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CHEM LECT > Levels of Protein Structure > Flashcards

Levels of Protein Structure Flashcards

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1
Q

The SEQUENCE of AMINO ACIDS linked by the peptide bonds; information; determines the overall shape, function and properties

A

Primary Structure

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2
Q

In sickle cell hemoglobin, what replaces what which causes the error?

A

Valine (Hydrophobic amino acid) replacing a glutamic acid (negatively charged amino acid

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3
Q

Amino acid sequencing steps (3)

A
  1. Hydrolysis - affected by acid, alkali, or enzyme
  2. Identification of the products of hydrolysis
  3. Fitting the pieces together as in a jigsaw puzzle
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4
Q

Determination of the N-terminal amino acid (2)

A

A) Sanger’s method (2,4 - dinitrofluorobenzene)
B)Edman degradation (PITC, phenylisothiocyanate)

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5
Q

Determination of the C-terminal amino acid (2)

A

Carboxypeptidase A - cleaves peptide bonds w? AROMATIC amino acid

Carboxypeptidase B - cleaves basic amino acid residues

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6
Q

Used to cleavage the polypeptide into fragments (4)

A

Trypsin - most reliable, cleaves peptide bonds on the carboxyl side of arg and lys

Chymotrypsin - Cleaves peptide bonds on the carboxyl side of phe, tyr, and trp

Pepsin - cleaves peptide bonds at amino end of AROMATIC and ACIDIC amino acids

Cyanogen Bromide - CNBr cleaves peptide bonds on the carboxyl side

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7
Q

DNFB

A

tags the amino end (start), becomes DNP

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8
Q

Carboxypeptidase A and B

A

cuts the carboxyl end (right)

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9
Q

Trypsin

A

Arg Lys

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10
Q

Chymotrypsin

A

Phe Tyr Trp

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11
Q

Pepsin

A

Amino end of aromatic and acidic amino acids

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12
Q

The primary sequnce of a protein, chain of covalently linked amino acids, folds into regularly repeating structures that resemble designs in tapestry

results of hydrogen bonding between the amide hydrogens and the carbonyl oxygens of the peptide bonds

A

Secondary structure

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13
Q

Most common type of secondary structure

Adopts a shape like a coiled spring

A

alpha-helix

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14
Q

Parallel - chains run in the same direction, N terminals head to head

Antiparallel - chains run in the opposite direction; more stable N aligned to C

A

Beta-pleated Sheet

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14
Q

Formed when two polypeptide chain segments line up side by side

Parallel - chains run in the same direction, N terminals head to head

Antiparallel - chains run in the opposite direction; more stable N aligned to C

A

Beta-pleated Sheet

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15
Q

Proline and Glycine are prevalent in beta turns (why?)

A

Pro is able to adopt cis conformation like the glycine

16
Q

Results from interactions between amino acid side chains separated from each other

Defines biological function of proteins

Fibrous - mechanical strength, structural components
Globular - transport, regulatory, enzymes

A

Tertiary Structure

17
Q

Strong between two cysteine groups; strongest of the tertiary bonds

A

Disulfide bond

18
Q

Salt bridges between charged side chains of acidic and basic amino acids

A

Electrostatic interactions

19
Q

Between polar acidic and basic R groups, must be attached to O, N or F

A

H bonding

20
Q

Between non-polar side chains

A

Hydrophobic interactions

21
Q

Quarternary structure which is a protective coating for organs, major constituent of hair, mainly hydrophobic

determined hardness from S-S bonds, becomes more brittle

A

Alpha-Keratin (fibrous)

22
Q

Quarternary structure which is the most abundant protein in humans, Organic component of bones and teeth
Rich in proline

A

Collagen (fibrous)

23
Q

Quarternary structure Oxygen storage molecule, higher oxygen affinity than hemoglobin

Reserve oxygen source for working muscles

A

Myglobin (Globular)

24
Q

Quarternary Structure, Oxygen carrier molecule in the blood

Transport oxygen from lungs to tissues

A

Hemoglobin, globular

25
Q

Occurs when there is a change that disrupts the interactions between R groups

Covalent amide bonds of the primary structure aren’t affected

A

Denaturation

26
Q

Ways to denature proteins (6)

A

Temperature - bonds vibrate violently and become disrupted, produce coagulation

pH - if isoelectric point no longer have surface charge, may clump together or precipitate

Organic solvents - distupt hydrogen bonds of protein, and form bonds with water

Detergents - disrupt hydrophobic interactions

Heavy Metals - Interferes with salt bridges, loses conformation, precipitate

Agitation - Causes protein to stretch until it breaks

CHEM LECT (11 decks)

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