Scooby-domain: prediction of globular domains in protein sequence
نویسندگان
چکیده
Scooby-domain (sequence hydrophobicity predicts domains) is a fast and simple method to identify globular domains in protein sequence, based on the observed lengths and hydrophobicities of domains from proteins with known tertiary structure. The prediction method successfully identifies sequence regions that will form a globular structure and those that are likely to be unstructured. The method does not rely on homology searches and, therefore, can identify previously unknown domains for structural elucidation. Scooby-domain is available as a Java applet at http://ibivu.cs.vu.nl/programs/scoobywww. It may be used to visualize local properties within a protein sequence, such as average hydrophobicity, secondary structure propensity and domain boundaries, as well as being a method for fast domain assignment of large sequence sets.
منابع مشابه
Identifying foldable regions in protein sequence from the hydrophobic signal
Structural genomics initiatives aim to elucidate representative 3D structures for the majority of protein families over the next decade, but many obstacles must be overcome. The correct design of constructs is extremely important since many proteins will be too large or contain unstructured regions and will not be amenable to crystallization. It is therefore essential to identify regions in pro...
متن کاملDiscovering Domains Mediating Protein Interactions
Background: Protein-protein interactions do not provide any direct information regarding the domains within the proteins that mediate the interactions. The majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. Most of the former studies focus only on interacting domain pairs. However they do not consider the in...
متن کاملPrediction of protein domain boundaries from inverse covariances
It has been known even since relatively few structures had been solved that longer protein chains often contain multiple domains, which may fold separately and play the role of reusable functional modules found in many contexts. In many structural biology tasks, in particular structure prediction, it is of great use to be able to identify domains within the structure and analyze these regions s...
متن کاملWhy do proteins divide into domains? Insights from lattice model simulations.
It is known that larger globular proteins are built from domains, relatively independent structural units. A domain size seems to be limited, and a single domain consists of from few tens to a couple of hundred amino acids. Based on Monte Carlo simulations of a reduced protein model restricted to the face centered simple cubic lattice, with a minimal set of short-range and long-range interactio...
متن کاملDesign and Production of Recombinant TAT Protein Structure, Catalytic Domain of Diphtheria Toxin, and Evaluation of Its Effect on Cell Line
Background and Objectives: Cancer is one of the most deadly diseases in the present age and its conventional therapies have had low success. Toxin therapy of cancer is a new therapeutic approach, which has attracted the attention of pharmaceutical specialists. Diphtheria toxin consists of three functional, transducing, and binding domains, that the functional part inhibits protein synthesis and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Nucleic Acids Research
دوره 33 شماره
صفحات -
تاریخ انتشار 2005