Foodchem Lecture 11 Pics

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    Beta sheets regions can form when alpha helices fold in upon themselves in order to reduce their molecular free energy state
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    Globular protein with random, helix and b-sheet forms
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    • Additional hydrogen bonding can take place any time a hydrogen and electronegative oxygen/nitrogen are in proximity
    • Can form electrostatic bonds or can be solvated
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    Additional hydrogen bonding can take place any time a hydrogen and electronegative oxygen or nitrogen are in proximity
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    Net result of all the different kinds of bonds result in a protein macromolecule will try to find an equilibrium structure dictated by its environment and tends to be structurally locked into a specific conformation by a range of forces
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    • Tetramer
    • Four tertiary globular proteins associating
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    • Lipoprotein
    • Proteins complexed with lipids, generally triglycerides and phospholipids
    • Abundant in nature and have good emulsifying properties
    • Examples: Egg yolk, and some milk proteins
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    • Glycoprotein
    • Proteins complexed with carbohydrate
    • Can range from simple sugars to heterosaccharides to polysaccharides
    • The carbohydrate is generally attached to the OH group of serine or threonine by an O-glycosidic bond or the amide group of asparagine, by an N-glycosidic linkage
    • Examples: Ovomucoid in eggs and soybean glycoproteins
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    • Metalloprotein
    • Complex proteins which are complexed with a metal ion which is generally loosely chelated
    • Examples: Fe++ in myoglobin and hemoglobin where Fe++ is chelated by a porphyrin ring structure
    • Numerous enzymes have metal ions as prosthetic groups
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    • Unfolding of the protein as it is denatured
    • Tertiary structure unfolds, secondary structure unravels
    • Leaves the peptide bonds more accessible to proteolytic enzymes
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    • Denaturation results in reduction in solubility
    • Hydrophobic domains become exposed
    • Exposed hydrophobic domains bind together
    • They aggregate together
    • Precipitate out of solution
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    • TD = Temperature of denaturation
    • Shows how with increasing temperature, degree of order is decreased
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    Shows the effect of pH on protein denaturation
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    • Urea
    • Can hydrogen bond competitively with the peptide linkage induced hydrogen bonds and disrupt both tertiary and secondary structure hydrogen bonds
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    Urea can hydrogen bond competitively with the peptide linkage induced hydrogen bonds and disrupt both tertiary and secondary structure hydrogen bonds
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    Water hydrogen bonding is integral to, and helps stabilize the structure of proteins, especially around charged groups
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    • Detergents have both hydrophilic and hydrophobic groups
    • They are able to bridge the hydrophobic and hydrophilic regions of the protein and result in the opening of the internal structure of a protein
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    • Bubble within a foam
    • Air is trapped within a protein/water matrix (bubble)
    • Each bubble has thin membrane (interface) which separates the two
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    Foam can cause denaturation at the interface between the hydrophobic and hydrophilic groups
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    The easy way to tenderize meat, by using papain, an enzyme to speed it up
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    The hard way to tenderize meat, using this tool and physical force
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Foodchem Lecture 11 Pics
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Foodchem Lecture 11 Pics
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