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Protein Structure - PowerPoint PPT Presentation


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Protein Structure. FDSC400. Biological?. Food?. Protein Functions. Protein Structure. 20 Amino Acids. Coded in DNA. Primary. Secondary. Self assembly to a single (native) structure. Depends on primary structure and solution conditions. Tertiary. ( ). Quaternary.

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protein structure1
Protein Structure

20 Amino Acids

Coded in DNA

Primary

Secondary

Self assembly to a single (native) structure. Depends on primary structure and solution conditions

Tertiary

( )

Quaternary

Common in foods. Many non-native forms depending on protein structure, solution conditions (& history) and ingredient interactions

Denatured

amino acids
Amino Acids
  • The monomer unit of proteins
  • R is the side chain.
  • One of 20 different chemical compounds
  • Some R-groups are acid (other alkali)
  • Some R-groups are water soluble (others are not)

Chiral carbon (L-series)

amino acids1
Polar

Uncharged. Ser, Thr, Asn, Gln, Cys

Positive (basic). Arg, Lys, His

Negative (acidic). Asp, Glu,

Non-Polar

Aliphatic. Ala, Ile, Leu, Met, Pro, Val

Aromatic. Phe, Trp, Tyr

Amino Acids
example amino acids
Example Amino Acids

Alanine

Phenylalanine

Glutamic acid

peptide bonds
Peptide Bonds

Amino acids

Water

peptide bonds1

O

C N

H

Peptide Bonds

:

-

O

C N

H

+

disulfide bonds
Two cysteine molecules under oxidizing conditions

Intermolecular or intramolecular cross-link

Disulfide Bonds
a helix
N-H to C=O hydrogen bonds in 4th succeeding A.A.

Hydrogen bonds parallel to axis

Typically amphiphilic

a-Helix
amphiphilic 2 structures
Amphiphilic 2° Structures

Hydrophilic

Hydrophobic

b sheet
C=O and N-H perpendicular to chain form inter-segment H-bonds

Parallel or antiparallel

b-strands typically 5-15 A.A.

More stable than a-helix

b-Sheet

b-sheet

slide13

Protein Folding

Hydrophobic amino acids

Peptide chain

types of tertiary structure
Types of Tertiary Structure

Globular

Disordered

Fibrous

Many insoluble amino acids, protein tends to minimize surface/volume ratio

Interacts well with water and takes up a random configuration

Strong secondary structure allows protein to retain a non-spherical shape

quaternary structure
Quaternary Structure

Folded protein unable to contain some hydrophobic residues

Dimerized protein shields the hydrophobic amino acids from water