Common physical basis of macromolecule-binding sites in proteins
نویسندگان
چکیده
منابع مشابه
Common physical basis of macromolecule-binding sites in proteins
Protein-DNA/RNA/protein interactions play critical roles in many biological functions. Previous studies have focused on the different features characterizing the different macromolecule-binding sites and approaches to detect these sites. However, no common unique signature of these sites had been reported. Thus, this work aims to provide a 'common' principle dictating the location of the differ...
متن کاملCommon and distinct tubulin binding sites for microtubule-associated proteins.
A specific binding assay was developed that monitors the interaction of 125I-labeled microtubule-associated proteins (MAPs) with tubulin or its fragments bound to nitrocellulose membrane. To identify the tubulin-binding domains for MAPs we have examined the binding of rat brain 125I-labeled MAP2 or 125I-labeled tau factors to 60 peptides derived from porcine alpha- and beta-tubulin. MAP2 and ta...
متن کاملMetal Binding Sites in Proteins
Metal ions play a critical role in living systems. About one third of proteins need to bind metal for their stability and/or function. In this review, current sequence based and structure based methods for metal binding site prediction will be presented, with emphasis on the CHED and SeqCHED methods of prediction from apo-protein structures and protein sequences having homologs (even remote) in...
متن کاملEngineering metal-binding sites in proteins.
Metal-binding sites have been engineered into both de novo designed and naturally occurring proteins. Although the redesign of existing metal-binding sites in naturally occurring proteins still offers the most promise for a successful design, the more challenging goal of engineering metal-binding sites in de novo designed proteins and peptides is being achieved with increasing frequency. Creati...
متن کامل5'-Phosphate-Binding Sites in Proteins
many enzymic reactions. Almost all these pyridoxal phosphate-dependent enzymes have an absorption band around 415nm, although most of them have higher peaks at 335 nm. The studies made with simple models have shown that the 415nm band is due to a Schiffbase in a hydrophilic medium [structure (I) of Scheme 1] (Matsushima & Martell, 1967). The 335nm band can be assigned either to the structure (I...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 2008
ISSN: 1362-4962,0305-1048
DOI: 10.1093/nar/gkn868