The Next Generation in Membrane Protein Structure Determination

Herausgegeben:Moraes, Isabel

• Gebundenes Buch

Produktbeschreibung

This book reviews current techniques used in membrane protein structural biology, with a strong focus on practical issues. The study of membrane protein structures not only provides a basic understanding of life at the molecular level but also helps in the rational and targeted design of new drugs with reduced side effects. Today, about 60% of the commercially available drugs target membrane proteins and it is estimated that nearly 30% of proteins encoded in the human genome are membrane proteins. In recent years much effort has been put towards innovative developments to overcome the numerous obstacles associated with the structure determination of membrane proteins.
This book reviews a variety of recent techniques that are essential to any modern researcher in the field of membrane protein structural biology. The topics that are discussed are not commonly found in textbooks. The scope of this book includes:

Expression screening using fluorescent proteins
The use of detergents in membrane protein research
The use of NMR
Synchrotron developments in membrane protein structural biologyVisualisation and X-ray data collection of microcrystalsX-ray diffraction data analysis from multiple crystals
Serial millisecond crystallographySerial femtosecond crystallographyMembrane protein structures in drug discovery

The information provided in this book should be of interest to anyone working in the area of structural biology. Students will find carefully prepared overviews of basic ideas and advanced protein scientists will find the level of detail required to apply the material directly to their day to day work.

Chapters 4, 5, 6, 8 and 9 of this book are published open access under a CC BY 4.0 license at link.springer.com.

Produktdetails

• Advances in Experimental Medicine and Biology 922
• Verlag: Springer / Springer International Publishing / Springer, Berlin / Wellcome Trust
• Artikelnr. des Verlages: 978-3-319-35070-7
• 1st ed. 2016
• Seitenzahl: 196
• Erscheinungstermin: 5. September 2016
• Englisch
• Abmessung: 260mm x 183mm x 17mm
• Gewicht: 543g
• ISBN-13: 9783319350707
• ISBN-10: 3319350706
• Artikelnr.: 44806974

Inhaltsangabe

Expression Screening of Integral Membrane Proteins by Fusion to Fluorescent Reporters.- Detergents in Membrane Protein Purification and Crystallisation.- NMR of Membrane Proteins: Beyond Crystals.- Characterisation of Conformational and Ligand Binding Properties of Membrane Proteins Using Synchrotron Radiation Circular Dichroism (SRCD).- Membrane Protein Crystallization: Current Trends and Future Perspectives.- Crystal Dehydration in Membrane Protein Crystallography.- Nonlinear Optical Characterization of Membrane Protein Microcrystals and Nanocrystals.- Exploiting Microbeams for Membrane Protein Structure Determination.- Applications of the BLEND Software to Crystallographic Data from Membrane Proteins.- Serial Millisecond Crystallography of Membrane Proteins.- Serial Femtosecond Crystallography of Membrane Proteins.- Beyond Membrane Protein Structure: Drug Discovery, Dynamics and Difficulties.

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Expression Screening of Integral Membrane Proteins by Fusion to Fluorescent Reporters.- Detergents in Membrane Protein Purification and Crystallisation.- NMR of Membrane Proteins: Beyond Crystals.- Characterisation of Conformational and Ligand Binding Properties of Membrane Proteins Using Synchrotron Radiation Circular Dichroism (SRCD).- Membrane Protein Crystallization: Current Trends and Future Perspectives.- Crystal Dehydration in Membrane Protein Crystallography.- Nonlinear Optical Characterization of Membrane Protein Microcrystals and Nanocrystals.- Exploiting Microbeams for Membrane Protein Structure Determination.- Applications of the BLEND Software to Crystallographic Data from Membrane Proteins.- Serial Millisecond Crystallography of Membrane Proteins.- Serial Femtosecond Crystallography of Membrane Proteins.- Beyond Membrane Protein Structure: Drug Discovery, Dynamics and Difficulties.