Using the Ring‐Shaped Protein TRAP to Capture and Confine Gold Nanodots on a Surface.

Heddle, Jonathan G.; Fujiwara, Isamu; Yamadaki, Hirokazu; Yoshii, Shigeo; Nishio, Kazuaki; Addy, Christine; Yamashita, Ichiro; Tame, J.R.H.

doi:10.1002/smll.200700400

Cited by 37 publications

(34 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Biomineralization using cage proteins such as ferritin and viral capsids has been shown to be possible if suitable mutations are introduced into the protein cavity (Douglas et al 2002;Miura et al 2006). We have shown it is possible to alter the inner cavity of the TRAP ring in the same way (Heddle et al 2007a). To form ordered arrays on surfaces, however, 12-fold symmetry is much more suitable than 11-fold symmetry.…”

Section: Discussionmentioning

confidence: 99%

Intersubunit linker length as a modifier of protein stability: Crystal structures and thermostability of mutant TRAP

et al. 2008

Self Cite

View full text Add to dashboard Cite

The ability of proteins to self-assemble into complex, functional nanoscale structures is expected to become of significant use in the manufacture of artificial nanodevices with a wide range of novel applications. The bacterial protein TRAP has potential uses as a nanoscale component as it is ringshaped, with a central, modifiable cavity. Furthermore, it can be engineered to make a ring of 12-fold symmetry, which is advantageous for packing into two-dimensional arrays. The 12mer form of TRAP is made by linking multiple subunits together on the same polypeptide, but the usefulness of the 12mers described to date is limited by their poor stability. Here we show that, by altering the length of the peptide linker between subunits, the thermostability can be significantly improved. Since the subunit interfaces of the different 12mers are essentially identical, stabilization arises from the reduction of strain in the linkers. Such a simple method of controlling the stability of modular proteins may have wide applications, and demonstrates the lack of absolute correlation between interactions observable by crystallography and the internal energy of a complex.

show abstract

Section: Discussionmentioning

confidence: 99%

Intersubunit linker length as a modifier of protein stability: Crystal structures and thermostability of mutant TRAP

et al. 2008

Self Cite

View full text Add to dashboard Cite

show abstract

“…In this study TRAP is employed as a model for investigating the influences of oligomeric state and stability of such assemblies. To date TRAP has already alluded to its value in bionanotechnology, showing that mutations to residues protruding into the central cavity allow gold nanoparticle binding [11]. Nanotubes consisting of stacked TRAP rings linked by disulfide bonds have also been shown to self-assemble, in response to the introduction of cysteine residues on the ring-faces orthogonal to the principal axis [12].…”

Section: Introductionmentioning

confidence: 99%

Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer

et al. 2012

View full text Add to dashboard Cite

BackgroundSubunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.Methodology/Principal FindingsAmong the wild type B. stearothermophilus, B. halodurans and B. subtilis TRAP, we find that the former is the most stable whilst the latter is the least. Thermal stability of all TRAP is shown to increase with L-tryptophan concentration. We also find that mutant TRAP molecules that are truncated at the C-terminus - and hence induced to form 12-mers, distinct from their 11-mer wild type counterparts - have increased melting temperatures. We show that the same effect can be achieved by a point mutation S72N at a subunit interface, which leads to exclusion of C-terminal residues from the interface. Our findings are supported by dye-based scanning fluorimetry, CD spectroscopy, and by crystal structure and mass spectrometry analysis of the B. subtilis S72N TRAP.Conclusions/SignificanceWe conclude that the oligomeric state of a circular protein can be changed by introducing a point mutation at a subunit interface. Exclusion (or deletion) of the C-terminus from the subunit interface has a major impact on properties of TRAP oligomers, making them more stable, and we argue that the cause of these changes is the altered oligomeric state. The more stable TRAP oligomers could be used in potential applications of TRAP in bionanotechnology.

show abstract

“…As well as an interesting and well-defined shape, the protein has other properties useful to bionanoscience, these include high thermostability [108] and ability to tolerate many surface mutations without a change in overall structure. To date, TRAP has been used to produce symmetry altered structures [109], as a component of a floating nanodot gate transistor [110], and to construct a self-assembled protein nanotube [111].…”

Section: Catalysis By Gnp Itselfmentioning

confidence: 99%

Gold Nanoparticle-Biological Molecule Interactions and Catalysis

Heddle

2013

Catalysts

View full text Add to dashboard Cite

This review gives a brief summary of the field of gold nanoparticle interactions with biological molecules, particularly those with possible catalytic relevance. Gold nanoparticles are well known as catalysts in organic chemistry but much is unknown regarding their potential as catalysts of reactions involving biological molecules such as protein and nucleic acids. Biological molecules may be the substrate for catalysis or, if they are the ligand coating the gold particle, may be the catalyst itself. In other cases biological molecules may form a template upon which gold nanoparticles can be precisely arrayed. As relatively little is currently known about the catalytic capabilities of gold nanoparticles in this area, this review will consider templating in general (including, but not restricted to, those which result in structures having potential as catalysts) before going on to consider firstly catalysis by the gold nanoparticle itself followed by catalysis by ligands attached to gold nanoparticles, all considered with a focus on biological molecules.

show abstract

Using the Ring‐Shaped Protein TRAP to Capture and Confine Gold Nanodots on a Surface.

Cited by 37 publications

References 23 publications

Intersubunit linker length as a modifier of protein stability: Crystal structures and thermostability of mutant TRAP

Intersubunit linker length as a modifier of protein stability: Crystal structures and thermostability of mutant TRAP

Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer

Gold Nanoparticle-Biological Molecule Interactions and Catalysis

Contact Info

Product

Resources

About