Physical-chemical determinants of turn conformations in globular proteins

The reverse turn as a polypeptide conformation in globular proteins.

The reverse turn, involving four consecutive amino acids, as a tertiary conformation in globular proteins is defined in terms of dihedral angles, the C(1) (alpha)...C(4) (alpha) distance and the O(1)...H-N(4) hydrogen bond distance. In seven proteins we find 125 examples of turns, comprising 33% of the amino acids in these proteins, as compared with 34% of the residues forming helices and only ...

Conformations of proteins in equilibrium.

We introduce a simple theoretical approach for an equilibrium study of proteins with known native-state structures. We test our approach with results on well-studied globular proteins, chymotrypsin inhibitor (2ci2), barnase, and the alpha spectrin SH3 domain, and present evidence for a hierarchical onset of order on lowering the temperature with significant organization at the local level even ...

Physical and chemical properties of soybean proteins.

Investigation of the Physical, Chemical and Antioxidant Properties of Nanoliposomes Loaded with Quinoa Seed Hydrolyzed Proteins

Background and Objectives: Encapsulation is a process; by which, a susceptible compound is surrounded with a membrane or matrix that is able to release its contents at a controlled speed under certain conditions. In recent years, popularity of adding bioactive compounds to food products has increased. These compounds are usually sensitive to environmental, processing and/or gastrointestinal con...

Stabilization of gamma-turn conformations in peptides by disulfide bridging.

The ideal y-turn conformation in peptides is stabilized by the formation of two intramolecular hydrogen These are between the NH of residue i and the C=O of residue i + 2 (1 3, CJ and the C=O of residue i and the NH of residue i + 2 (3 1, C7).334 While this reverse-turn structural feature has been observed in proteins, '~~ unambiguous characterization of this conformation has yet to be realized...