منابع مشابه
Protein 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 کاملProtein folds and protein folding.
The classification of protein folds is necessarily based on the structural elements that distinguish domains. Classification of protein domains consists of two problems: the partition of structures into domains and the classification of domains into sets of similar structures (or folds). Although similar topologies may arise by convergent evolution, the similarity of their respective folding pa...
متن کاملChirality and Protein Folding
There are several simple criteria of folding to a native state in model proteins. One of them involves crossing of a threshold value of the root mean square deviation distance away from the native state. Another checks whether all native contacts are established, i.e. whether the interacting amino acids come closer than some characteristic distance. We use Go-like models of proteins and show th...
متن کامل10 Protein Folding
Since Anfinsen’s famous experiments in the 1960s, it has been known that the complex three‐ dimensional structure of protein molecules is encoded in their amino acid sequences, and the chains autonomously fold under proper conditions. Cracking this code, which is sometimes called ‘‘the second part of the genetic code,’’ has been one of the greatest challenges of molecular biology. Although a fu...
متن کاملSub-microsecond protein folding.
We have investigated the structure, equilibria, and folding kinetics of an engineered 35-residue subdomain of the chicken villin headpiece, an ultrafast-folding protein. Substitution of two buried lysine residues by norleucine residues stabilizes the protein by 1 kcal/mol and increases the folding rate sixfold, as measured by nanosecond laser T-jump. The folding rate at 300 K is (0.7 micros)(-1...
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ژورنال
عنوان ژورنال: Chemistry & Biology
سال: 2000
ISSN: 1074-5521
DOI: 10.1016/s1074-5521(00)00096-x