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How are the 4 protein structures related?

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  1. They give rise to the final 3-D structure of the molecule.

    Most proteins fold into unique 3-dimensional structures. The shape into which a protein naturally folds is known as its native state.. Biochemists often refer to four distinct aspects of a protein's structure:

    Primary structure: the amino acid sequence.

    Secondary structure: regularly repeating local structures stabilized by hydrogen bonds. The most common examples are the alpha helix and beta sheet. Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.

    Tertiary structure: the overall shape of a single protein molecule; the spatial relationship of the secondary structures to one another. Tertiary structure is generally stabilized by nonlocal interactions, most commonly the formation of a hydrophobic core, but also through salt bridges, hydrogen bonds, disulfide bonds, and even post-translational modifications. The term "tertiary structure" is often used as synonymous with the term fold.

    Quaternary structure: the shape or structure that results from the interaction of more than one protein molecule, usually called protein subunits in this context, which function as part of the larger assembly or protein complex.

    The sequence,type and number of the the different amino acids in the protein determine the final 3-D shape and it is this 3-D shape which determines its function.Eg. Collagen is a fibrous protein (long and rope-like), insoluble and is found in blood vessel walls and tendons as a structural protein.

    Most enzymes are globular and soluble with a precise 3-D site (active site) in its structure to enable the binding of its substrate. This structure enables them to function in metabolism.

    Haemoglobin structure enables the binding of O2

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