free download primary structure of protein

Linkage of many amino acids through peptide bonds results in an unbranched chain called a polypeptide.

For example, a tripeptide composed of an N-terminal valine, a glycine, and a C-terminal leucine is called valylglycylleucine.

When a polypeptide is named, all amino acid residues have their suffixes (-ine, -an, -ic, or -ate) changed to (- yl) with the exception of the C-terminal amino acid.

All amino sequences are read from the N- to the C-terminal end of the peptide.

The free amino end of the peptide chain(N-terminal) is written to the left and the free carboxyl end to the right (C-terminal).

Prolonged exposure to a strong acid or base at elevated temperatures is required to hydrolyze these bonds nonenzymically.

Peptidebondsare not broken by conditions that denature proteins, such as heating or high concentrations of urea.

In proteins, amino acids are joined covalently by peptide bonds, which are amide linkages between the α-carboxylgroup of one amino acid, and the α-aminogroup of another.

If the primary structures of the normal and the mutated proteins are known, this information may be used to diagnose or study the disease.

Understanding the primary structure of proteins is important because many genetic diseases result in proteins with abnormal amino acid sequences, which cause improper folding and loss or impairment of normal function.

The sequenceof amino acids in a protein is called the primary structure of the protein.

The complexity of protein structure is best analyzed by considering the molecule in terms of four organizational levels primary, secondary, tertiary, and quaternary.

The linear sequence of the linked amino acids contains the information necessary to generate a protein molecule with a unique three-dimensional shape.The twenty amino acids commonly found in proteins are joined together by peptidebonds.

Free download primary structure of protein