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Biochemistry (BY1BC1) > Week 8 (Proteins I) > Flashcards

Week 8 (Proteins I) Flashcards

1
Q

What are proteins?

A

A linear polymer of amino acids (Amino acids joined together to form long chains)

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2
Q

How many different amino acids are there?

A

20

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3
Q

How do amino acids differ?

A

Amino acids all have the same basic structure, but with one side chain that differs

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4
Q

Which isomers are found in proteins?

A

Only L-amino acids are found in proteins

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5
Q

How to amino acid side chains vary?

A

Side chains vary in size, shape, charge, polarity and chemical reactivity

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6
Q

Which amino acid isn’t chiral?

A

Glycines variable group is ‘H’ so does not have 4 different groups attached to the central carbon atom

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7
Q

Which amino acid links to itself?

A

Proline

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8
Q

what is the 1 letter code for Glycine?

A

G (Gly)

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9
Q

what is the 1 letter code for Alanine?

A

A (Ala)

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10
Q

what is the 1 letter code for Valine?

A

V (Val)

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11
Q

what is the 1 letter code for Leucine?

A

L (Leu)

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12
Q

what is the 1 letter code for Isoleucine?

A

I (Ile)

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13
Q

what is the 1 letter code for Methionine?

A

M (Met)

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14
Q

what is the 1 letter code for Proline?

A

P (Pro)

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15
Q

what is the 1 letter code for Phenylalanine?

A

F (Phe)

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16
Q

what is the 1 letter code for Tryptophan?

A

W (Trp)

17
Q

what is the 1 letter code for Serine?

A

S (Ser)

18
Q

what is the 1 letter code for Threonine?

A

T (Thr)

19
Q

what is the 1 letter code for Cysteine?

A

C (Cys)

20
Q

what is the 1 letter code for Tyrosine?

A

Y (Tyr)

21
Q

what is the 1 letter code for Asparagine?

A

N (Asn)

22
Q

what is the 1 letter code for Glutamine?

A

E (Gln)

23
Q

what is the 1 letter code for Aspartic Acid?

A

D (Asp)

24
Q

what is the 1 letter code for Glutamic Acid?

A

E (Glu)

25
Q

what is the 1 letter code for Lysine?

A

K (Lys)

26
Q

what is the 1 letter code for Arginine?

A

R (Arg)

27
Q

what is the 1 letter code for Histidine?

A

H (His)

28
Q

What is each amino acid within a polypeptide chain called?

A

A residue

29
Q

How do you know which is residue number 1?

A
  • Chain has an amino or N – terminus and a carboxyl or C – terminus.
  • Always go from amino to carboxyl
  • the N-terminal residue is numbered 1.
30
Q

What is the primary structure?

A

The primary structure of a protein is simply the amino acid sequence in the polypeptide chain Every protein has a unique, precisely defined sequence

The function of a protein is dependent upon its amino acid sequence

31
Q

What determines the 3D structure of a protein?

A

Proteins fold up into complex 3-D shapes/structures which are essential for their function, and the structure is determined by the amino acid sequence.

32
Q

Describe folding of the polypeptide chain

A
  • The polypeptide chain is quite flexible and can fold up to form structures
  • 3 types of non-covalent bond help to stabilise the folded structure
33
Q

What is the secondary structure?

A

Secondary structure is when the sequence of amino acids are linked by hydrogen bonds (between the amino hydrogen N-H and carboxyl oxygen C=O atoms in the peptide backbone) to form repeating structures:

  • α-helices
  • β-sheets

-Turns & loops

34
Q

Describe an alpha helix

A
  • The polypeptide chain forms a helical coil
  • Hydrogen bonding stabilises the structure
  • Amino acid side chains protrude on the outside of the helix
35
Q

What are important measurements characteristic of alpha helices?

A

Right-handed helix

  • you go from left to right as you go up the helix 36 amino acids per 10 turns = 3.6 amino acids per turn Pitch
  • distance along the long axis for one turn of the helix = 0.54 nm
  • Rise per amino acid = 0.15 nm
  • The C=O group of a residue i hydrogen bonds with the N-H group of residue i+4 along the sequence
36
Q

Describe the properties of beta sheets

A
  • Comprised of 2 or more polypeptide β-strands
  • Hydrogen bonding between the strands holds them together in a sheet
  • Strands can be parallel or anti-parallel
  • Amino acid side chains are alternately above and below the plane of the β-sheet
  • Sometimes referred to as β-pleated sheet
37
Q

What are beta turns?

A
  • Many amino acids are found in turns or loops
  • Particularly common are β-turns or hairpin turns, which connect the ends of two adjacent segments of an antiparallel β-sheet
  • Commonly contain proline residues (its unique structure allows a tighter turn) and glycine (small and flexible)
38
Q

What is the single letter code for each amino acid?

A

Biochemistry (BY1BC1) (17 decks)

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