Protein structure refers to the three-dimensional arrangement of amino acid atoms in a protein molecule. Proteins are polymers formed from sequences of amino acids, the monomers of the polymer. A single amino acid monomer may also be called a residue indicating a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule in each reaction attaching to one another with a peptide bond. By convention, a chain under 30 amino acids is usually identified as a peptide, rather than a protein. In order to perform biological function, protein molecules fold into one or more spatial conformations driven by lots of non-covalent interactions such as Van der Waals forces, hydrophobic packing, hydrogen bonding, and ionic interactions. To understand the functions of proteins at a molecular level, it is very important to determine their three-dimensional structure. This is the topic of the research field of structural biology, which applies techniques, such as NMR spectroscopy and X-ray crystallography, to determine protein structures. Now, bioinformaticians at Creative Proteomics are proud to tell you we are open to help you with Protein Structure Analysis Service!
The size of protein structures ranges from tens to several thousand amino acids. Proteins are classified as nanoparticles by physical size (1-100 nm). Very large aggregates can be formed from protein subunits. For instance, many thousands of actins assemble into a microfilament. A protein may experience reversible structural changes in performing its biological functions. The alternative structures of the same protein molecule are referred to as distinct conformational isomers, or simply, transitions, and conformations between them are called conformational changes. There are four distinct levels of protein structure: primary structure, secondary structure, tertiary structure, and quaternary structure.
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