Protein hydrophobic-hydrophilic

The optimum water content of most cells is around 80%. Liquid water is absolutely necessary for the stability of the lipid membrane and the hydrophobic regions in proteins. The hydrophilic fractions of the nucleic acids and the proteins require liquid water for maintaining their three-dimensional structures and thus their functionality. 

The ProteinChip System from Ciphergen Biosystems uses patented SELDI (Surface-Enhanced Laser Desorption/Ionization) ProteinChip technology to rapidly perform the separation, detection, and analysis of proteins at the femtomole level directly from biological samples. ProteinChip Systems use ProteinChip Arrays which contain chemically (cationic, anionic, hydrophobic, hydrophilic, etc.) or biochemically (antibody, receptor, DNA, etc.) treated surfaces for specific interaction with proteins of interest. Selected washes create on-chip, high-resolution protein maps. This protein mass profile, or reten-tate map of the proteins bound to each of the ProteinChip Array surfaces, is quantitatively detected in minutes by the ProteinChip Reader. 

Clay minerals or phyllosilicates are lamellar natural and synthetic materials with high surface area, cation exchange and swelling properties, exfoliation ability, variable surface charge density and hydrophobic/hydrophilic character [85], They are good host structures for intercalation or adsorption of organic molecules and macromolecules, particularly proteins. On the basis of the natural adsorption of proteins by clay minerals and various clay complexes that occurs in soils, many authors have investigated the use of clay and clay-derived materials as matrices for the immobilization of enzymes, either for environmental chemistry purpose or in the chemical and material industries. 

Common bean procyanidins are capable of both hydrophilic and hydrophobic interaction with protein. Hydrophilic interactions are favored with a hydrophilic glycoprotein like common bean globulin Gl, while hydrophobic interactions are favored after protein denaturation, when protein hydrophobic groups are exposed to the solvent. 

The chelate effect in proteins is also important, since the three-dimensional (3-D) structure of the protein can impose particular coordination geometry on the metal ion. This determines the ligands available for coordination, their stereochemistry and the local environment, through local hydrophobicity/hydrophilicity, hydrogen bonding by nearby residues with bound and non-bound residues in the metal ion s coordination sphere, etc. A good example is illustrated by the Zn2+-binding site of Cu/Zn superoxide dismutase, which has an affinity for Zn2+, such that the non-metallated protein can extract Zn2+ from solution into the site and can displace Cu2+ from the Zn2+ site when the di-Cu2+ protein is treated with excess Zn2+. 

The preparation of monoliths with polyNIPAAm chains grafted to the internal pore surface was discussed previously. The extended solvated polyNIPAAm-chains that are present below the lower critical solution temperature of this particular polymer are more hydrophilic, while the collapsed chains that prevail above the lower critical solution temperature are more hydrophobic. In contrast to isothermal separations in which the surface polarity remains constant throughout the run [ 136], HIC separation of proteins can be achieved at constant salt concentrations (isocratically) while utilizing the hydrophobic-hydrophilic... 

A series of carboxyl containing bioerodible polymeric materials, characterized by modulated functionality and hydrophobic/hydrophilic balance, was prepared both on a lab-scale and in the pilot plant. Procedures were setup as amenable for scaled-up productions. Those materials displayed a high versatility to combine with proteins in different proportion and to provide hybrid bioerodible matrices without any adverse effect on protein structure and activity. 

In a related approach, arrays with different types of surface chemistries such as hydrophobic, hydrophilic, anionic, and affinity are used to absorb certain protein groups from biological or patient samples. The chip-absorbed proteins are then directly detected by surface-enhanced laser desorption/ionization time-of-flight MS (SELDl-TOF MS) (Issaq et al. 2002). The resulting protein masses can be used in pattern analysis and thereby provide a useful diagnostic tool. 

Flavonoids and other polyphenols can interact with lipids and proteins. The interactions with proteins could be both unspecific or specific, meanwhile the interactions with lipids seems to be rather unspecific, based essentially on physical adsorption. This physical adsorption would mostly depend on the hydrophobic/hydrophilic characteristics of the flavonoid molecule, the number of hydroxyl substituents, and the polymerization degree [Erlejman et al., 2004 Verstraeten et al., 2005, 2003, 2004]. 

