Optimizing Seed Aging for Single Crystal Gold Nanorod Growth: The Critical Role of Gold Nanocluster Crystal Structure

2016 ◽  
Vol 120 (49) ◽  
pp. 28235-28245 ◽  
Author(s):  
Kyoungweon Park ◽  
Ming-Siao Hsiao ◽  
Hilmar Koerner ◽  
Ali Jawaid ◽  
Justin Che ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Critical Role ◽  
Gold Nanorod ◽  
Gold Nanocluster ◽  
Seed Aging ◽  
Nanorod Growth

Short Gold Nanorod Growth Revisited: The Critical Role of the Bromide Counterion

ChemPhysChem ◽  
2011 ◽  
Vol 13 (1) ◽  
pp. 193-202 ◽  
Author(s):  
Satyabrata Si ◽  
Cecile Leduc ◽  
Marie-Hélène Delville ◽  
Brahim Lounis
Keyword(s):  
Critical Role ◽  
Gold Nanorod ◽  
Nanorod Growth

scholarly journals From single crystal surfaces to single atoms: investigating active sites in electrocatalysis

Nanoscale ◽  
2014 ◽  
Vol 6 (8) ◽  
pp. 4012-4026 ◽  
Author(s):  
Anthony P. O'Mullane
Keyword(s):  
Single Crystal ◽  
Active Sites ◽  
Critical Role ◽  
Crystal Surfaces ◽  
Single Crystal Surfaces ◽  
Single Atoms

Electrocatalysis will be at the heart of energising future transportation and technology. This article discusses the critical role of active sites and the recent efforts in their characterisation and visualisation.

scholarly journals Crystal Structure of INTS3/INTS6 complex reveals Functional Importance of INTS3 dimerization in DSB Repair

2020 ◽  
Author(s):  
Yu Jia ◽  
Zixiu Cheng ◽  
Sakshibeedu R Bharath ◽  
Qiangzu Sun ◽  
Nannan Su ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Critical Role ◽  
Repair Process ◽  
Dsb Repair ◽  
Ssdna Binding ◽  
C Terminus ◽  
Ssdna Binding Protein ◽  
Direct Binding ◽  
Biochemical Analyses

AbstractSOSS1 is a single-stranded DNA (ssDNA)-binding protein complex that plays a critical role in double-strand DNA break (DSB) repair. SOSS1 consists of three subunits: INTS3, SOSSC, and hSSB1 with INTS3 serving as a scaffold to stabilize this complex. Moreover, the integrator complex subunit 6 (INTS6) participates in the DNA damage response through direct binding to INTS3 but how INTS3 interacts with INTS6 thereby, impacting DBS repair is not clear. Here, we determined the crystal structure of the C-terminus of INTS3 (INTS3c) in complex with the C-terminus of INTS6 (INTS6c) at a resolution of 2.4 Å. Structure analysis revealed that two INTS3c subunits dimerize and interact with INTS6c via conserved residues. Subsequent biochemical analyses confirmed that INTS3c forms a stable dimer and INTS3 dimerization is important for recognizing the longer ssDNA. Perturbation of INTS3c dimerization and disruption of the INTS3c/INTS6c interaction, impair the DSB repair process. Altogether, these results unravel the underappreciated role of INTS3 dimerization and the molecular basis of INTS3/INTS6 interaction in DSB repair.

scholarly journals Potential photoacid generators based on oxime sulfonates

2019 ◽  
Vol 43 (1-2) ◽  
pp. 26-33
Author(s):  
M John Plater ◽  
William TA Harrison ◽  
Ross Killah
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Single Crystal Structure ◽  
Fragmentation Pathways ◽  
X Ray ◽  
Photoacid Generators ◽  
Structure Determinations ◽  
Secondary Reactions

The bis-oxime of acenaphthenequinone and the mono-oxime of benzil have been sulfonated by reaction with 4-methylbenzenesulfonyl chloride and propylsulfonyl chloride. The four sulfonated oximes were characterised by X-ray single-crystal structure determinations. Some photochemical decompositions were studied using a 6-W 254-nm immersion well lamp in dichloromethane. The 4-methylbenzenesulfonate bis-oxime of acenaphthenequinone and the 4-methylbenzenesulfonate mono-oxime of benzil both give 4-methylbenzenesulfonic acid upon irradiation but not 4-methylbenzenesulfinic acid. Fragmentation pathways are discussed. The possible use of these compounds as photoacid generators in polymer resists and the role of secondary reactions to liberate acid is discussed.

scholarly journals Crystal structure of the INTS3/INTS6 complex reveals the functional importance of INTS3 dimerization in DSB repair

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Yu Jia ◽  
Zixiu Cheng ◽  
Sakshibeedu R. Bharath ◽  
Qiangzu Sun ◽  
Nannan Su ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Critical Role ◽  
Repair Process ◽  
Dsb Repair ◽  
Ssdna Binding ◽  
C Terminus ◽  
Ssdna Binding Protein ◽  
Direct Binding ◽  
Biochemical Analyses

