The ends of linear chromosomes - telomeres are protected by
specific protein complexes which bind telomeric ¬DNA. The human
teleomere binding complex consisting of  six proteins  is
called shelterin.
Protein TIN2 has central position in shelterin complex. Protein
TIN2 participates in three pivotal interactions within
shelterin protein complex, which makes this protein primary
target for detailed studies with the aim to clarify assembly
and function of shelterin complex.
In this diploma thesis, interactions of protein TIN2 with
protein TRF2 were characterized. Measurements of fluorescence
anisotropy were used for analysis of the binding affinity TIN2
and TRF2. The dissociation constant for the binding interaction
was estiamted. The results of this study could be used for
comparison of TIN2 binding affinity to other proteins of
shelterin complex and could contribute to elucidate the
mechanism of shelterin protein complex formation.
Even though the estiamation of stochiometric ratio for
interaction of proteins TIN2 and TRF2 by gel retardation assay
wasn`t successful, the initial results could be helpful for
future gel mobility studies of TRF2 protein and its
interaction.
New knowledge of molecular properites of shelterin protein
complex could help to shed more ligt on structure and function
of the complicated shelterin protein complex, which stabilizes
shape of telomeres and regulates their prolongation. These
finding could be used in applications that could once lead into
possibility of direct control of telomere length. These new
possibilities of molecular regulation of cell life would
allowed mankind to rejuvenate cells and selectively heal cancer
tissues.