Titlebook: Synthetic Protein Switches; Methods and Protocol Viktor Stein Book 2017 Springer Science+Business Media LLC 2017 Bioluminescent sensors.Flu

Chameleon

增长

Synthetic Protein Switches: Theoretical and Experimental Considerationssical, and biochemical information to modeling the structure and function of proteins ab initio. The following chapter provides an overview over the theoretical considerations and experimental approaches that have been successful applied in the construction of synthetic protein switches.

frenzy

Construction of Allosteric Protein Switches by Alternate Frame Folding and Intermolecular Fragment Elecular biology, and construct optimization—remain the same for any target protein. We highlight effective strategies as well as common pitfalls based on our experience with multiple AFF and FREX constructs.

phlegm

Construction of Protein Switches by Domain Insertion and Directed Evolutioninput signal (such as the binding of a molecule, recognition of light). Here, we describe several methods for randomly fusing two domains to create domain insertion libraries from which protein switches can be identified by selections and/or screens.

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STALL

Creation of Antigen-Dependent β-Lactamase Fusion Protein Tethered by Circularly Permuted Antibody Va Fv introduced with two circular permutations, called Clampbody. By tethering the Clampbody to a circularly permuted TEM-1 β-lactamase (BLA), we successfully constructed a genetically encoded molecular switch Cbody-cpBLA that shows antigen-dependent catalytic activity.

竖琴

Synthetic Protein Switches: Theoretical and Experimental Considerationsumber of successful design strategies emerging, the construction of synthetic protein switches still frequently necessitates an integrated approach that combines detailed biochemical and biophysical characterization in combination with high-throughput screening to construct tailored synthetic protei

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Construction of Allosteric Protein Switches by Alternate Frame Folding and Intermolecular Fragment Eteins that have no pre-existing allosteric properties. One of their chief purposes is to turn an ordinary protein into a biomolecular switch capable of transforming an input event into an optical or functional readout. Here, we present a guide for converting an arbitrary binding protein into a fluor

acrobat

Construction of Protein Switches by Domain Insertion and Directed Evolutionitches can be created by fusing two domains in such a way that the activity of the output domain is regulated by the input domain’s recognition of an input signal (such as the binding of a molecule, recognition of light). Here, we describe several methods for randomly fusing two domains to create do

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