Molecular dynamic simulation study o n native and glycate d form of myoglobin

The prevalence of diabetes ha s reached epidemic proportions wo rldwide. Diabetes mellitus is a chronic meta bolic disorder charac terized by rise in blood gluco se level called “hyperglycemia“[۱]. Increased glucose c oncentration in diabetes mellitus causes glycation of several proteins like hemoglo bin and myoglobin, lea ding to change in their properties. These heme-containing proteins are involved in the storage and transfe r of oxygen within blood and muscle cells [۲]. Poor blood glucose control increase s the risk of heart attack, kidney fa ilure, blindn ess etc. The preferential glycation sites of hem oglobin ha ve been dete cted, while there have been few structural studies on myoglobin [۳]. In this stu dy we intent to discus s the impact of N-terminal glycation of myoglobin on the stability of its secondary structure

کلیدواژه ها:

myog lobin ، glyca ted myoglobin ، molecular dynamic simulation ، potential energy