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

GNAT

1064-3745 practical, .Microcalorimetry of Biological Molecules: Methods and Protocols. aims to ensure successful results in the further study of this vital field..978-1-4939-9179-2Series ISSN 1064-3745 Series E-ISSN 1940-6029

軟弱

Value of DSC in Characterization and Optimization of Protein StabilityDifferential scanning calorimetry (DSC) is a well-established technique for biomolecular stability studies. The technique is based on forced thermal denaturation of biomolecules in solution. Here we describe the use of DSC for characterization and optimization of stability of two proteins, a protein kinase and a mAb protein.

Multiple

Analysis of Isothermal Titration Calorimetry Data for Complex Interactions Using I2CITC for systems involving a self-aggregating ligand and a host offering one or two binding sites can be analyzed, how interaction models can be tested, and how confidence intervals for the optimized parameters can be determined.

Opponent

encomiast

Microcalorimetry of Biological Molecules978-1-4939-9179-2Series ISSN 1064-3745 Series E-ISSN 1940-6029

GOAT

Methods in Molecular Biologyhttp://image.papertrans.cn/m/image/633126.jpg

細(xì)微差別

https://doi.org/10.1007/978-1-4939-9179-2thermodynamic parameters; structure-based drug design; enzyme kinetics; conformational changes; isotherm

不幸的人

Eric EnnifarIncludes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains keynotes and implementation advice from the experts

Hypomania

Protocols of IATC, DSC, and PPC: The Multistate Structural Transition of Cytochrome aled that the MG state is an equilibrium intermediate state of the reversible thermal three-state transition of the protein, and we successfully determined its volumetric properties by pressure perturbation calorimetry (PPC). Our findings underscore the importance of a precise calorimetry and analysis model for protein research.

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