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Modular enzyme design: regulation by mutually exclusive protein folding

Modular enzyme design: regulation by mutually exclusive protein folding

http://www.wikidata.org/entity/Q42845389

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The Expanding Landscape of Moonlighting Proteins in Yeasts Structural and Thermodynamic Analysis of a Conformationally Strained Circular Permutant of Barnase †Engineering Domain-Swapped Binding Interfaces by Mutually Exclusive Folding On the mechanism of protein fold-switching by a molecular sensor.Engineering an artificial zymogen by alternate frame protein folding Molecular simulations of mutually exclusive folding in a two-domain protein switch.Structural specificity in coiled-coil interactions.Chemical biology strategies for posttranslational control of protein function.Regulated unfolding of proteins in signaling Challenges in the computational design of proteins Influence of Secondary-Structure Folding on the Mutually Exclusive Folding Process of GL5/I27 Protein: Evidence from Molecular Dynamics Simulations.Designing switchable enzymes Converting a protein into a switch for biosensing and functional regulation.Engineering protein switches: sensors, regulators, and spare parts for biology and biotechnology.Protein conformational switches: from nature to design.Protein design in systems metabolic engineering for industrial strain development.Protein unfolding with a steric trap.Designing redox potential-controlled protein switches based on mutually exclusive proteins Effect of interdomain linker length on an antagonistic folding-unfolding equilibrium between two protein domains.Engineered Domain Swapping as an On/Off Switch for Protein Function.Thermodynamic analysis of an antagonistic folding-unfolding equilibrium between two protein domains.A genetically encoded copper(I) sensor based on engineered structural distortion of EGFP.

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P2860

Modular enzyme design: regulation by mutually exclusive protein folding

http://www.wikidata.org/entity/Q42845389

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2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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name

Modular enzyme design: regulation by mutually exclusive protein folding

@en

Modular enzyme design: regulation by mutually exclusive protein folding

@nl

type

label

Modular enzyme design: regulation by mutually exclusive protein folding

@en

Modular enzyme design: regulation by mutually exclusive protein folding

@nl

prefLabel

Modular enzyme design: regulation by mutually exclusive protein folding

@en

Modular enzyme design: regulation by mutually exclusive protein folding

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J.JMB.2006.01.073

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Journal of Molecular Biology

P1476

Modular enzyme design: regulation by mutually exclusive protein folding

@en

P2093

Diana M Mitrea

http://www.w3.org/2001/XMLSchema#string

James S Butler

http://www.w3.org/2001/XMLSchema#string

Jeung-Hoi Ha

http://www.w3.org/2001/XMLSchema#string

Stewart N Loh

http://www.w3.org/2001/XMLSchema#string

P2860

X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil

Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

Urea unfolding of peptide helices as a model for interpreting protein unfolding.

Allosteric switching by mutually exclusive folding of protein domains

GCN4 binds with high affinity to DNA sequences containing a single consensus half-site.

Barnase has subsites that give rise to large rate enhancements.

Conditional cell ablation by stringent tetracycline-dependent regulation of barnase in mammalian cells.

A novel strategy for regulated expression of a cytotoxic gene.

Monomeric and dimeric bZIP transcription factor GCN4 bind at the same rate to their target DNA site.

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1058-1062

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10.1016/J.JMB.2006.01.073

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4

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357

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16483603

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protein folding

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3145369

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