Original Articles
K Mukherjee1, A. K. Bothra2 an
Abstract
A fundamental appreciation for how biological macromolecules work requires knowledge of structure and its dynamics. Molecular dynamics simulation provides links between structure and dynamics by enabling the exploration of the conformational energy landscape accessible to protein molecules. In this perspective we illustrate the application of molecular dynamics simulations to biology by describing the conformational changes of Human Telomere Repeat Binding factor 2 (hTRF2). hTRF2 is a sequence specific DNA-binding protein. The progress of the simulation was monitored by calculating several structural parameters over time in both the vacuum and water condition. The result shows some huge amount of fluctuation in the region of N-terminal end of the hTRF2 that give us some new information about the structural changes of the global protein.