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Page 13
... activity of proteins. III. PROTEIN STRUCTURE Proteins are polymers
composed of 20 naturally occurring amino acids linked through peptide bonds.
Each protein has a unique sequence and distribution of amino acid residues
which is ...
... activity of proteins. III. PROTEIN STRUCTURE Proteins are polymers
composed of 20 naturally occurring amino acids linked through peptide bonds.
Each protein has a unique sequence and distribution of amino acid residues
which is ...
Page 14
In addition, the bulky side chains of the amino acid residues cause steric
hindrance to the rotation of other covalent single bonds in the backbone. This
further decreases the flexibility of the polypeptide chain. The secondary and
tertiary ...
In addition, the bulky side chains of the amino acid residues cause steric
hindrance to the rotation of other covalent single bonds in the backbone. This
further decreases the flexibility of the polypeptide chain. The secondary and
tertiary ...
Page 56
... number of amino acid residues in the protein), a0 is the limiting, close-packed
area per amino acid residue, Z is the lattice coordination number, k is the
Boltzman constant, T is the temperature, and 6 is the degree of surface coverage
which ...
... number of amino acid residues in the protein), a0 is the limiting, close-packed
area per amino acid residue, Z is the lattice coordination number, k is the
Boltzman constant, T is the temperature, and 6 is the degree of surface coverage
which ...
Page 414
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Page 442
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Contents
81 | |
Chapter 3 The Gelation of Proteins | 203 |
A Molecular Basis for Modeling Biomacromolecular Processes | 299 |
Chapter 5 Meat Mutagens | 387 |
Index | 451 |
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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