Chapter 2.4 proteins Flashcards

1
Q

Peptide

A

two or more amino acids joined by peptide bonds

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2
Q

How are peptide bonds formed?
Which functional groups connect peptides together?

A

Dehydration synthesis

Amino group of one amino acid to carboxyl group of the next

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3
Q

3 Characteristics of amino acids

A

-Central carbon atom with an amino group, carboxyl group, hydrogen, and R group
-All amino acids identical except for radical group
-Often amphipathic

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4
Q

Oligopeptide

A

Chains of amino acids fewer than 10 or 15

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5
Q

Polypeptides

A

10 or 15 or more chains of amino acids

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6
Q

How many chains Of amino acids does a polypeptide need to be a protein?

A

50 or more

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7
Q

Primary structure Of a protein And it’s associated bond

A

Proteins sequence of amino acids; peptide bonds

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8
Q

Secondary structures and Associated bond

A

Alpha helix or beta sheets held together by hydrogen bonds

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9
Q

Tertiary structure and associated bonds

A

further bending and folding of proteins into various globular and fibrous shapes.
Van der waals forces and hydrophilic/phobic interactions

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10
Q

Globular proteins

A

Look like a watered ball of yarn;

-Embedded in cell membranes
-proteins that must move freely like Enzymes and antibodies

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11
Q

Fibrous proteins

A

Slender filaments such as myosin, keratin, and collagen; provide strength to skin hair and tendons

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12
Q

Disulfide bridges

A

-In amino acid cysteine
-Formed by covalent bonds
-Holds tertiary structures (separate polypeptide chains) together.

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13
Q

Quaternary structure and associated bonds

A

-two or more polypeptide chains
-ionic bonds and hydrophilic/hydrophobic interactions
-non-amino moiety: prosthetic group
Ex: hemoglobin

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14
Q

Denaturation

A

Conformation change that breaks hydrogen bonds; lose structure=lose function

Ex: cook egg white 

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15
Q

Conjugated protein has what bonded to it and how bonded?

A

Has a prosthetic group; covalently bonded

Ex: glycoproteins: the carbohydrate moiety is a prosthetic group

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16
Q

6 Protein functions:

A
  1. Structure
  2. Communication
    3. Membrane transport
  3. Catalysis
  4. Movement/ adhesion
  5.  Recognition
17
Q

Examples of protein structures

A

Keratin for hair, skin, nails

Collagen for deep layers of skin, bones, cartilage, teeth

18
Q

Protein recognition and protection

A

-Antibodies and other proteins attack and Neutralize invading organisms. 
-also clotting proteins

19
Q

What are enzymes

A

Proteins that function as biological catalysts

20
Q

Substrate

A

The substance the enzyme acts upon

(Adds the suffix -ase
Ex: amylase amyl=starch)

21
Q

Activation energy

A

The energy needed to get the reaction started; Enzymes lower activation energy needed

Ex: Burning paper: the match supplies activation energy

22
Q

Conformation change is important to what?

A

enzyme function, muscle contraction, and the opening and closing of pores in cell membranes

23
Q

Enzymes lower the ______ of a reaction 

A

Activation energy

24
Q

Enzyme structure and action order of events:

A
  1. substrate approach activation site
  2. Enzyme – substrate complex (Enzyme – substrate specificity)
  3.  Bond broken or formed; enzyme releases product(s)
25
Q

Cofactors of enzymes

A

non-protein INORGANIC partner

26
Q

Coenzymes

A

Organic cofactors

Acts as a shuttle that picks up electrons from one metabolic pathway and delivers them to another

27
Q

Metabolic pathway

A

A chain of reactions with each step usually catalyzed by a different enzyme

28
Q

When a macromolecule is conjugated, it is

A

Covalently bonded to another macromolecule

29
Q

Conformation

A

3 dimensional shape

30
Q

Function of a protein is derived from its what?

A

Structure