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Macronutrients > Exam #4 > Flashcards

Exam #4 Flashcards

1
Q

Essential AA

A

9 or 10 are not synthesized (made) in body

body can’t synthesize the side R chain

Arg*, His, Ile, Leu, Met, Phe, Thr, Trp, Val

Must be obtained from diet:

Animal products contain all essential. (dairy)

Vegetables and grains are missing 1 or more AA (not complete PTNs) but they can compliment each other like rice and beans

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2
Q

Protein Functions

A

SAM THE AaF

  1. Structure (tendons, cartilage, hair, nails)
  2. Antibodies (immune response)
  3. Muscles (contractile)
  4. Transport (hemoglobin)
  5. Hormonal (insulin and growth hormone)
  6. Enzyme (catalyzes cell rxns)
  7. Amino acids (acid/base-buffer)
  8. Fluid balance (osmosis)
  9. Roles in: RASS

Receptors

Adhesion (Collagen)

Signaling (neurotransmitters)

Storage

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3
Q

Structure

A
  1. contractile proteins (actin and myosin) in cardiac, skeletal (voluntary), and smooth muscles (involuntary)

Calcium induced, troponin, tropomysosin

  1. fibrous proteins (collagen, elastin, keratin)

collagen is rich in glycine and proline

helical arrangement, are considered glycoproteins

  1. globular proteins (myoglobin, calmondulin, and many enzymes) spherical shape
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4
Q

Antibodies

A

immunoproteins - provide body protection by a group of proteins (immunoglobulins (Ig) or antibodies (Ab))

there are 5 classes (IgG, IgA, IgM, IgE, IgD)

Y shaped proteins produced by plasma cells from B-lymphocytes (white bld cells)

makes antigens (bacteria, viruses) inactive

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5
Q

Muscles

A

contractile proteins (actin and myosin) in cardiac, skeletal (voluntary), and smooth muscles (involuntary)

Calcium induced, troponin, tropomysosin

smooth - blood vessels, lungs, uterus, GI tract (involuntary by calcium induced phosphorylations of myosin)

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6
Q

Transporters

A

Transport proteins are proteins that combine with other substances (vits, and minerals, and other nutrients) to provide means of carrying those substances in the blood, or into cells, or out of cells, or within cells.

  1. Albumin (transports variety of nutrients like Ca, Zn, Vit B6 in bld)
  2. Transthyretin (prealbumin) - transports vit A in bld with retinol bining protein, thyroid hormone in bld
  3. Transferrin (Iron and Zinc transport in bld)
  4. Ceruloplasmin (Copper transport in bld)
  5. Lipoproteins (transports lipids in bld)
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7
Q

Hormones

A

Hormones that are proteins act as chemical messengers.

endocrine -> blood -> target tissues -> PTN receptors

tyrosine is used to make thyroid hormone

trypotophan is used to make melatonin

insulin is made up of one or more polypeptide chains linked by disulfide bridge

single polypeptide chain include glucagon, parathyroid hormone, and calcitonin

ADH, and somatotropin (growth hormone)

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8
Q

Enzymes

A

are protein molecules that act as catalysts, they change the rate rxns occur in the body

found both intracellularly and extracellularly

  1. Hydrolases (cleaves)
  2. Isomerases (transfer atoms within a molecule)
  3. Ligases (synthases - join compounds)
  4. Oxidoreductases (transfer electrons)
  5. Transferases (move functional groups)

Human physiological processes require enzymes to promote chemical changes: digestion, energy production, blood coagulation, neuromuscular tissue excitation and contraction

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9
Q

Amino Acids

A

serve as buffers in the body to regulate acid base balance

hemoglobin protein function buffer for red blood cells

amino acids act as acids or bases in aqueous solutions in the body by releasing or accepting hydrogen ions

H+ + protein <-> Hprotein

pH high (basic) = AA donates hydrogen

pH low (acidic) = AA accepts hydrogen

Zwitterion = AA with no amino or carboxyl groups in its side chain to generate additional charge to the molecule ( no net electrical charge = side chains uncharged the + & - side chains cancel each other out)

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10
Q

Fluid Balance

A

presence of protein in blood and in cells helps to maintain fluid balance (helps attract water and maintain osmostic pressure)

DEC in albumin = DEC in plasma osmostic pressure

edema = PTN concentrations in bld are LESS fluid leaks out of bld and into interstitial spaces

