Works (3)
Updated: July 5th, 2023 15:58
2018 journal article
Measurements and correlation of liquid-liquid equilibrium data for the ternary (methyl tert-butyl ketone plus o, m, p-benzenediol plus water) system at (333.2, 343.2 and 353.2) K
CHINESE JOURNAL OF CHEMICAL ENGINEERING, 27(4), 905–911.
author keywords: Liquid-liquid equilibrium; Methyl tert-butyl ketone; Benzenediol; NRTL model; UNIQUAC model
UN Sustainable Development Goal Categories
6. Clean Water and Sanitation
(OpenAlex)
13. Climate Action
(Web of Science)
Source: Web Of Science
Added: June 17, 2019
2006 journal article
Substitutions of prolines examine their role in kinetic trap formation of the caspase recruitment domain (CARD) of RICK
PROTEIN SCIENCE, 15(3), 395–409.
author keywords: caspase recruitment domain; RICK; Greek key; folding kinetics; equilibrium folding; folding intermediates; kinetic traps
MeSH headings : Amino Acid Substitution; Binding Sites; Caspase 1; Caspases / chemistry; Caspases / metabolism; Circular Dichroism; Enzyme Precursors / chemistry; Enzyme Precursors / metabolism; Kinetics; Models, Molecular; Proline / chemistry; Proline / genetics; Protein Folding; Protein Serine-Threonine Kinases / chemistry; Protein Serine-Threonine Kinases / genetics; Protein Serine-Threonine Kinases / metabolism; Protein Structure, Tertiary; Receptor-Interacting Protein Serine-Threonine Kinase 2; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / chemistry; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / genetics; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / metabolism
TL;DR:
The results show that P85 is critical for maintaining the function of the protein and that all mutations decrease the stability, and the complex folding pathway, especially formation of kinetically trapped species, is not due to prolyl isomerism.
(via Semantic Scholar)
open access via onlinelibrary.wiley.com (publisher PDF)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
15. Life on Land
(OpenAlex)
Source: Web Of Science
Added: August 6, 2018
2004 journal article
Kinetic traps in the folding/unfolding of procaspase-1 CARD domain
PROTEIN SCIENCE, 13(8), 2196–2206.
author keywords: caspase recruitment domain; alpha-helical Greek key; kinetic trap; double jump; interrupted refolding; equilibrium folding
MeSH headings : Amino Acid Sequence; Animals; Caspase 1; Caspases / chemistry; Caspases / genetics; Chromatography, Gel; Enzyme Precursors / chemistry; Enzyme Precursors / genetics; Humans; Kinetics; Molecular Sequence Data; Protein Denaturation / genetics; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary / genetics
TL;DR:
The data show that both unfolding and refolding processes are slow, and the pathways contain kinetically trapped species.
(via Semantic Scholar)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
Source: Web Of Science
Added: August 6, 2018
Citation Index includes data from a number of different sources. If you have questions about the sources of data in the Citation Index or need a set of data which is free to re-distribute, please contact us.
Certain data included herein are derived from the Web of Science© and InCites© (2024) of Clarivate Analytics. All rights reserved. You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.