The N-terminal to C-terminal motif in protein folding and function
نویسندگان
چکیده
منابع مشابه
The N-terminal to C-terminal motif in protein folding and function.
Essentially all proteins known to fold kinetically in a two-state manner have their N- and C-terminal secondary structural elements in contact, and the terminal elements often dock as part of the experimentally measurable initial folding step. Conversely, all N-C no-contact proteins studied so far fold by non-two-state kinetics. By comparison, about half of the single domain proteins in the Pro...
متن کاملHow determinant is N-terminal to C-terminal coupling for protein folding?
This work investigates the role of N- to C- termini coupling in the folding transition of small, single domain proteins via extensive Monte Carlo simulations of both lattice and off-lattice models. The reported results provide compelling evidence that the existence of native interactions between the terminal regions of the polypeptide chain (i.e. termini coupling) is a major determinant of the ...
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مالاریا یکی از بیماری های مهم انگلی در کشورهای گرمسیری دنیا است. پلاسمودیوم فالسیپاروم انگل تک یاخته ای است که تب سه یک بدخیم را ایجاد می کند. آنتی ژن های پلاسمودیوم فالسیپاروم در سطح انگل یا در سطح سلول های آلوده ،کاندیداهای عمده جهت تولید واکسن می باشند، مانند: msp 1 و msp2 . کربوهیدرات های متصل به پروتئین های انگل مالاریا بعنوان اپی توپ های آنتی ژنیک مطرح بوده و بوسیله سیستم ایمنی میزبان تشخ...
Contrasting Function of Structured N-Terminal and Unstructured C-Terminal Segments of Mycobacterium tuberculosis PPE37 Protein
Pathogens frequently employ eukaryotic linear motif (ELM)-rich intrinsically disordered proteins (IDPs) to perturb and hijack host cell networks for a productive infection. Mycobacterium tuberculosis has a relatively high percentage of IDPs in its proteome, the significance of which is not known. The Mycobacterium-specific PE-PPE protein family has several members with unusually high levels of ...
متن کاملMotif within the C-Terminal Binding Region
The reovirus capsid protein o3 was examined for double-stranded RNA (dsRNA)-binding activity by Northwestern (RNA-protein) blot analysis. Treatment of virion-derived o3 protein with Staphylococcus aureus V8 protease led to an increase in the dsRNA-binding activity associated with the C-terminal fragment of the protein. Recombinant C-terminal fragments of the o3 protein were expressed in Escheri...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2005
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0409114102