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Organ Chem > Chapter 18- Amino acids and proteins > Flashcards

Chapter 18- Amino acids and proteins Flashcards

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1
Q

Secondary structure

A

regular folding patterns seen in localized regions of polypeptide backbone

a and B helix

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2
Q

Tertiary structure

A

Overall shape of protein molecule produced by overall bedding and folding of a protein chain

3

Non covalent interactions and disulfide covalent bonds

A helix and B helix, loops connect

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3
Q

Quaternary structure

A

Overall structure of proteins composed of more than one polypeptide

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4
Q

Enzymes

A

Catalyze biochemical reactions

Ex. Amylase begins digestion of carbohydrates by hydrolysis

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5
Q

Hormones

A

Regulate body functions by carrying messages to receptors

Ex. Insulin facilitates use of glucose for energy generation

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6
Q

Storage proteins

A

Make essential substances available when needed

Ex. Myoglobin stores oxygen in muscles

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7
Q

Transport proteins

A

Carry substances through body fluids

Ex. Serum albumin carries fatty acids in blood
Fatty acids can not easily go through blood because non polar

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8
Q

Structural proteins

A

Provide mechanical shape and support

Example. Collagen provides structure to tendons and cartilage

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9
Q

Protective proteins

A

Defend body against foreign matter

Ex. Immunoglobulin AIDS in destruction of invading bacteria

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10
Q

Contractile proteins

A

Do mechanical work

Ex. Myosin and actin govern muscle movement

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11
Q

Zwitterion

A

Neutral ion with one positive charge and one negative charge

Very soluble

High melting point

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12
Q

Isoelectric point

A

pH at which sample of an amino acid has equal numbers of + and - charges

Net charge= 0

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13
Q

Enantiomers /optical isomers

A

Two mirror -image forms of chiral molecule like alanine

Type of stereoisomers have same formula and atoms with diff connections

Only L in proteins

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14
Q

Primary structure

A

Order

Sequence of amino acids in protein chain connected by peptide bonds

along backbone of protein chain is alternating peptide bonds and a-carbon atoms

DETERMINES PROTEIN SHAPE

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15
Q

Globular protein

A

Water soluble chain is folded in a compact shape with hydrophilic groups

Many are enzymes

Overall shape is tertiary

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16
Q

Fibrous proteins

A

INSOLUBLE

Keratin

Collagen

Elastin

Myosin

Fibrin

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17
Q

Keratin

A

Found in skin, wool, feather, hooves, fingernails

Fibrous

18
Q

Collagens

A

Animal hide, tendons, bone, eye cornea, other CT

Fibrous

19
Q

Elastins

A

Blood vessels, ligaments

Fibrous

20
Q

Myosins

A

Muscle tissue

Fibrous

21
Q

Fibrin

A

Found in blood clots

Fibrous

22
Q

Globular proteins

A

SOLUBLE , hydrophilic groups on outside

insulin

Ribonuclease

Immuglobulins

Hemoglobin

Albumins

23
Q

Insulin

A

Control glucose metabolism

Globular

24
Q

Ribonuclease

A

Enzyme that catalyzes RNA hydrolysis

Globular

25
Q

Immunoglobulins

A

Involved in immune response

Globular

26
Q

Hemoglobin

A

Oxygen transport

Globular

27
Q

Albumins

A

Perform many transport function in blood; protein in egg white

Globular

28
Q

Native protein

A

Shape in which it functions in living systems

29
Q

Simple protein

A

Protein composed of only amino acid residues

30
Q

Conjugated protein

A

Aided by its function by non-amino acid unit

Ex. Myoglobin

31
Q

Edmar degradation

A

Cleaves N-terminal amino acid of polypeptide chain (left)

32
Q

Chemical properties of proteins

A

Heat

Mechanical agitation

Detergents

Organic compounds

pH change

Inorganic salts

33
Q

Denaturation

A

Loss of secondary, tertiary, or quaternary protein structure leaves primary intact

Irreversible

34
Q

Functions of proteins

A

Transport necessary chemicals

Support organs or tissues

Protect against foreign substances

Storage of energy

35
Q

Saponification reaction used to form soaps can be best describe as

A

Base hydrolysis

36
Q

Soaps

A

Salts of carboxylic acids

Alkali metal salts of long chain carboxylic acids

37
Q

Basic structure of cell membrane consists of

A

Phospholipid bilayers studded with proteins

38
Q

Lecithin commonly used as

A

Emulsifying agent

39
Q

Heat affects

A

Hydrogen bonds and hydrophobic interactions

40
Q

Acids and bases affect

A

Hydrogen bonds and salt bridges

41
Q

Agitation affects

A

Hydrogen bonds and hydrophobic interactions

42
Q

Organic compounds are affected by

A

Hydrophobic interactions

Organ Chem (5 decks)

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