Proteins (pronounced /protinz/) are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous

form, facilitating a biological function. A polypeptide is a single linear polymer chain of amino acids bonded together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues. The sequence of amino acids in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteineand in certain archaeapyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes. Building block of protein Amino acid (pronounced /mino ..., mano ..., mno .../) are molecules containing an amine group, a carboxylic acid group and a side-chain that varies between different amino acids. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen. They are particularly important in biochemistry, where the term usually refers to alpha-amino acids Classification of amino acid Classification Amino Acid Glycine Alanine Valine Leucine Nonpolar Isoleucine Proline Methionine Phenylalanine Tryptophan Polar Serine

Threonine Asparagine Glutamine Cysteine Tyrosine Aspartic Acid Glutamic Acid Lysine Basic (Polar) Arginine Histidine Protein structural levels Biochemists refer to four distinct aspects of a protein's structure: [edit]Primary structure Primary structure is practically a synonym of the amino acid sequence. It can also contain informations on amino acids linked by disulfide bonds. Primary structure is typically written as a string of three letter sequences, each representing an amino acid, separated by dashes, or it is written as a string of letters with each individual letter representing one of the twenty biologically useful amino acids.

Acidic (Polar)

[edit]Secondary structure Secondary structure elements are elementary structural patterns that are present in most,if not all,known proteins. These are highly patterned sub-structures --alpha helix and beta sheet-- consisting of loops between elements or segments of polypeptide chain that assume no stable shape. Secondary structure elements, when mapped on the sequence and depicted in the relative position they have in respect to each other, define the topology of the protein. It is also relevant to note that hydrogen bonding between residues is the cause for secondary structure features; secondary structure is usually described to beginning biochemists as (almost) entirely independent of residue side-chain interactions.

[edit]Tertiary structure Tertiary structure is the name given to refer to the overall shape of a single protein molecule. Although tertiary structure is sometimes described (especially to beginning biology and biochemistry students) as being a result of interactions between amino acid residue side chains, a more correct understanding of tertiary structure is the interactions between elements of secondary protein structure, i.e. alpha-helices and beta-pleated sheets. Tertiary structure is often referred to as the "fold structure" of a protein, since it is the result of the complex three-dimensional interplay of other structural and environmental elements. [edit]Super-tertiary structure (protein modules) Some literature refers to elements of super-tertiary structure, which often refers to elements of folding that, for whatever reason, do not neatly fit into the category of tertiary structure. Often this level of distinction is saved for graduate level coursework. Protein denaturation can be a reversible or an irreversible process, i.e., it may be possible or impossible to make the protein regain its original spatial conformation. [edit]Quaternary structure Quaternary structure is the shape or structure that results from the union of more than one protein molecule, usually called subunit proteinssubunits in this context, which function as part of the larger assembly or protein complex. In addition to considering the quaternary level of protein structure, biochemistry students should also keep in mind that proteins may shift between several similar structures in the process of performing their biological function. In the context of these functional rearrangements, such tertiary or quaternary structures are usually referred to as "conformations," and transitions between them are simply calledconformational changes.

CELL MEMBRANE