Advances in Food and Nutrition ResearchAdvances in Food and Nutrition Research |
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Page 2
... attributed to nonspecific variations in the amphipathicity of proteins because, within reasonable limits, most proteins exhibit similar distribution of hydrophobic and hydrophilic residues. This is evident 2 SRINIVASAN DAMODARAN.
... attributed to nonspecific variations in the amphipathicity of proteins because, within reasonable limits, most proteins exhibit similar distribution of hydrophobic and hydrophilic residues. This is evident 2 SRINIVASAN DAMODARAN.
Page 3
hibit similar distribution of hydrophobic and hydrophilic residues. This is evident from the average hydrophicity values of many proteins (Bigelow and Channon, 1976). It then follows that the differences in the surfaceactive properties ...
hibit similar distribution of hydrophobic and hydrophilic residues. This is evident from the average hydrophicity values of many proteins (Bigelow and Channon, 1976). It then follows that the differences in the surfaceactive properties ...
Page 13
... residues which is defined as the primary structure. Given an amino acid composition, it is theoretically possible to construct billions and billions of proteins of different size, amino acid sequence, and distribution pattern in the ...
... residues which is defined as the primary structure. Given an amino acid composition, it is theoretically possible to construct billions and billions of proteins of different size, amino acid sequence, and distribution pattern in the ...
Page 14
... residues, neither a-helix nor 3-sheet is formed. When the neighboring amino acid residues are hydrophilic, the hydrophobic residues, such as methionine, leucine, and isoleucine, induce formation of helix. When the local hydrophobicity ...
... residues, neither a-helix nor 3-sheet is formed. When the neighboring amino acid residues are hydrophilic, the hydrophobic residues, such as methionine, leucine, and isoleucine, induce formation of helix. When the local hydrophobicity ...
Page 15
... residues to be buried in the interior and for the hydrophilic residues to be at the surface. However, in most proteins, while almost all the hydrophilic residues are located at the surface, not all the hydrophobic residues are totally ...
... residues to be buried in the interior and for the hydrophilic residues to be at the surface. However, in most proteins, while almost all the hydrophilic residues are located at the surface, not all the hydrophobic residues are totally ...
Contents
81 | |
Chapter 3 The Gelation of Proteins | 203 |
A Molecular Basis for Modeling Biomacromolecular Processes | 299 |
Chapter 5 Meat Mutagens | 387 |
Index | 451 |
Common terms and phrases
8-lactoglobulin acid phosphatase adsorbed adsorption aggregation Agric air-water interface amino acid analysis aqueous beef behavior binding bovine bovine serum albumin calcium casein cell walls changes Chattoraj cheese coalescence Colloid Colloid Interface Sci conformation constant creaming cross-links decrease denaturation droplets effect elasticity electrostatic emulsifying emulsifying properties emulsion stability emulsions enzyme equation film flocculation foam food emulsions Food Sci formed free energy functional properties gelatin gelatin gels gelation globulin Graham and Phillips heat-induced heating Hermansson increase interactions interfacial tension ionic strength k-casein kinetics Kinsella liquid lysozyme MacRitchie meat microemulsion modulus molecular molecule monolayers mutagen formation mutagenic mutagenic activity myosin NaCl nonlinear regression oil/water interface ovalbumin phase polymer protein concentration protein gels residues rheological salt serum albumin solubility solution solvent soy protein structure studies succinylated surface pressure surfactants Table temperature thermodynamic tion values viscosity whey protein