AbstractSOSS1 is a single-stranded DNA (ssDNA)-binding protein complex that plays a critical role in double-strand DNA break (DSB) repair. SOSS1 consists of three subunits: INTS3, SOSSC, and hSSB1, with INTS3 serving as a scaffold to stabilize this complex. Moreover, the integrator complex subunit 6 (INTS6) participates in the DNA damage response through direct binding to INTS3, but how INTS3 interacts with INTS6, thereby impacting DSB repair, is not clear. Here, we determined the crystal structure of the C-terminus of INTS3 (INTS3c) in complex with the C-terminus of INTS6 (INTS6c) at a resolution of 2.4 Å. Structural analysis revealed that two INTS3c subunits dimerize and interact with INTS6c via conserved residues. Subsequent biochemical analyses confirmed that INTS3c forms a stable dimer and INTS3 dimerization is important for recognizing the longer ssDNA. Perturbation of INTS3c dimerization and disruption of the INTS3c/INTS6c interaction impair the DSB repair process. Altogether, these results unravel the underappreciated role of INTS3 dimerization and the molecular basis of INTS3/INTS6 interaction in DSB repair.

HMT-Induced and NaOH Assisted Hydrothermal Synthesis of ZnO Single Crystal Nanorods

2013 ◽  
Vol 311 ◽  
pp. 413-418 ◽  
Author(s):  
Kuo Chin Hsu ◽  
Jiunn Der Liao ◽  
Yaw Shyan Fu
Keyword(s):  
Crystal Structure ◽  
Hydrothermal Synthesis ◽  
Aspect Ratio ◽  
Single Crystal ◽  
Hydrothermal Method ◽  
Zno Nanorods ◽  
Single Crystal Structure ◽  
Good Crystallinity ◽  
Zno Single Crystal ◽  
Nanorod Growth

This experiment involves the growth of ZnO nanorods with NaOH by the HMT-assisted hydrothermal method and discusses the efficiency of NaOH is helpful to the growth of ZnO nanorods. The analyses of the synthesized ZnO nanorods by XRD, SEM, EDS and TEM reveal a single crystal structure with good crystallinity where the nanorod growth is along the [001] direction. In addition, it is discovered experimentally that the aspect ratio of the product is increased with the addition of NaOH, which verifies that the basic environment is beneficial to the growth of ZnO nanorods.

scholarly journals Human hepatic tryptophan 2,3-dioxygenase ubiquitin-dependent protein degradation: The critical role of its exosite as the molecular lynchpin of its substrate-mediated protein stabilization

2019 ◽  
Author(s):  
Sung-Mi Kim ◽  
Yi Liu ◽  
YongQiang Wang ◽  
Shay Karkashon ◽  
Ariel Lewis-Ballester ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Essential Amino Acid ◽  
Opposite Effect ◽  
Critical Role ◽  
Protein Stabilization ◽  
High Affinity ◽  
Dependent Protein ◽  
Rate Limiting

AbstractHepatic tryptophan 2,3-dioxygenase (TDO) is a cytoplasmic homotetrameric hemoprotein and the rate-limiting enzyme in the irreversible degradation of the essential amino acid L-tryptophan (L-Trp) to N-formylkynurenine, thus controlling the flux of L-Trp into its serotonergic and kynureninic/NAD pathways. TDO has long been recognized to be substrate-inducible via protein stabilization, but the molecular mechanism of this stabilization has remained elusive. Recent elucidation of human TDO (hTDO) crystal structure has identified a high-affinity (Kd ≈ 0.5 μM) Trp-binding exosite in each of its 4 monomeric subunits. Mutation of the Glu105, Trp208 and Arg211 comprising this exosite not only abolished the high-affinity L-Trp binding, but also accelerated the ubiquitin-dependent proteasomal degradation of hTDO. We have further characterized this hTDO degradation by documenting that its ubiquitination by gp78/AMFR and CHIP E2/E3 ligase complexes occurs on external Lys-residues within or vicinal to acidic Asp/Glu and phosphorylated pSer/pThr (DEpSpT)-clusters. Furthermore, we have identified the unstructured hTDO N- and C-termini as imparting relatively high proteolytic instability, as their deletion (ΔNC) markedly prolonged hTDO t1/2. Additionally, although previous studies reported that upon hepatic heme-depletion, the heme-free apoTDO turns over with a t1/2 ≈ 2.2 h relative to the t1/2 of 7.7 h of holoTDO, mutating the axial heme-ligating His328 to Ala has the opposite effect of prolonging hTDO t1/2. Most importantly, introducing the exosite mutation into the ΔNC-deleted or H328A-mutant completely abolished their prolonged half-lives irrespective of L-Trp presence or absence, thereby revealing that the exosite is the molecular lynchpin that defines L-Trp-mediated TDO induction via protein stabilization.

scholarly journals Electrochemical reduction of O2 in Ca2+ containing DMSO – Role of roughness and single crystal structure

ChemSusChem ◽  
2021 ◽  
Author(s):  
Andreas Koellisch-Mirbach ◽  
Inhee Park ◽  
Martina Hegemann ◽  
Elke Thome ◽  
Helmut Baltruschat
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Electrochemical Reduction ◽  
Single Crystal Structure
Sign in / Sign up

Export Citation Format

Share Document