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11
Q

Storage

A

minerals (Cu, Fe, and Zn) are stored in the body tissues bound to proteins

proteins are called metalloproteins

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12
Q

Amide (Peptide) Bond

A

formed from the -COOH of an amino acid and the -NH2 of the next amino acid

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13
Q

Peptide

A

dipeptides, tripeptides, tetrapeptides

amino acids linked by peptide bond always one free amine end and one free carboxyl end

H2N-Gly-Lys-Phe-Arg-Ser-COOH

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14
Q

Primary Structure

A

sequence of amino acids in a polypeptide chain

the particular sequence of amino acids that is the backbone of a peptide chain or protein

level of organization determined by the sequence of amino acids specified by the messenger RNA

amino acids linked by peptide bonds

covalent bonds

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15
Q

Secondary Structure

A

Hydrogen bonding (weak electrical attractions)

1.) Alpha Helix (most popular)

3-D arrangement of amino acids in a corkscrew shape with H bonds between amino acids

H bonds between the H of -NH and the -O of the C=O of the 4th amino acid along the chain

R-groups extend outward

telephone cord

2.) Beta Pleated Sheet

polypeptide chains are arranged side by side by H bonds

hydrogen bonds form between chains

R-groups extend above and below

typical of fibrous proteins (silk)

3.) Triple Helix (stronger)

three peptide chains woven like a rope

H bonding between -OH groups gives a strong structure

sources collagen, connective tissue, skin, tendons, and cartilage

glycine, proline, hydroxyproline, and hydroxylysine

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16
Q

Tertiary Structure

A

the way a protein folds in a 3-dimensional space

structure results from interactions among amino acid side chains these interactions can produce linear, globular or spherical structure

globular protein (spherical shape) - insulin, hemoglobin, enzymes, antibodies

fibrous proteins (long, thin fibers) - hair, wool, skin, nails

Interactions:

  1. ) hydrophobic - clustering of amino acids toward the center of the protein (leucine and valine) -CH3—H3C
  2. ) ionic - electrostatic attraction of oppositely charged amino acid side chains (lysine +1 and glutamate -1) (lysine +1 and aspartic acid -1) -COO-—H+3N-
  3. ) disulfide - strong covalent bonding involving electron sharing between cysteine side chains where the -SH groups are oxidized to form disulfide bridges -S-S-
  4. ) hydrogen bonding - among side chains usually occur along the chain (serine and threonine) C=O—HO-
17
Q

Quaternary Structure

A

proteins with two or more polypeptide chains held together by hydrogen bonds

important in intracellular regulation bc the subunits can assume different spatial orientations relative to each other and in doing so change the properties

Examples:

Hemoglobin (4 chains) - each chain has a heme group to bind oxygen. carries oxygen in blood

Insulin (2 chains) - regulatory enzymes similarly undergo conformational changes on interaction with substrate molecules

18
Q

Protein Hydrolysis

A

break down of peptide bonds

requires an acid or a base with heat and water (body can’t use heat)

results in smaller peptides and amino acids

similar to digestion of proteins using enzymes

In cell to provide amino acids to sythesize other proteins and tissues

complete hydrolysis = free amino acids

Ala-Ser-Val -> Alanine, Serine, and Valine

19
Q

Denaturation

A

disruption of secondary, tertiary, and quaternary protein structure (uncoil so enzyme can work on linkage and make smaller) by:

  1. ) Heat/organics - break apart H bonds and disrupt hydrophobic attractions
  2. ) Acids/bases - break H bonds between polar R groups and ionic bonds
  3. ) Heavy metal ions - react with S-S bonds to form solids
  4. ) Agitation - stretches chains until bonds break

Examples

hard boiled egg, wiping skin with alcohol swab for injection, cooking food to destroy E. coli, heat used to cauterize blood vessels, autoclave sterilizes instruments, milk is heated to make yogurt, tannic acid used to form a scab on a burn.

20
Q

PTN RDA

A

0.8 g/kg of body weight (>19y old)

exogenous RDA 56g/46g

21
Q

PTN Sources

A

Serve as sources of essential amino acids and are the primary source of the additional nitrogen needed to synthesize the nonessential amino acids and nitrogen-containing compounds.

Animal

meat, poultry, fish, and dairy

Plant

grains, legumes, and vegetables

22
Q

Endogenous PTN

A

derived from digestive secretions of the salivary glands, stomach, intestine, biliary tract, and pancreas. they are digested and provide amino acis available for absorption

  1. ) desquamated mucosal cells, 50g/day
  2. ) digestive enzymes and glycoproteins, 17g/day

don’t store PTNs in body no AAs they are either by diet or broken down from PTN in tissues (muscles, structures, and antibodies)

Macronutrients (4 decks)

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