Folding and Aggregation

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This discussion is focused on the nature, structure and functions of proteins, how these are formed and the role played by folding and aggregation in protein and the various interactions that are part of protein functions.
Proteins are a class of macromolecules, also described as polymers of amino acids present in all biological organisms and made up of carbon, hydrogen, nitrogen and oxygen.


The three dimensional structures of proteins aid in delineating protein functions at a molecular level and the structure of proteins are determined usually with X ray crystallography, NMR spectroscopy etc. Some structural features of proteins would be necessary to perform certain biochemical functions although multifunctional and structural proteins may have higher number of residues than the average of 300 residues. Large aggregates are formed as a result of folding from protein subunits and actin molecules also assemble into actin filaments.
The protein structure has four distinct features including amino acid sequence of peptide chains as seen in a primary structure, secondary structures which are regular sub structures, such as strands of beta sheet, tertiary structure as seen in the three dimensional structure of a single protein molecule and quaternary structure which represents a complex of polypeptide chains and protein molecules (Copley, 1997; Berg, 2002). Proteins tend to transition between structures to perform the biological functions and this would be known as conformational changes.
The primary structure of proteins with amino acid sequences would be held together by covalent peptide bonds and t ...
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