R group of amino acids

The R groups of amino acids determine their unique biochemical functions. Amino acids are classified as basic, acidic, aromatic, aliphatic, or sulfur-containing based on the properties of their R groups. 

R, R group of amino acid 5aR, testosterone 5a-reductase cr-R, sigma receptor (metabotropic or ionotropic)... 

Hydrogen bonds are formed between the side chain (R group) of amino acids having a hydrogen donor group and an acceptor group. 

R group. An abbreviation used to denote an organic substituent such as the R groups of amino acids. 

Globular proteins contain varying amounts of a-helix and P-pleated sheet folded into higher levels of structure called the tertiary structure. The tertiary structure of a protein is maintained by attractive forces between the R groups of amino acids. These forces include hydrophobic interactions, hydrogen bonds, ionic bridges, and disulfide bonds. 

What properties of the side chains (R groups) of amino acids are important in affeding the amino acids overall biochemical behavior Give examples to illustrate your reply. 

The 20 different R groups of amino acids are important factors in determining the physical and chemical properties of proteins that contain the amino acids. Acid-base behavior is... 

All proteins are polymers of amino acids, which are bifunctional organic compounds that contain both an amino group and a carboxylate group. Differences in the R groups of amino acids cause differences in the properties of amino acids and proteins. 

Remarkably, the resulted total munber (20) is exactly the same as the available number of and interstices (excluding central octahedral interstice) in face-centered cubic stmcture, see the right side in Figures 4.23 and 4.25 these holes, once occupied by the R groups of amino acids will compact the tertiary structure of proteins. 

Moreover, the fact that the R groups of amino acids can be classified in two groups according to their weight is paralleling the two types of cavities available in a face centered cubic structure, with interstices precisely occupied by these R groups (Purves et al., 2001). 

Tertiary structure refers to the large-scale twists and folds within the protein. These are maintained by interactions between the R groups of amino acids that are separated by long distances in the chain sequence. 

Tertiary A protein folds into a compact, three-dimensional shape stabilized by interactions between R groups of amino acids... 

The tertiary structure of a protein involves attractions and repulsions between the R groups of the amino acids in the polypeptide chain. As interactions occur between different parts of the peptide chain, segments of the chain twist and bend until the protein acquires a specific three-dimensional shape. The tertiary structure of a protein is stabilized by interactions between the R groups of the amino acids in one region of the polypeptide chain and the R groups of amino acids in other regions of the protein (see Figure 16.7). 

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