In our previous study, a set of homology models of the tetramerization (T1) domain of six eukaryotic potassium channels Kv1.1-Kv1.6 from Homo Sapiens was constructed based on the crystal structure of the Shaker T1 domain from Aplysia californica. The results reveal that the T1 domains of these Kv channels exhibit similar folds as those of Shaker K+ channel. In this study, several molecular dynamics (MD) simulations towards the Shaker and Kv1.1 T1 domains were conducted at various temperatures. Our results show that the Shaker T1 domain exhibit higher structural integrity than the Kv1.1 T1 domain at all temperatures examined. In addition, the thermal unfolding of the Shaker T1 domain begins at layer 3. In contrast, layers land 2 exhibit higher structural stability because layer I remains more hydrogen bonding interactions at elevated temperatures and layer 2 is located in the highly conserved hydrophobic core. Ile121 in the Shaker T1 domain plays an important role in disrupting the loop between helices 4 and 5. During the thermal unfolding process, the newly formed hydrophobic interactions between Ala120, Ile121, Leu122, Leu131, and Leu151 may distort the native contact between layers 2 and 3 of the T1 domain.