Coiled coils are important structural modules and domains of protein-protein interactions. Further, they provide the required framework to proteins, like kinesins, myosins and SNAREs, which are either structural or involved in transport of biomolecules. We provide an interactive webserver to measure the strength of interactions between two helices involved in coiled coils. Interactions are measured using non-bonded and electrostatic interactions and the presence of hydrogen bonds and salt bridges. The sum of these interactions is expressed as psuedoenergy, whose ranges have been standardized using all structural entries that are classified to contain coiled coils. The results are displayed conveniently as energy per residue along with optio...
Coiled coils represent the simplest form of a complex formed between two interacting protein partner...
Coiled coils represent the simplest form of a complex formed between two interacting protein partner...
Additional resources and features associated with this article are available within the HTML version...
Coiled coils are important structural modules and domains of protein-protein interactions. Further, ...
Abstract Background Coiled-coils are found in different proteins like transcription factors, myosin ...
Coiled-coil motifs are elements of protein structure, which, whilst based on relatively simple seque...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
Coiled Coils are simple quarternary protein struc-tures that are used frequently in studies involvin...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
Coiled Coils are simple tertiary protein structures that are used frequently in studies involving pr...
Protein-protein interactions play a central role in many cellular functions, and as whole-genome dat...
AbstractProtein-protein interactions are sometimes mediated by coiled coil structures. The evolution...
Coiled coils represent the simplest form of a complex formed between two interacting protein partner...
Coiled coils represent the simplest form of a complex formed between two interacting protein partner...
Additional resources and features associated with this article are available within the HTML version...
Coiled coils are important structural modules and domains of protein-protein interactions. Further, ...
Abstract Background Coiled-coils are found in different proteins like transcription factors, myosin ...
Coiled-coil motifs are elements of protein structure, which, whilst based on relatively simple seque...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
Coiled Coils are simple quarternary protein struc-tures that are used frequently in studies involvin...
The coiled-coil is a widespread protein structural motif known to have a stabilization function and ...
Coiled Coils are simple tertiary protein structures that are used frequently in studies involving pr...
Protein-protein interactions play a central role in many cellular functions, and as whole-genome dat...
AbstractProtein-protein interactions are sometimes mediated by coiled coil structures. The evolution...
Coiled coils represent the simplest form of a complex formed between two interacting protein partner...
Coiled coils represent the simplest form of a complex formed between two interacting protein partner...
Additional resources and features associated with this article are available within the HTML version...