What is she best known for?
The fields of study she is best known for:
- Organic chemistry
- Enzyme
- Catalysis
Her primary areas of study are Stereochemistry, Substrate, Enzyme catalysis, Catalysis and Binding energy.
Tina L. Amyes combines subjects such as Decarboxylation and Active site with her study of Stereochemistry.
Her Decarboxylation study combines topics in areas such as Deprotonation and Transition state.
While the research belongs to areas of Deprotonation, Tina L. Amyes spends her time largely on the problem of Hydroxide, intersecting her research to questions surrounding Medicinal chemistry and Aqueous solution.
Her work deals with themes such as Dihydroxyacetone phosphate and Triosephosphate isomerase, which intersect with Substrate.
Her Catalysis study combines topics from a wide range of disciplines, such as Inorganic chemistry, Carbanion and Photochemistry.
Her most cited work include:
- Formation and Stability of N-Heterocyclic Carbenes in Water: The Carbon Acid pKa of Imidazolium Cations in Aqueous Solution (384 citations)
- Lifetimes of oxocarbenium ions in aqueous solution from common ion inhibition of the solvolysis of α-azido ethers by added azide ion (118 citations)
- A role for flexible loops in enzyme catalysis. (114 citations)
What are the main themes of her work throughout her whole career to date?
Her scientific interests lie mostly in Stereochemistry, Substrate, Medicinal chemistry, Catalysis and Reaction rate constant.
Her study in Stereochemistry is interdisciplinary in nature, drawing from both Active site, Decarboxylation, Enzyme kinetics and Triosephosphate isomerase.
Her Triosephosphate isomerase research incorporates elements of Isomerase, Carboxylate, DHAP, Glyceraldehyde and Isomerization.
Tina L. Amyes interconnects Inorganic chemistry, Iminium, Acid dissociation constant, Organic chemistry and Deprotonation in the investigation of issues within Medicinal chemistry.
Her is doing research in Glycolaldehyde and Enzyme catalysis, both of which are found in Catalysis.
Along with Reaction rate constant, other disciplines of study including Carbocation, Photochemistry, Azide, Aqueous solution and Reactivity are integrated into her research.
She most often published in these fields:
- Stereochemistry (45.60%)
- Substrate (28.00%)
- Medicinal chemistry (29.60%)
What were the highlights of her more recent work (between 2012-2021)?
- Stereochemistry (45.60%)
- Substrate (28.00%)
- Catalysis (24.80%)
In recent papers she was focusing on the following fields of study:
Tina L. Amyes spends much of her time researching Stereochemistry, Substrate, Catalysis, Enzyme kinetics and Triosephosphate isomerase.
Her research in Stereochemistry intersects with topics in Dihydroxyacetone phosphate, Active site, Isomerase, Decarboxylation and Glycolaldehyde.
The study incorporates disciplines such as Orotidine 5'-phosphate decarboxylase, Conformational change and Enzyme in addition to Decarboxylation.
Tina L. Amyes conducted interdisciplinary study in her works that combined Enzyme kinetics and Orotidine.
Her Triosephosphate isomerase research is multidisciplinary, relying on both Enzyme catalysis and Deprotonation.
The various areas that she examines in her Deprotonation study include Carboxylate and Isomerization.
Between 2012 and 2021, her most popular works were:
- Enzyme architecture: on the importance of being in a protein cage. (63 citations)
- Specificity in Transition State Binding: The Pauling Model Revisited (58 citations)
- Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomerase. (31 citations)
In her most recent research, the most cited papers focused on:
- Organic chemistry
- Enzyme
- Catalysis
Tina L. Amyes focuses on Stereochemistry, Triosephosphate isomerase, Catalysis, Substrate and Glycolaldehyde.
Her Stereochemistry research includes elements of Decarboxylation, Enzyme kinetics and Deprotonation.
Her studies in Deprotonation integrate themes in fields like Dihydroxyacetone phosphate and Carboxylate.
In her study, Diaminopimelate epimerase, Directed evolution, Protein engineering and Enzyme catalysis is strongly linked to Active site, which falls under the umbrella field of Triosephosphate isomerase.
Her work investigates the relationship between Catalysis and topics such as Reactivity that intersect with problems in Substituent.
Tina L. Amyes integrates many fields in her works, including Substrate and Side chain.
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