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PROTEINS

  • Jef Marc Valencia

    • 問題数 26 • 4/10/2024

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  • 1

    Chief nitrogenous macromolecules of cellular structure and organization

    PROTEIN

  • 2

    Proteins Composes _ of the cell’s dry weight

    50-70%

  • 3

    are linked via peptide bond (formed upon removal of a water molecule)

    AMINO ACID

  • 4

    (positive or negative charges); either acidic or basic

    AMPHOTERIC

  • 5

    Protein Provide _ of the total daily body energy requirement

    12-20%

  • 6

    Protein responsible for transport of metabolic substances

    TRANSFERRIN

  • 7

    Protein responsible for Maintenance of osmotic pressure

    ALBUMIN

  • 8

    These are proteins Biocatalysts

    LIPASE

  • 9

    Protein structure Which the polypeptide chain is linear and also Determines the overall shape of the protein

    PRIMARY STRUCTURE

  • 10

    Refers to the identity and specificity of Amino Acid

    AMINO ACID SEQUENCE

  • 11

    Protein Structure which Conformation of the segments of polypeptide chain is . Maintained by hydrogen bond

    SECONDARY STRUCTURE

  • 12

    Protein Structure which Important for the strength and flexibility of proteins and also rises from the interaction among the different segments of a polypeptide chain

    SECONDARY STRUCTURE

  • 13

    3 SECONDARY STRUCTURES - Chain forms a regular helix; coil resembling a spring - In fully extended structures; flat, corrugated structure - No apparent pattern

    ALPHA HELIX, BETA PLEATED SHEET, RANDOM COIL

  • 14

    Intramolecular folding pattern of the protein maintained by covalent disulfide bond Responsible for many of the physical and chemical properties of proteins

    TERTIARY STRUCTURE

  • 15

    Association of several polypeptide chains into larger “oligomeric” aggregate unit maintained by non-covalent bond (hydrogen bond)

    QUATERNARY STRUCTURE

  • 16

    QUATERNARY STRUCTURE Example:

    HEMOGLOBIN, LACTATE DEHYDROGENASE, CREATINE PHOSPHOKINASE

  • 17

    When the secondary, tertiary or quaternary structure of protein is disturbed, the protein may

    LOSS FUNCTION

  • 18

    REFERS TO THE LOSS OF FUNCTION OF PROTEIN

    DENATURATION

  • 19

    Factors of Denaturation

    HEAT, HYDROLYSIS, ENZYMATIC REACTION, UV LIGHT

  • 20

    Contain peptide chains that on hydrolysis yield only AA

    SIMPLE PROTEIN

  • 21

    Simple Protein Class - more elongated and asymmetrical and have a higher viscosity - relatively symmetrical with compactly folded and coiled polypeptide chains

    FIBROUS, GLOBULAR

  • 22

    Globular Sample

    HEMOGLOBIN, PLASMA PROTEIN, ENZYME, PEPTIDE HORMONE

  • 23

    Fibrous sample

    FIBRINOGEN, TROPONIN, COLLAGEN

  • 24

    Protein (apoprotein) + nonprotein (prosthetic group)

    CONJUGATED PROTEIN

  • 25

    PROSTHETIC GROUPS OF CONJUGATED PROTEIN

    LIPOPROTEIN, CARBOHYDRATE, METAL

  • 26

    METABOLISM OF CONJUGATED PROTEIN -Stomach -Small Intestine - Liver and Reticuloendothelial -Liver kidneys and Intestines - Waste

    DIETARY INTAKE, ABSORPTION, PRODUCTION, STORAGE, DESTRUCTION

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