Mechanical stability of proteins.
نویسندگان
چکیده
A number of experiments and experimentally based simulations showed that beta-proteins are mechanically more stable than alpha-proteins. However, the theory that might explain this evidence is still lacking. In this paper we have developed a simple elastic theory, which allows to estimate critical forces for stretching both kinds of proteins. It has been shown that unfolding of beta-proteins does really require notably higher forces as compared to the stretching of alpha-proteins.
منابع مشابه
A review of methods to increase the stability of recombinant pharmaceutical proteins during the production and storage process
The production of biotechnological drug proteins plays an important role against disease. The process of producing drug recombinant proteins is not a direct path, because it requires a lot of work and on the other hand, one of the important and significant aspects in the production of proteins is the discussion of their stability and solubility during the expression and purification process. Pr...
متن کاملSingle molecule force spectroscopy reveals engineered metal chelation is a general approach to enhance mechanical stability of proteins.
Significant mechanical stability is an essential feature shared by many elastomeric proteins, which function as molecular springs in a wide variety of biological machinery and biomaterials of superb mechanical properties. Despite the progress in understanding molecular determinants of mechanical stability, it remains challenging to rationally enhance the mechanical stability of proteins. Using ...
متن کاملThe influence of disulfide bonds on the mechanical stability of proteins is context dependent.
Disulfide bonds play a crucial role in proteins, modulating their stability and constraining their conformational dynamics. A particularly important case is that of proteins that need to withstand forces arising from their normal biological function and that are often disulfide bonded. However, the influence of disulfides on the overall mechanical stability of proteins is poorly understood. Her...
متن کاملOsmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
متن کاملSingle molecule force spectroscopy reveals that electrostatic interactions affect the mechanical stability of proteins.
It is well known that electrostatic interactions play important roles in determining the thermodynamic stability of proteins. However, the investigation into the role of electrostatic interactions in mechanical unfolding of proteins has just begun. Here we used single molecule atomic force microscopy techniques to directly evaluate the effect of electrostatic interactions on the mechanical stab...
متن کاملOsmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of chemical physics
دوره 131 2 شماره
صفحات -
تاریخ انتشار 2009