L4 Flashcards

1
Q

List the 4 levels of organization of protein structure?

A

primary structure :
secondary structure :
tertiary structure:
quaternary structure:

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2
Q

describe the primary structure of proteins .

A

the primary structure of protein organization refers to the number and sequence of amino acids joined by peptide bonds.

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3
Q

how is the sequence of amino acids(primary structure) determined ?

A

the sequence is determined by genetics and it is coded in DNA

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4
Q

What determines the final 3D structure and function of a protein ?

A

sequence of amino acids

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5
Q

describe the secondary structure of proteins .

A

it refers to the conformation of the polypeptide chain by twisting or folding

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6
Q

what are the 2 major types of secondary structure and what makes them different?

A

the two major types are alpha-helix and beta sheet .

alpha- helix is a right handed helix structure that is stabilized by hydrogen bonds.Alpha-helix structure is formed by small and uncharged amino acids. bulky and charged amino acids prevent helix formation

beta sheet or beta pleated structure is composed of 2 or more segments of sully extended peptide chain

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7
Q

describe the tertiary structure of proteins .

A

it refers to the spatial relationship of distant amino acids in the same polypeptide chain

it is the 3-Dimentional arrangement of proteins

it is a compact structure with hydrophobic side chains held interior while the hydrophobic groups are on the surface of the molecule

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8
Q

what are the bonds that stabilize the tertiary structure?

A

disulfide bond (covalent)

electrostatic attractions

hydrogen bond

hydrophobic interactions

van der Waals interactions

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9
Q

describe the quaternary structure of proteins .

A

it refers to the spatial relationship between individual polypeptide chains in a multimeric protein .

the monomeric subunits are held by noncovalent bonds (hydrogen bandstand hydrophobic iterations and ionic bonds)

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10
Q

what are domains ?

A

domains are secondary-tertiary structures found in proteins associated with specific functions .

ex: antigen binding domain of the immunoglobulin

catalytic domain of an enzyme

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11
Q

what is the final structure of any protein made from one chain?

A

tertiary structure.

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12
Q

what happens to a protein after it is synthesized?

A

each protein undergoes folding to form a unique structure which is essential for its function after it is synthesized.

for example , the active site of the enzyme chymotrypsin is formed by polypeptide chain folding.

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13
Q

what other proteins help in the process of folding?

A

enzymes and chaperones .

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14
Q

what are chaperones ?

A

special proteins that help other proteins fold.

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15
Q

what is the denaturation of proteins ?

A

it is the change in native conformation of a protein .it occurs when there is a breakdown of quaternary , tertiary and secondary structure but the primary structure stays intact .

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16
Q

what are some causes of denaturation ?

A

physical agents ( heat , agitation )

chemical agents (urea , acids)

17
Q

can proteins be renatured ?(go back to their original state)

A

only some proteins can do that.

18
Q

what can abnormal protein folding cause?

A

diseases such as Creutzfeldt-jakob disease or the mad cow disease .