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The Resource Intrinsically disordered protein analysis, Volume 2, Methods and experimental tools, edited by Vladimir N. Uversky, A. Keith Dunker

Intrinsically disordered protein analysis, Volume 2, Methods and experimental tools, edited by Vladimir N. Uversky, A. Keith Dunker

Label
Intrinsically disordered protein analysis, Volume 2, Methods and experimental tools
Title
Intrinsically disordered protein analysis
Title number
Volume 2
Title part
Methods and experimental tools
Statement of responsibility
edited by Vladimir N. Uversky, A. Keith Dunker
Title variation
Methods and experimental tools
Contributor
Subject
Genre
Language
eng
Summary
Over the past decade, there has been an explosive development of research of intrinsically disordered proteins (IDPs), which are also known as unfolded proteins. Structural biologists now recognize that the functional diversity provided by disordered regions complements the functional repertoire of ordered protein regions. In Intrinsically Disordered Protein Analysis: Methods and Experimental Tools, expert researchers explore the high abundance of IDPs in various organisms, their unique structural features, numerous functions, and crucial associations with different diseases. Volume 2 includes sections on single molecule techniques, methods to assess protein size and shape, analyzing conformational behavior, mass-spectrometry, expression and purification of IDP's. Written in the highly successful Methods in Molecular Biology series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory. Thorough and intuitive, Intrinsically Disordered Protein Analysis: Methods and Experimental Tools helps scientists further their investigations of these fascinating and dynamic molecules
Member of
Dewey number
572.6
Illustrations
illustrations
Index
index present
Language note
English
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
http://library.link/vocab/relatedWorkOrContributorName
  • Uversky, Vladimir N
  • Dunker, A. Keith
Series statement
Methods in molecular biology,
Series volume
896
http://library.link/vocab/subjectName
  • Proteins
  • Proteins
  • Proteins
Label
Intrinsically disordered protein analysis, Volume 2, Methods and experimental tools, edited by Vladimir N. Uversky, A. Keith Dunker
Instantiates
Publication
Antecedent source
unknown
Bibliography note
Includes bibliographical references and index
Color
multicolored
Contents
  • Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins
  • Javier Oroz [and others]
  • Sedimentation velocity analytical ultracentrifugation for intrinsically disordered proteins
  • Andres G. Salvay, Guillaume Communie, and Christine Ebel
  • Analysis of intrinsically disordered proteins by small-angle x-ray scattering
  • Pau Bernado and Dmitri I. Svergun
  • Small angle neutron scattering for the structural study of intrinsically disordered proteins in solution : a practical guide
  • Frank Gabel
  • Dynamic and static light scattering of intrinsically disordered proteins
  • Klaus Gast and Christian Fiedler
  • Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics
  • Estimation of intrinsically disordered protein shape and time-averaged apparent hydration in native conditions by a combination of hydrodynamic methods
  • Johanna C. Karst [and others]
  • Size-exclusion chromatography in structural analysis of intrinsically disordered proteins
  • Vladimir N. Uversky
  • Denaturant-induced conformational transitions in intrinsically disordered proteins
  • Paolo Neyroz, Stefano Ciurli, and Vladimir N. Uversky
  • Identification of intrinsically disordered proteins by a special 2D electrophoresis
  • Agnes Tantos and Peter Tompa
  • pH-induced changes in intrinsically disordered proteins
  • Matthew D. Smith and Masoud Jelokhani-Niaraki
  • Ucheor B. Choi, Keith R. Weninger, and Mark E. Bowen
  • Temperature-induced transitions in disordered proteins probed by NMR spectroscopy
  • Magnus Kjaergaard, Flemming M. Poulsen, and Birthe B. Kragelund
  • Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses
  • Magnus Kjaergaard, Flemming M. Poulsen, and Birthe B. Kragelund
  • Osmolyte-, binding-, and temperature-induced transitions of intrinsically disordered proteins
  • Allan Chris M. Ferreon and Ashok A. Deniz
  • Laser temperature-jump spectroscopy of intrinsically disordered proteins
  • Stephen J. Hagen ...
  • Differential scanning microcalorimetry of intrinsically disordered proteins
  • Sergei E. Permyakov
  • Application of confocal single-molecule FRET to intrinsically disordered proteins
  • Identifying disordered regions in proteins by limited proteolysis
  • Angelo Fontana [and others]
  • Effect of counter ions on the conformation of intrinsically disordered proteins studied by size-exclusion chromatography
  • Magdalena Wojtas [and others]
  • Mean net charge of intrinsically disordered proteins : experimental determination of protein valence by electrophoretic mobility measurements
  • Ana Cristina Sotomayor-Perez [and others]
  • Protein characterization by partitioning in aqueous two-phase systems
  • Larissa Mikheeva, Pedro Madeira, and Boris Zaslavsky
  • Detection and characterization of large-scale protein conformational transitions in solution using charge-state distribution analysis in ESI-MS
  • Rinat R. Abzalimov, Agya K. Frimpong, and Igor A. Kaltashov
  • Benjamin Schuler [and others]
  • Localizing flexible regions in proteins using hydrogen-deuterium exchange mass spectrometry
  • Cedric E. Bobst and Igor A. Kaltashov
  • Mass-spectrometry tools for analysis of intermolecular interactions
  • Jared R. Auclair [and others]
  • Characterization of oligomerization-aggregation products of neurodegenerative target proteins by ion mobility mass spectrometry
  • Camelia Vlad [and others]
  • Identifying solubility-promoting buffers for intrinsically disordered proteins prior to purification