Protein chains generally contain hydrophobic, hydrophilic and/or charged amino acid residues, which can be regarded as amphiphilic copolymers in a broad definition. The coordinate and cooperative interactions, such as... 

The nature of the side chains of amino acids determines the hydrophobic (water hating) and hydrophilic (water loving) nature of the amino acid. Amino acids with hydrophobic side chains will be less soluble in water than those with hydrophilic side chains. The hydrophobic/hydrophilic nature of the side chains of amino acids has a considerable influence on the conformation adopted by a peptide or protein in aqueous solution. Furthermore, the hydrophobic/hydrophilic balance of the groups in a molecule will have a considerable effect on the ease of its passage through membranes (Appendix 5). 

The conclusion that was drawn for the stabilization of protein structure in aqueous solvent systems was as follows the type of protein, the hydrophilic or hydrophobic character and thus the subsequent interaction of the protein with, (i) water and, (ii) the additives themselves, all play an important part of the stabilization process. 

SURFACE PROPERTIES AFFECTING PROTEIN ADSORPTION HYDROPHILICITY/HYDROPHOBICITY TOPOGRAPHY ENERGY CHARGE ETC. 

Table I shows that the foaming properties of whole casein improved by slight phosphorylation. The lowest phosphorylated form of casein (4 mol P/mol protein) showed higher foam hydration and stability than the native whole casein. However, the highly phosphorylated whole casein (11 mol P/mol protein) showed poor foaming properties. The foam hydration of as-casein deteriorated while that of K-casein improved by phosphorylation. This discrepancy seemed to be caused by a different initial hydrophobic/ hydrophilic balance of the proteins in their native states. However, foam stabilities of all casein fractions were reduced by phosphorylation, with K-casein being only slightly affected.

Other IRRAS applications to peptides and proteins. In addition to the pulmonary surfactant system, a variety of other applications employing IRRAS to study peptide and protein conformation and orientation have appeared. The secondary structure conversion of the amyloid (prion)-protein in the normal form into the abnormal form is the main cause of several human and animal diseases, such as Alzheimer s disease [68]. The secondary structure of the first 40 residues of the amyloid protein was detected by circular dichroism (CD) in aqueous solution and with IRRAS at the interface. A stable /1-sheet-enriched state of the amyloid is formed at the air-water interface, in contrast to the initial bulk solution containing high a-helix/random coil and low /l-sheet parts. The change in the pH going from bulk (alkaline pH) to the interface (neutral or slightly acidic pH) can have effects on the conformation at the interface. Another alternative might be the intrinsic hydrophobicity of the air-water interface, which is a hydrophobic-hydrophilic system with air as the hydrophobic part. 

ATP extraction has been used for the separation and large-scale purification of enzymes.45 47 Proteins and nucleic acids partition between the two phases differently due to differences in their surface charges and hydrophobic-hydrophilic domains. Proteins generally prefer the aqueous phase rich in... 

Hydrophilic nanoparticle carriers have important potential applications for the administration of therapeutic molecules [28,53]. Most of the recently developed hydrophobic-hydrophilic carriers require the use of organic solvents for their preparation and have a limited protein-loading capacity [54,55]. Calvo et al. [56] reported a new approach for the preparation of nanoparticles, made solely of hydrophilic polymer, to address these limitations. The preparation technique, based on an ionic gelation process, is extremely mild and involves the mixing of two aqueous phases at room temperature. 

Schneider and others (Schneider et al., 1993) applied the perception approach to identifying cleavage sites in protein sequences. Again, a matrix approach was used, with 12 rows representing a sequence of 12 amino acid residues (one row per residue) and four columns representing physico-chemical features of each residue hydrophobicity, hydrophilicity, polarity and volume. The trained perceptron predicted cleavage sites correctly in 100% of test cases. 

It is very conceivable that series of protein derivatives with graded differences in functional properties (thermal stability, hydrophobicity, hydrophilicity, molecular dimensions, etc.) will become available in the future. Such functional derivatives should facilitate the exploitation of the wide range of novel proteins in the world. 

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