Probing the Molecular Origin of Native-State Flexibility in Repeat Proteins

Cohen, Sharona; Riven, Inbal; Cortajarena, Aitziber L.; Rosa, Lucía De; D’Andrea, Luca Domenico; Regan, Lynne; Haran, Gilad

doi:10.1021/jacs.5b06160

Cited by 16 publications

(15 citation statements)

References 49 publications

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“…The more extended CTPR4‐16 conformations maximize the π–π interactions of His, Tyr, and Trp residues located in the concave face of the protein with the SWCNT. The access to these extended conformations is in agreement with the previously reported flexibility of the CTPR superhelices . CTPR16 and CTPR8 systems can completely wrap the SWCNT.…”

Section: Resultssupporting

confidence: 91%

Toward Bioelectronic Nanomaterials: Photoconductivity in Protein–Porphyrin Hybrids Wrapped around SWCNT

López‐Andarias

Mejías

Sakurai

et al. 2017

Adv Funct Materials

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The development of sophisticated ordered functional materials is one of the important challenges in current science. One of the keys to enhance the properties of these materials is the control of the organization and morphology at different scales. This work presents a novel bioinspired methodology to achieve highly ordered donor/acceptor bio-nanohybrids using a designed repeat protein as scaffold, endowed with photoactive and electron donating porphyrin (P) units, to efficiently wrap around electron accepting single wall carbon nanotubes (SWCNT). A systematic experimental and theoretical study to evaluate the effect of the length of the protein reveals that longer proteins wrap around the SWCNT in a more efficient manner due to the stronger supramolecular interaction existing between the inner concave surface of the protein (namely Trp and His residues) and the convex surface of the (7,6)-SWCNT. Interestingly, spectroscopy and X-ray diffraction data further confirm that the so-called protein-P-SWCNT donor-acceptor bio-nanohybrids retain the original protein structure. Finally, the new bio-nanohybrids show a remarkable enhancement on the photoconductivity values by flash-photolysis microwave conductivity (FP-TRMC technique) demonstrating that the major charge carriers of electrons are injected into the SWCNTs and move along the 1D-structures.

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Section: Resultssupporting

confidence: 91%

Toward Bioelectronic Nanomaterials: Photoconductivity in Protein–Porphyrin Hybrids Wrapped around SWCNT

López‐Andarias

Mejías

Sakurai

et al. 2017

Adv Funct Materials

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“…1A). [27] There are several reasons that will account for the smaller size measured by AFM: (1) CTPR20-Cys adsorption onto gold surface through its thiol group might be tilted with an angle relative to an orthogonal orientation to the surface; (2) vertical elastic tip compression of the elongated superhelical structure, as it has been described for other repeat proteins; [54] (3) AFM characterizes single protein molecules in solution, which might have some flexibility [55] compared to the dimensions determined from the rigid crystal structure of the protein. [56] Following, CTPR20-Cys monolayer assembly on gold surface was studied.…”

Section: Resultsmentioning

confidence: 99%

Assembly of designed protein scaffolds into monolayers for nanoparticle patterning

Mejías

Couleaud

Casado

et al. 2016

Colloids and Surfaces B: Biointerfaces

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The controlled assembly of building blocks to achieve new nanostructured materials with defined properties at different length scales through rational design is the basis and future of bottom-up nanofabrication. This work describes the assembly of the idealized protein building block, the consensus tetratricopeptide repeat (CTPR), into monolayers by oriented immobilization of the blocks. The selectivity of thiol-gold interaction for an oriented immobilization has been verified by comparing a non-thiolated protein building block. The physical properties of the CTPR protein thin biomolecular films including topography, thickness, and viscoelasticity, are characterized. Finally, the ability of these scaffolds to act as templates for inorganic nanostructures has been demonstrated by the formation of well-packed gold nanoparticles (GNPs) monolayer patterned by the CTPR monolayer.

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“…Armadillo repeat domains, by comparison, are more rigid, although they are still sufficiently flexible to accommodate a range of different binding partners [4]. The computationally predicted nanospring behaviour of alpha-solenoid domains has been experimentally confirmed for a designed protein consisting of three TPR repeats [5]. Altogether, it appears likely that the consensus sequence of the repetitive units governs the global dynamics of the domain.…”

Section: Introductionmentioning

confidence: 89%

“…Altogether, it appears likely that the consensus sequence of the repetitive units governs the global dynamics of the domain. Depending on the specific functional role of the domain, this enables fine-tuning of its flexibility, while retaining stability against unfolding [5,6].…”

Section: Introductionmentioning

confidence: 99%

Disease-related single-point mutations alter the global dynamics of a tetratricopeptide (TPR) a-solenoid domain

Llabrés

Zachariae

2019

Preprint

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Tetratricopeptide repeat (TPR) proteins belong to the class of α-solenoid proteins, in which repetitive units of α-helical hairpin motifs stack to form superhelical, often highly flexible structures. TPR domains occur in a wide variety of proteins, and perform key functional roles including protein folding, protein trafficking, cell cycle control and post-translational modification. Here, we look at the TPR domain of the enzyme O-linked GlcNAc-transferase (OGT), which catalyses O-GlcNAcylation of a broad range of substrate proteins. A number of single-point mutations in the TPR domain of human OGT have been associated with the disease Intellectual Disability (ID). By extended steered and equilibrium atomistic simulations,we show that the OGT-TPR domain acts as a reversibly elastic nanospring, and that each of the ID-related local mutations substantially affect the global dynamics of the TPR domain. Since the nanospring character of the OGT-TPR domain is key to its function in binding and releasing OGT substrates, these changes of its biomechanics likely lead to defective substrate interaction. Our findings may not only help to explain the ID phenotype of the mutants, but also aid the design of TPR proteins with tailored biomechanical properties.

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Probing the Molecular Origin of Native-State Flexibility in Repeat Proteins

Cited by 16 publications

References 49 publications

Toward Bioelectronic Nanomaterials: Photoconductivity in Protein–Porphyrin Hybrids Wrapped around SWCNT

Toward Bioelectronic Nanomaterials: Photoconductivity in Protein–Porphyrin Hybrids Wrapped around SWCNT

Assembly of designed protein scaffolds into monolayers for nanoparticle patterning

Disease-related single-point mutations alter the global dynamics of a tetratricopeptide (TPR) a-solenoid domain

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