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Protein loops are patternless regions which connect two regular secondary structures. They are generally located on the protein's surface in solvent exposed areas and often play important roles, such as interacting with other biological objects.

Mass spectrometry (MS) is a commonly used, high-throughput tool for studying proteins. The procedure of MS-based protein identification involves digesting proteins into peptides, which are then separated, fragmented, ionised, and captured by mass spectrometers.

Various biophysical techniques such as nuclear magnetic resonance, cryo-EM, small-angle X-ray scattering, mass spectrometry, atomic force microscopy and single-molecule fluorescence resonance energy transfer, etc., are used to study the pH, temperature, or ligand-induced conformational modulations.

In order to determine the quantity of protein in food, it is important to have standardized analytical methods. Several methods exist that are used in different food industries to quantify the protein content in foods and these include the Kjeldahl, Lowry, Bradford and total amino acid content methods.

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Proteins fold into stable three‐dimensional shapes, or conformations, that are determined by their amino acid sequence. The complete structure of a protein can be described at four different levels of complexity: primary, secondary, tertiary, and quaternary structure.