  • Kelly A. Churion and Sarah E. Bondos
  • Proteomic methods for the identification of intrinsically disordered proteins
  • Agnes Tantos and Peter Tompa
  • Single-molecule force spectroscopy of chimeric polyprotein constructs containing intrinsically disordered domains
  • Selective isotope labeling of recombinant proteins in Escherichia coli
  • Kit I. Tong, Masayuki Yamamoto, and Toshiyuki Tanaka
  • Marco Brucale [and others]
  • Visualization of mobility by atomic force microscopy
  • Toshio Ando and Noriyuki Kodera
Control code
ocn801653449
Dimensions
unknown
Extent
1 online resource (xiv, 454 pages)
File format
unknown
Form of item
online
Isbn
9781461437048
Level of compression
unknown
Note
SpringerLink
Other control number
10.1007/978-1-4614-3704-8
Other physical details
illustrations (some color)
Quality assurance targets
not applicable
Reformatting quality
unknown
Sound
unknown sound
Specific material designation
remote
System control number
(OCoLC)801653449
Label
Intrinsically disordered protein analysis, Volume 2, Methods and experimental tools, edited by Vladimir N. Uversky, A. Keith Dunker
Publication
Antecedent source
unknown
Bibliography note
Includes bibliographical references and index
Color
multicolored
Contents
  • Unequivocal single-molecule force spectroscopy of intrinsically disordered proteins
  • Javier Oroz [and others]
  • Sedimentation velocity analytical ultracentrifugation for intrinsically disordered proteins
  • Andres G. Salvay, Guillaume Communie, and Christine Ebel
  • Analysis of intrinsically disordered proteins by small-angle x-ray scattering
  • Pau Bernado and Dmitri I. Svergun
  • Small angle neutron scattering for the structural study of intrinsically disordered proteins in solution : a practical guide
  • Frank Gabel
  • Dynamic and static light scattering of intrinsically disordered proteins
  • Klaus Gast and Christian Fiedler
  • Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics
  • Estimation of intrinsically disordered protein shape and time-averaged apparent hydration in native conditions by a combination of hydrodynamic methods
  • Johanna C. Karst [and others]
  • Size-exclusion chromatography in structural analysis of intrinsically disordered proteins
  • Vladimir N. Uversky
  • Denaturant-induced conformational transitions in intrinsically disordered proteins
  • Paolo Neyroz, Stefano Ciurli, and Vladimir N. Uversky
  • Identification of intrinsically disordered proteins by a special 2D electrophoresis
  • Agnes Tantos and Peter Tompa
  • pH-induced changes in intrinsically disordered proteins
  • Matthew D. Smith and Masoud Jelokhani-Niaraki
  • Ucheor B. Choi, Keith R. Weninger, and Mark E. Bowen
  • Temperature-induced transitions in disordered proteins probed by NMR spectroscopy
  • Magnus Kjaergaard, Flemming M. Poulsen, and Birthe B. Kragelund
  • Analyzing temperature-induced transitions in disordered proteins by NMR spectroscopy and secondary chemical shift analyses
  • Magnus Kjaergaard, Flemming M. Poulsen, and Birthe B. Kragelund
  • Osmolyte-, binding-, and temperature-induced transitions of intrinsically disordered proteins
  • Allan Chris M. Ferreon and Ashok A. Deniz
  • Laser temperature-jump spectroscopy of intrinsically disordered proteins
  • Stephen J. Hagen ...
  • Differential scanning microcalorimetry of intrinsically disordered proteins
  • Sergei E. Permyakov
  • Application of confocal single-molecule FRET to intrinsically disordered proteins
  • Identifying disordered regions in proteins by limited proteolysis
  • Angelo Fontana [and others]
  • Effect of counter ions on the conformation of intrinsically disordered proteins studied by size-exclusion chromatography
  • Magdalena Wojtas [and others]
  • Mean net charge of intrinsically disordered proteins : experimental determination of protein valence by electrophoretic mobility measurements
  • Ana Cristina Sotomayor-Perez [and others]
  • Protein characterization by partitioning in aqueous two-phase systems
  • Larissa Mikheeva, Pedro Madeira, and Boris Zaslavsky
  • Detection and characterization of large-scale protein conformational transitions in solution using charge-state distribution analysis in ESI-MS
  • Rinat R. Abzalimov, Agya K. Frimpong, and Igor A. Kaltashov
  • Benjamin Schuler [and others]
  • Localizing flexible regions in proteins using hydrogen-deuterium exchange mass spectrometry
  • Cedric E. Bobst and Igor A. Kaltashov
  • Mass-spectrometry tools for analysis of intermolecular interactions
  • Jared R. Auclair [and others]
  • Characterization of oligomerization-aggregation products of neurodegenerative target proteins by ion mobility mass spectrometry
  • Camelia Vlad [and others]
  • Identifying solubility-promoting buffers for intrinsically disordered proteins prior to purification
  • Kelly A. Churion and Sarah E. Bondos
  • Proteomic methods for the identification of intrinsically disordered proteins
  • Agnes Tantos and Peter Tompa
  • Single-molecule force spectroscopy of chimeric polyprotein constructs containing intrinsically disordered domains
  • Selective isotope labeling of recombinant proteins in Escherichia coli
  • Kit I. Tong, Masayuki Yamamoto, and Toshiyuki Tanaka
  • Marco Brucale [and others]
  • Visualization of mobility by atomic force microscopy
  • Toshio Ando and Noriyuki Kodera
Control code
ocn801653449
Dimensions
unknown
Extent
1 online resource (xiv, 454 pages)
File format
unknown
Form of item
online
Isbn
9781461437048
Level of compression
unknown
Note
SpringerLink
Other control number
10.1007/978-1-4614-3704-8
Other physical details
illustrations (some color)
Quality assurance targets
not applicable
Reformatting quality
unknown
Sound
unknown sound
Specific material designation
remote
System control number
(OCoLC)801653449

Library Locations

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