Lactoferrin is a 80 kDa glycoprotein responsible for binding ferric ions from physiological fluids. Due to its main feature and the fact that it presents structural similarities to serum transferrin this protein was accepted as a member of transferrins family. Human lactoferrin consists of a single polypeptide chain of 691 amino acids, mostly organized in α-helix and β-sheets structures. The chain is folded into two globular lobes, referred to as the N- and C- lobes connected by a 3-turn-helix peptide chain [1]. In the both the C- and Nbinding sites the metal is coordinated by four amino acid side chains: an aspartic acid, two tyrosines and a histidine. The coordination is completed in each binding site by a synergistic carbonate/bicarbonate anion. Iron binding process leads to conformational changes within the protein structure (see Figure 1.). We have investigated theoretically the apo-open and apo-closed forms of human lactoferrin using the performance capabilities of Molecular Dynamics simulations technique. Results of this study will help gain additional understanding about the process of iron binding and iron release by human lactoferrin. Main chain representation produced using VMD [2] software package for the open iron-free and (1LFH pdb code) and closed iron-loaded (1B0L) forms of the Nterminal of human lactoferrin. Position of the carbonate ion and iron ion are presented in the closed form of the studied protein.