Proteins for foods, in addition to providing nutrition, should also possess specific functional properties that facilitate processing and serve as the basis of product performance. Functional properties of proteins for foods connote the physicochemical properties which govern the behavior of protein in foods. This general article collates the published information concerning the major functional properties of food proteins, e.g., solubility, binding properties, surfactant properties, viscogenic texturizing characteristics, etc. The effects of extraction and processing on functional properties and possible correlations between structure and function are discussed, in relation to practical performance in food systems. Modification of proteins to improve functional characteristics is briefly mentioned.

Functional properties of proteins in foods: A survey

Conformational states and biological activity of cyclic peptides

The conformational space accessible to the N-acetyl N′-methyl amides of the 20 naturally occurring amino acids has been explored extensively with the aid of empirical energy functions, and many minima have been located. The statistical weights for all minima with energy ≤ 3 kcal above the lowest for each residue have been calculated. In numerous cases, the conformation of lowest energy does not possess the highest statistical weight, thereby emphasizing the importance of considering the conformational librations when comparing theoretical and experimental results. The calculated minimum-energy conformations, as well as those of highest statistical weight, are for the most part in good agreement with experimental results from studies of these compounds in solution and in the crystalline state.

Energy Parameters in Polypeptides. VI. Conformational Energy Analysis of the N‐Acetyl N′‐Methyl Amides of the Twenty Naturally Occurring Amino Acids

Previous energy calculations for isolated (single‐stranded) homopolymer polyamino acids, to find the most stable regular (helical) conformations, have been extended to poly‐L‐aspartic acid, poly‐L‐glutamic acid, and several related compounds. Since rotation about all single bonds (including the acid and ester groups of side chains) was taken into account, it was necessary to obtain expressions for the torsional potentials for these internal rotations. The computed helix sense was found to agree with the experimental one in all cases except one, using a single set of potential functions and parameters. The various contributions to the total energy are all important in their influence on the conformation. For most of the polymers studied, there are only four principal side‐chain conformations of low energy, two for the right‐handed and two for the left‐handed helix sense. Essentially the same set of four conformations was found for poly‐L‐aspartic acid and all of its esters; a different set of four conforma...

Conformational Analysis of Macromolecules. V. Helical Structures of Poly‐L‐aspartic Acid and Poly‐L‐glutamic Acid, and Related Compounds

At one point in the history of protein chemistry it was thought that—because of the vast number of possible sequences—proteins ought to exist in a countless number of forms befitting any conceivable function or structure. In fact, as the number of known amino acid sequences continues to mount, it is becoming abudantly clear that there is a practical limit to the number of types of protein structures that exist in living systems on Earth. Thus, although the number of possible sequences for 20 amino acids arranged randomly in strings of 350 units is a superastronomical 20350, certainly nowhere near that number of protein sequences has ever or will ever exist. Instead, a small number of genetically encoded protein structures has been expanded by the general route of “duplication and modification.” The duplications come in various degrees, from the very short to the supragenic or chromosomal. Postduplication modification mostly takes the form of base substitutions leading to amino acid replacement, and, theoretically, the history of any protein ought to be evident by appropriate comparison of the diverging sequences.

Redundancies in Protein Sequences

Minimization of polypeptide energy, iii. Application of a rapid energy minimization technique to the calculation of preliminary structures of gramicidin-s.

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Minimization of polypeptide energy, iii. Application of a rapid energy minimization technique to the calculation of preliminary structures of gramicidin-s.