Topic
Substrate (chemistry)
About: Substrate (chemistry) is a research topic. Over the lifetime, 35902 publications have been published within this topic receiving 740722 citations. The topic is also known as: enzyme substrate.
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141 citations
TL;DR: Tertbutylallylcobalttricarbonyl (tBu-AllylCo(CO)3) is shown to have strong substrate selectivity during atomic layer deposition of metallic cobalt as mentioned in this paper.
Abstract: Tertbutylallylcobalttricarbonyl (tBu-AllylCo(CO)3) is shown to have strong substrate selectivity during atomic layer deposition of metallic cobalt. The interaction of tBu-AllylCo(CO)3 with SiO2 surfaces, where hydroxyl groups would normally provide more active reaction sites for nucleation during typical ALD processes, is thermodynamically disfavored, resulting in no chemical reaction on the surface at a deposition temperature of 140 °C. On the other hand, the precursor reacts strongly with H-terminated Si surfaces (H/Si), depositing ∼1 ML of cobalt after the first pulse by forming Si–Co metallic bonds. This remarkable substrate selectivity of tBu-AllylCo(CO)3 is due to an ALD nucleation reaction process paralleling a catalytic hydrogenation, which requires a coreactant that acts as a hydrogen donor rather than a source of bare protons. The chemical specificity demonstrated in this work suggests a new paradigm for developing selective ALD precursors. Namely, selectivity can be achieved by tailoring the li...
141 citations
TL;DR: The enzyme was shown to be a tetramer which has a molecular weight of about 230,000 and is composed of two different types of subunits, indicating that the structural integrity of the enzyme is maintained in part by either intrachain or interchain disulfide bonds.
141 citations
TL;DR: chemical modification of about 80% of the free amino groups with PEG chains significantly improved the resistance to heat and detergents and might result from the formation of a highly hydrogen-bonded structure around the enzyme.
141 citations
TL;DR: The emergence of compensatory drug-resistant mutations in HIV-1 protease challenges the common view of the reaction mechanism of this enzyme by performing classical and ab initio molecular dynamics simulations on a complex between the enzyme and a peptide substrate.
140 citations