Structural Basis of Conformational Transitions Involved in Pseudopilus Assembly and Stability

stability and attraction domains of traffic equilibria in day-to-day dynamical system formulation

در این پژوهش مسئله واگذاری ترافیک را از دید سیستم های دینامیکی فرمول بندی می کنیم.فرض کرده ایم که همه فاکتورهای وابسته در طول زمان ثابت باشند و تعادل کاربر را از طریق فرایند منظم روزبه روز پیگیری کنیم.دینامیک ترافیک توسط یک نگاشت بازگشتی نشان داده می شود که تکامل سیستم در طول زمان را نشان می دهد.پایداری تعادل و دامنه جذب را توسط مطالعه ویژگی های توپولوژیکی تکامل سیستم تجزیه و تحلیل می کنیم.پاید...

Structural Plasticity and Conformational Transitions of HIV Envelope Glycoprotein gp120

HIV envelope glycoproteins undergo large-scale conformational changes as they interact with cellular receptors to cause the fusion of viral and cellular membranes that permits viral entry to infect targeted cells. Conformational dynamics in HIV gp120 are also important in masking conserved receptor epitopes from being detected for effective neutralization by the human immune system. Crystal str...

Structural basis of conformational transitions in the active site and 80′s loop in the FK506-binding protein FKBP12

The extensive set of NMR doublings exhibited by the immunophilin FKBP12 (FK506-binding protein 12) arose from a slow transition to the cis-peptide configuration at Gly89 near the tip of the 80's loop, the site for numerous protein-recognition interactions for both FKBP12 and other FKBP domain proteins. The 80's loop also exhibited linebroadening, indicative of microsecond to millisecond conform...

Structural basis of human γ-secretase assembly.

The four-component intramembrane protease γ-secretase is intricately linked to the development of Alzheimer's disease. Despite recent structural advances, the transmembrane segments (TMs) of γ-secretase remain to be specifically assigned. Here we report a 3D structure of human γ-secretase at 4.32-Å resolution, determined by single-particle, electron cryomicroscopy in the presence of digitonin a...

Predicting slow structural transitions in macromolecular systems: Conformational flooding.