Globular and fibrous proteins: haemoglobin and collagen

Membranes, Proteins, DNA and Gene Expression · Proteins and enzymes · note 3 of 6

Globular and fibrous proteins: haemoglobin and collagenSpec 2.6

In short

Globular proteins such as haemoglobin are compact, rounded and soluble, with hydrophilic R groups outside, so they carry out metabolic roles. Fibrous proteins such as collagen are long and rope-like, insoluble and strong, with many cross-links, so they provide structural support. Each structure suits its function.

Globular and fibrous proteins compared
FeatureGlobular (for example haemoglobin)Fibrous (for example collagen)
ShapeCompact, rounded, folded.Long, rope-like fibres.
SolubilitySoluble in water: hydrophilic R groups face outwards, hydrophobic R groups face inwards.Insoluble: many hydrophobic R groups on the outside.
StructureComplex tertiary (and often quaternary) structure.Repetitive amino acid sequence; little tertiary folding; chains wound together.
RoleMetabolic: transport, enzymes, hormones, antibodies.Structural: strength and support.

Haemoglobin

Haemoglobin is a globular protein with quaternary structure: four polypeptide chains (two alpha and two beta chains). Each chain is folded around a haem group that contains an iron ion (Fe²⁺), which binds one oxygen molecule, so each haemoglobin molecule can carry four oxygen molecules. The hydrophilic R groups on the outside make haemoglobin soluble in the cytoplasm of red blood cells, and the precise shape allows it to bind and release oxygen.

Collagen

Collagen is a fibrous protein found in tendons, skin, bones, the walls of arteries and cartilage. Three polypeptide chains, each a left-handed helix, are wound together into a right-handed triple helix. Every third amino acid is glycine, the smallest amino acid, which allows the three chains to pack tightly together. The chains are held together by many hydrogen bonds, and neighbouring collagen molecules are linked by covalent cross-links, making fibrils and fibres. This gives collagen a very high tensile strength and makes it insoluble, which suits its structural function.

Exam tip:

Always link structure to function: 'haemoglobin is soluble because hydrophilic R groups are on the outside, so it can be carried in the cytoplasm of red blood cells'; 'collagen has high tensile strength because of hydrogen bonds between three chains and cross-links between molecules'.

Haemoglobin with two alpha and two beta chains, each with a haem group containing Fe2+ and bound oxygen and hydrophilic R groups on the outside, and collagen as a triple helix of three chains cross-linked into a fibril. (opens full size in a new tab)
Haemoglobin is globular and soluble; collagen is fibrous with high tensile strength.

Written and checked against the Edexcel International AS Level Biology (XBI11) specification · Updated October 2026

Frequently asked questions

What is the difference between primary, secondary, tertiary and quaternary protein structure?

Primary structure is the sequence of amino acids joined by peptide bonds. Secondary is coiling into an alpha helix or folding into a beta pleated sheet, held by hydrogen bonds. Tertiary is the overall 3D folding, held by hydrogen, ionic and disulfide bonds. Quaternary is two or more polypeptides together.

How are the structures of haemoglobin and collagen related to their functions?

Haemoglobin is globular and soluble, with four polypeptides each holding an iron-containing haem group that binds oxygen. Collagen is fibrous and insoluble: three polypeptides form a triple helix with hydrogen bonds and cross-links, giving great tensile strength for support in tendons and skin.

Why do enzymes denature at high temperatures?

High temperatures give the enzyme molecule more kinetic energy, which breaks the hydrogen and ionic bonds holding the tertiary structure. The active site changes shape, so the substrate can no longer fit, and the enzyme-substrate complex cannot form. This denaturation is not reversible.

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