Protein

“The peptide is formed between the amino group (-NH2) of the first amino acid and Carboxyl group (-COOH) of the second amino acid by eliminating one molecule of water.” The amino acids are held together in a protein by covalent peptide bonds or linkages. These bonds are rather strong and serve as the cementing material between the individual amino acids. …

Marcello Malpighi described the RBCs in 1665.Felix Hope Seyler in 1862 isolated pure Hemoglobin.Christian Bohr in 1904 discovered that hemoglobin is the transporter of oxygen.In 1912 Kutster established the structure of hemoglobin.Hans Fischer synthesized heme in the laboratory in 1920 (Nobel prize, 1930).In 1945, Linus Pauling (Nobel prize, 1954) described abnormal hemoglobins.Max Perutz (Nobel Prize, 1962) studied the 3D structure …

Protein folding has nothing to do with laundry. It is, in fact, one of the central questions in biochemistry. Protein folding is the continual and universal process whereby the long, coiled strings of amino acids that make up proteins in all living things fold into more complex three-dimensional structures. By understanding how proteins fold, and what structures they are likely …

Proteins are very important in biological systems as control and structural elements. Control functions of proteins are carried out by enzymes and proteinaceous hormones. Enzymes are chemicals that act as organic catalysts (a catalyst is a chemical that promotes but is not changed by a chemical reaction). What are Proteins? The building block of any protein is the amino acid, …

One of the most important proteins in the human body is MYOGLOBIN (symbol as MB or Mb). Today we are discussing Myoglobin in this post. It found in muscle tissue, where it binds oxygen, helping to provide extra oxygen to release energy to power muscular contractions. Let us come to the history of Myoglobin. It was the first protein they determined whose structure. In 1958, Max …

Do you know the tertiary structure of proteins? All Globular Proteins are tertiary proteins. These have consisted of a small helix and elongated structures with considerable length and small cross-sectional area. In the Globular protein formation, few of the bonds are involved. They are Hydrogen bonds, disulfide bonds, hydrophobic interactions, and ionic interactions. This is a very compact three-dimensional structure, …

Secondary Structure of Protein Organizational assumption points are No rotation occurs around the peptide bond (as it is partly double-bonded in nature). The chain of amino acids forms a rhythmical structure – forming a repeating pattern. That the maximum number of interactions from Hydrogen bonding possible are occurring, independent of the type of residue (amino acid). Basic explanation of the …

The peptide bond , strong, is responsible. It has adjacent atoms in the same plane where the fact that it is coplanar  and Linear molecule. It has a partial double bond character of resonance between two forms. This confers it an almost full strength. The rotations are absent and there are two possible conformations for binding:. Cis or trans This …