Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Susan E. Taylor"'
Publikováno v:
Polymers, Vol 10, Iss 6, p 678 (2018)
The need for a sustainable development and improved whole life performance of concrete infrastructure has led to the requirement of more durable and sustainable concrete bridges alongside accurate predictive analysis tools. Using the combination of S
Externí odkaz:
https://doaj.org/article/057c4533e7ff4141945899cf1c031b8d
Expansive corrosion in steel reinforcement significantly reduces the design life and durability of concrete structures. Composite materials such as Glass Fibre Reinforced Polymer (GFRP) and Basalt Fibre Reinforced Polymer (BFRP) can provide a more du
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b46c3d8ac11a71c70b925b98e6138be7
https://doi.org/10.21203/rs.3.rs-2264455/v1
https://doi.org/10.21203/rs.3.rs-2264455/v1
Publikováno v:
Journal of the Chemical Society, Perkin Transactions 2. :751-755
Oxaldie-4, a 31-residue polypeptide designed to catalyse the decarboxylation of oxaloacetate, has been synthesised and its structural and catalytic properties characterised. The solution structure of Oxaldie-4 was studied by CD and NMR spectroscopy.
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 11:2631-2635
The synthesis of Oxaldie-3, a synthetic 31-residue peptide with oxaloacetate decarboxylase activity, is described. Biophysical characterisation by gel filtration, CD and NMR spectroscopy indicated that the peptide adopted a folded structure in soluti
Autor:
Susan E. Taylor, Kenneth B. White
Publikováno v:
Groundwater Monitoring & Remediation. 15:74-76
Publikováno v:
Chemical communications (Cambridge, England). (17)
Analysis of the hydrocarbons produced during catalysis by mutants of aristolochene synthase from Penicillium roqueforti indicated that Trp 334 had a pivotal function for the efficient production of aristolochene from farnesylpyrophosphate most likely
Publikováno v:
Chemical communications (Cambridge, England). (20)
A mutant of Aristolochene Synthase (AS), in which Tyr 92 was replaced by Val, produced the alicyclic beta-(E)-farnesene as the major product, indicating that cyclisation of FPP is controlled by Tyr 92 in AS.
Publikováno v:
Chemical Communications. :2384-2385
A mutant of Aristolochene Synthase (AS), in which Tyr 92 was replaced by Val, produced the alicyclic β-(E)-farnesene as the major product, indicating that cyclisation of FPP is controlled by Tyr 92 in AS.