protein (undone) Flashcards

1
Q

what is the elemental composition of protein

A

carbon (C), hydrogen (H), oxygen (O), and nitrogen (N) and contain small amounts of sulfur (S) , iron (Fe) and phosphorus (P)

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2
Q

what is the chemical structure of protein

A

proteins are large molecules composed of amino acids. amino acids are joined together by peptide links to form long polypeptide chains that make up proteins

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3
Q

what is the basic structure of an amino acid

A

-an amino group (NH2) (basic)
-a carboxyl group (COOH) (acidic)
-a central carbon (C)
-a single hydrogen (H)
-a variable group (R): changes with each amino acid

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4
Q

what are essential amino acids

A

cannot be manufactured by the body, therefore must be obtained from food

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5
Q

give examples of essential amino acids

A

-valine
-lysine
-leucine
-isoleucine

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6
Q

what are non-essential amino acids

A

can be manufactured by the body, therefore don’t need to be obtained from food

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7
Q

give examples of non-essential amino acids

A

-serine
-glycine
-glutamic acid
-alanine

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8
Q

how are peptide links formed

A

are formed when two amino acids join together. this results in the loss of a water molecule and is called a condensation reaction

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9
Q

what are the stages in formation of peptide links

A
  1. the COOH (acidic) group of one amino acids reacts with the NH2 (basic) group of another
  2. the COOH (acidic) group loses an OH group. the NH2 (basic) group loses a hydrogen (H) atom 3. the result is a CO-NH bond. this new molecule is called dipeptide . when more than 20 amino acids join together, a polypeptide is formed. when more than 50 amino acids join together, a protein is formed. each protein consists of one or more polypeptide
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10
Q

what is the reverse of the condensation reaction called

A

hydrolysis

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11
Q

what is a primary structure

A

is the order or sequence of amino acids in protein chains, e.g. insulin contains 51 amino acids

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12
Q

what is a secondary structure

A

involves the folding of the primary structure into definite shapes

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13
Q

what are the main two types of cross-links

A

disulfide bonds and hydrogen bonds

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14
Q

how do disulfide bonds occur

A

occur when two sulphurs from two amino acids from either a single polypeptide chain link together

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15
Q

how do hydrogen bonds form

A

occurs when a hydrogen (N-H) from one amino acid group and an oxygen (C=0) from another amino acid group are joined together from either one or two Polypeptide Chains.

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16
Q

what is a tertiary structure

A

involves the folding of the secondary structure of proteins into three dimensional shapes. form definite shapes such as fibrous and globular

17
Q

how are fibrous shapes arranged

A

polypeptide chains are arranged in straight, spiral or zigzag shapes

18
Q

what are the properties of fibrous shapes

A

-insoluble in water
-not easily denatured

19
Q

give examples of fibrous shapes

A

-gluten (wheat)
-elastin and collagen

20
Q

how are globular shapes arranged

A

polypeptide chains are arranged in a globular shape

21
Q

what are the properties of globular shapes

A

-soluble in water
-easily denatured

22
Q

give examples of globular shapes

A

-ovalbumin (egg whites)
-lactalbumin (milk)

23
Q

what is high biological value proteins

A

contain all the essential amino acids

24
Q

give sources of HBV proteins

A

egg, fish, milk, meat, cheese

25
Q

what is low biological value proteins

A

lack one or more of the essential amino acids

26
Q

give sources of LBV proteins

A

rice, wheat, maize, meat bones

27
Q

what are the properties of protein

A

denaturation, elasticity, maillard reactionm solubility, gel