Compaction and folding in model proteins
نویسندگان
چکیده
Protein folding is modeled as diffusion on a free-energy landscape, allowing use of the diffusion equation to study the impact of energetic parameters on the folding dynamics. The free-energy landscape is characterized by two different order parameters, one representing the degree of compactness, the other a measure of the progress towards the folded state. For marginally stable proteins, fastest folding is achieved when the nonspecific interactions favoring compaction are strong, resulting in a high folding temperature. Such proteins fold by rapid collapse followed by slower accumulation of correct contacts. © 1997 American Institute of Physics. S0021-9606 97 50435-1
منابع مشابه
Monitoring Protein Conformation along the Pathway of Chaperonin-Assisted Folding
The GroEL/GroES chaperonin system mediates protein folding in the bacterial cytosol. Newly synthesized proteins reach GroEL via transfer from upstream chaperones such as DnaK/DnaJ (Hsp70). Here we employed single molecule and ensemble FRET to monitor the conformational transitions of a model substrate as it proceeds along this chaperone pathway. We find that DnaK/DnaJ stabilizes the protein in ...
متن کاملMacromolecular crowding induces polypeptide compaction and decreases folding cooperativity.
A cell's interior is comprised of macromolecules that can occupy up to 40% of its available volume. Such crowded environments can influence the stability of proteins and their rates of reaction. Using discrete molecular dynamics simulations, we investigate how both the size and number of neighboring crowding reagents affect the thermodynamic and folding properties of structurally diverse protei...
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 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 کاملProtein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions
Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...
متن کامل