Ultrasonic Studies and Intermolecular/Interionic Interactions Of L-Isoleucine, L-Proline and L-Glutamine in Aqueous K2SO4, KNO3 and KCI Solutions

Riffat Basharat

Ultrasonic Studies and Intermolecular/Interionic Interactions Of L-Isoleucine, L-Proline and L-Glutamine in Aqueous K2SO4, KNO3 and KCI Solutions

Author(s)	Riffat Basharat
Country	India
Abstract	Proteins, large molecules with high molecular weights are composed of varying amount of essentially the same about twenty amino acids well known for this purpose. Proteins play a vital role in nearly all the biological processes. Every protein has a unique three-dimensional structure that may reflect its envisaged function. Its structure is known to be stabilized by the presence of multiple weak interactions. Hydrophobic interactions provide the major contribution to stabilizing the globular form of most soluble proteins; hydrogen bonds and ionic interactions are optimized in the specific structure that is thermodynamically most stable. The thermodynamic stability of the native structure of protein has provided one of the great challenges in Biophysical Chemistry and Biophysics; and still currently remains the subject of extensive investigations (1-14). The knowledge of stability of proteins in aqueous and mixed aqueous solutions is essential for understanding their structures and functions. The stability of a globular protein in aqueous solutions can be determined by studying the disruption of its native structure, i.e., the process of denaturation. The denaturation of globular proteins in aqueous solutions is a fundamental biological process. During this process, the native folded conformation of protein is converted predominantly into an extended unfolded form and during this process various changes occur in protein hydration. Protein hydration that is the interaction of water with various functional groups of proteins is an important factor in determining the conformational stability of proteins (8-10). Thus, the thermodynamic studies of native and denatured states of proteins are necessary to understand the role of hydration in protein folding / unfolding processes (15-17). The structural details revealed by the high-resolution x-ray crystallography, neutron diffraction, spectroscopy and thermodynamic methods have contributed a great deal towards our understanding of protein functions (18). The amino acids, the alphabet of protein structure, can be arranged in an almost infinite number of sequences to make an almost infinite number of different proteins. Amino acids are characterized by the presence of a carboxyl group (-COOH) and an amino group (-NH2) attached to the same carbon at the end of the compound. Every amino acid except glycine can occur as either of the optically active stereoisomers, D or L; the more common isomer in nature is the L-form. When the carboxyl carbon atom of one amino acid covalently binds to the amino nitrogen atom of another amino acid with the release of water molecule, a peptide bond is formed. Asparagine was the first amino acid to be discovered in proteins in 1806.
Published In	Volume 4, Issue 1, January-June 2013
Published On	2013-06-28

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Ultrasonic Studies and Intermolecular/Interionic Interactions Of L-Isoleucine, L-Proline and L-Glutamine in Aqueous K2SO4, KNO3 and KCI Solutions

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