Molecular dynamic simulation of Hum an Lysozyme: insig ht into the thermal s tability of enzyme

Understanding the dynamic of protein h as been a subject of study in both theoretical and experimental biophysics[۱]. C omputer si mulations act as a bridge between microscopic length and ti me scales an d the macro scopic world of the laboratory. In this work, we have perfo rmed molecular dynamic simulation and component analy sis of the H uman Lyso zyme enzy me in soluti on of salts and ethanol. Human lyso zyme itself is a relatively simple structure made up of ۱۳ ۰ residues.T his protein is presentin high con centration in various tissues and fluids including liver, articular cartilage, saliva and tears[۲]. Its native structure consists of two domains: an alph a-domain that has fou r alpha-helices (A–D) and one ۳/۱۰ helix, and a betado main, which consists mainly of an antiparallel betasheet and a long loop.

کلیدواژه ها:

Huma n Lysozym e ، Molecular Dynamics ، Protein Sta bility ، Solvent Accessible Surfac e.