CHEM 160 MODULE 3.

PROTEINS

RESOURCE 4: PROTEIN STRUCTURE, FOLDING AND DENATURATION

FOUR LEVELS OF PROTEIN ARCHITECTURE

A. Primary Structure – refers to the definite amino acid sequence in a protein brought about by
stable, covalent peptide bonds

B. Secondary Structure – refers to the regular repetitive conformation of amino acids that are
spatially close to one another

– dictated by the maximum H-bonding involving the carbonyl group of

one peptide bond and the amino group of another

Types of secondary structures

1. -helix – right-handed helix with 3.6 amino acids per turn

– helix rises 5.4 angstroms for each turn (pitch)
– stabilized by H-bonding between the carbonyl oxygen of one peptide bond
and the amide hydrogen of another peptide bond 4 amino acid residues away
– interrupted by 2 or more consecutive residues with like charges or bulky
groups

2. -pleated sheets – repeating units of amino acids with small compact R groups
– can be parallel or anti-parallel
– interchain H-bonding exists among peptide bonds

Figure 1. The α-helix and β-pleated sheet (OpenStax College, Biology (CC BY 3.0)).

C. Tertiary Structure – three-dimensional structure resulting from R-group interactions

– coils may be looped, twisted, or folded upon itself in a variety of ways

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 Figure 2. Types of R-group interactions (OpenStax College, Biology (CC BY 3.0)).

Classification based on three-dimensional structure

Fibrous proteins – consist of polypeptide chains arranged side by side in long filaments
– tend to be mechanically strong and insoluble in water
– have structural or protective role

Ex. Collagen – principal constituent of connective tissue in animals

Globular proteins – coiled into compact, roughly spherical shape

– generally soluble in water and are mobile within cells

Ex. Hemoglobin, Immunoglobulins

The tertiary structure is stabilized by R-group interactions and are therefore dictated by the
primary structure. Thus, to function in a certain way, a protein must have the correct tertiary
structure.

D. Quaternary Structure – concerns interactions by which two or more polypeptide chains

associate in a specific manner to form biologically active proteins
– formed by noncovalent association of tertiary structures
– evident among globular proteins

Oligomer – 2 or more polypeptides (protomers or subunits)

Ex. Hemoglobin (tetramer)

Tobacco mosaic virus (has 2,130 subunits)

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 Figure 3. The four levels of protein structure (OpenStax College, Biology (CC BY 3.0)).

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 DENATURATION OF PROTEINS

A protein is defined by its primary, secondary, and tertiary structures. This gives the protein
certain identifying properties – biological, enzymatic, solubility, ionic, reactivity of side group, MW,
and size → NATIVE STRUCTURE.

Any change in the native structure results in DENATURATION, brought about by disruption
of forces that stabilize the secondary, tertiary, and quaternary structures.

urea, heat

extremes of pH

Native conformation Random-coil

Source:

Lecture Booklet in Biochemistry. November 2014. Biochemistry and Agricultural Chemistry Division,
Institute of Chemistry, University of the Philippines Los Baños, College, Laguna. pp. 10-11

“Proteins” by OpenStax College, Biology (CC BY 3.0):

https://cnx.org/contents/GFy_h8cu@11.10:2zzm1QG9@8/Proteins. The Openstax book can be
downloaded for free at https://openstax.org/details/books/biology.

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