Determines the protein's function.

Quaternary Structure -
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Assembly of multiple polypeptide chains (subunits) into a functional protein.
Examples: hemoglobin (four subunits), DNA polymerase.

Protein Function -
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Enzymes -
Biological catalysts that speed up biochemical reactions.
Specificity for substrates and regulation by inhibitors and activators.
Examples: amylase, DNA polymerase, proteases.

Structural Proteins -
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Provide support and shape to cells and tissues.
Examples: collagen (connective tissue), keratin (hair, nails).

Transport Proteins -
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Carry molecules across cell membranes or through the bloodstream.
Examples: hemoglobin (oxygen transport), albumin (carries various substances in blood).

Signal Proteins -
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Involved in cell communication and signaling pathways.
Examples: insulin (regulates glucose metabolism), growth factors.

Defense Proteins -
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Protect the body from pathogens and foreign substances.
Examples: antibodies (immune response), complement proteins.

Protein Synthesis -

Transcription -
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DNA is transcribed into messenger RNA (mRNA) in the nucleus.
RNA polymerase catalyzes the formation of mRNA from the DNA template.

Translation -
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mRNA is translated into a polypeptide chain at the ribosome.
Transfer RNA (tRNA) brings amino acids to the ribosome, matching the mRNA codons with anticodons.
The ribosome catalyzes peptide bond formation between amino acids.

Protein Folding and Stability -
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Chaperones -
Assist in the proper folding of proteins.
Prevent misfolding and aggregation.

Denaturation -
Loss of protein structure due to external stress (heat, pH changes, chemicals).
Often irreversible and leads to loss of function.

Renaturation -
Refolding of denatured proteins under favorable conditions.
Not always possible.

Clinical Relevance -
Protein Misfolding Diseases -
Abnormal protein folding leads to diseases like Alzheimer's, Parkinson's, and prion diseases.
Accumulation of misfolded proteins forms toxic aggregates.

Enzyme Deficiencies -
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Genetic mutations can lead to dysfunctional enzymes, causing metabolic disorders.
Examples: phenylketonuria (PKU), lactose intolerance.
Understanding protein chemistry is fundamental for diagnosing and treating various medical conditions, as well as for the development of new drugs and therapies. 🌟🧬💉

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