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Titlebook: Microcalorimetry of Biological Molecules; Methods and Protocol Eric Ennifar Book 2019 Springer Science+Business Media, LLC, part of Springe

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發(fā)表于 2025-3-28 17:02:13 | 只看該作者
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發(fā)表于 2025-3-28 20:03:30 | 只看該作者
The Contribution of Differential Scanning Calorimetry for the Study of Peptide/Lipid Interactionsicated in several pathologies. They constitute important targets because they are either at the basis of novel therapies (drug delivery for CPPs or antimicrobial activity for AMPs) or they are the agents causing these pathologies (viral and amyloid peptides). They all share the common property of in
43#
發(fā)表于 2025-3-29 03:00:10 | 只看該作者
Protocols of IATC, DSC, and PPC: The Multistate Structural Transition of Cytochrome terize the thermodynamic property changes accompanying three-dimensional structure changes. We developed isothermal acid-titration calorimetry (IATC) to evaluate the pH dependence of protein enthalpy. Using the double deconvolution method with precise differential scanning calorimetry (DSC), we reve
44#
發(fā)表于 2025-3-29 04:13:18 | 只看該作者
Plasmatic Signature of Disease by Differential Scanning Calorimetry (DSC). It allows to determine the denaturation temperature and enthalpy of individual domains of proteins, thus giving new insights into their domain organization and ligand interaction. Over the past decade, it has been shown that this technique can also be used to study biofluids such as plasma or cere
45#
發(fā)表于 2025-3-29 10:18:47 | 只看該作者
Intrinsic Thermodynamics of Protein-Ligand Binding by Isothermal Titration Calorimetry as Aid to Drun. This technique is commonly used in drug development programs when low-molecular-weight molecules are sought that bind tightly and specifically to a protein (disease target) molecule. The method allows a complete thermodynamic characterization of an interaction, i.e., ITC enables direct determinat
46#
發(fā)表于 2025-3-29 12:43:46 | 只看該作者
47#
發(fā)表于 2025-3-29 16:46:03 | 只看該作者
48#
發(fā)表于 2025-3-29 19:50:47 | 只看該作者
High-Quality Data of Protein/Peptide Interaction by Isothermal Titration Calorimetrys of affinities and thermodynamic parameters of single interactions in order to fully dissect the mechanisms of binding. To this end, isothermal titration calorimetry (ITC) is a well-established and convenient label-free technique covering a broad range of affinities..This review describes the caref
49#
發(fā)表于 2025-3-30 03:38:45 | 只看該作者
ITC Measurement for High-Affinity Aptamers Binding to Their Target Proteinsmatic evolution of ligands by exponential enrichment (SELEX). Because of their high affinity and specificity, aptamers were developed as therapeutic agents. Although aptamers are investigated as promising therapeutic agents, the mechanism of their high affinity and specificity is not clear. Therefor
50#
發(fā)表于 2025-3-30 04:43:39 | 只看該作者
Thermodynamics of Molecular Machines Using Incremental ITChly regulated tasks, with a remarkable accuracy. Significant advances in structural studies during the past 20?years provided a wealth of information regarding their architecture and considerably contributed to a better understanding of their mechanism of action. However, the three-dimensional struc
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