Proteins Structure And Functionality

This discussion of protein structure begins with amino acids as building blocks of proteins, followed by different levels of protein structure. Chemical forces that maintain the protein structure or change the structure level are then explained. Interactions of proteins, especially proteinprotein, protein-lipid and protein-water interactions, are briefly reviewed. Finally, structure-function relationships are discussed. For more details, readers are referred to the work by R. D. Ludescher (1).

Four levels of structural organization in proteins can be distinguished: primary, secondary, tertiary, and quaternary structures. These terms refer to the amino acid sequence, the regular arrangements of the polypeptide backbone, the three-dimensional structure of the globular protein, and the structures of aggregates of globular proteins, respectively. In addition to this classification, the su-persecondary structure is frequently described, which refers to association products of secondary structure, eg, coiled-coil a-helix in which two a-helixes are wound around each other, a-/? mixed structure, and /ta/?-unit structure (2). Furthermore, domain refers to a structurally independent unit that has the characteristics of a small globular protein (3). A domain is composed of supersecondary structures. Domains often have a specific function. A functional motif (sequences shorter than 25 amino acids) or domain (larger than 50 amino acids) is part of a protein that serves a particular function (4).

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