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Structure and Properties of Proteins: Amino Acids and Their Classification, Study notes of Biochemistry

An introduction to the structure and properties of proteins, focusing on the role of amino acids. It explains the difference between simple and conjugated proteins, the presence of prosthetic groups, and the classification of conjugated proteins. The document also discusses the three main groups of amino acids based on the polarity and charge of their side chains, with examples of nonpolar, uncharged polar, and charged polar amino acids.

Typology: Study notes

Pre 2010

Uploaded on 07/23/2009

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Download Structure and Properties of Proteins: Amino Acids and Their Classification and more Study notes Biochemistry in PDF only on Docsity! Today we begin our discussion of the structure and properties of proteins. Proteins consist in whole or large part of amino acids. Simple proteins consist only of amino acids. Conjugated proteins contain a non-amino acid component called the prosthetic group. The prosthetic group can be an organic or an inorganic component such as a sugar molecule or a metal ion. Conjugated proteins are classified by the prosthetic group. Examples are nucleoproteins, lipoproteins and metalloproteins that contain nucleic acids, lipids and metal ions respectively. There are approximately 20 different amino acids found in proteins. Most of the 20 common amino acids (a.a.) have the following general structure- The amino acids are distinguished from each other by the R group often referred to as the side-chain in proteins. The amino acids have an amino and a carboxylic acid group that are joined to the same carbon atom. This carbon atom is referred to as the α carbon. In proteins, amino acids are covalently linked to one another by peptide (amide) bonds involving the carboxyl group of one a.a. and the amino group of another a.a. to form linear polymers- Asparagine and glutamine have amide groups as part of their side chains. They differ from one another by a methylene, -CH2-, unit. Tyrosine has a phenolic group. Cysteine has a mercapto, -SH, group. The mercapto group is only weakly polar. The a.a. with charged polar side chains have basic or acidic groups that are partly or completely ionized at pH 7.0. The basic a.a. include lysine, arginine and histidine. Because they are basic, they will associate with H+ in solution to form the positively charged groups as shown in Table 4-1 for lysine and arginine. Lysine has an amino group on the ε (epsilon) carbon atom. The basic group of arginine is referred to as the guanidino group- The conjugate acid form shown in Table 4-1 is called the guanidinium group- The basic group of histidine is an imidazole group. The imidazole group of histidine is less basic than the amino or guanidino group so that at pH 7.0 it is predominately unprotonated as shown in Table 4-1. The acid form is called the imidazolium group- The acidic amino acids include aspartic and glutamic acids that differ from one another by a methylene unit. Because the carboxylic acid groups are acidic, they will dissociate to give a H+ and the negatively charged carboxylate group at pH 7.0 as shown in Table 4-1. Note that these groups are referred to as the β and χ carboxyl groups because they are attached to the β and χ carbon atoms. Note that each a.a. has a 3 letter and a 1 letter abbreviation. This is useful in representing the sequence of a.a. in a protein.
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