The Resource Misbehaving Proteins : Protein (Mis)Folding, Aggregation, and Stability, edited by Regina Murphy, Amos Tsai, (electronic resource)

Misbehaving Proteins : Protein (Mis)Folding, Aggregation, and Stability, edited by Regina Murphy, Amos Tsai, (electronic resource)

Label
Misbehaving Proteins : Protein (Mis)Folding, Aggregation, and Stability
Title
Misbehaving Proteins
Title remainder
Protein (Mis)Folding, Aggregation, and Stability
Statement of responsibility
edited by Regina Murphy, Amos Tsai
Contributor
Editor
Editor
Subject
Language
  • eng
  • eng
Summary
Misfoldedaggregatedproteinoncewasconsideredasinterestingasyesterday’strash—a bothersome by-product of important and productive activities, to be disposed of and forgotten as quickly as possible. Yesterday’s trash has become today’s focus of cons- erable scienti?c interest for at least two reasons: (1) protein aggregates are at the core of a number of chronic degenerative diseases such as Alzheimer’s disease, and (2) - gregation poses signi?cant obstacles to the manufacture of safe, ef?cacious, and stable protein products. As interest in protein misfolding, aggregation, and stability has soared beyond the core group of traditional protein-folding scientists, and as substantial scienti?c progress in understanding and controlling protein misfolding has been achieved, the need to summarize the state of the art became manifest. Although there are many excellent texts and edited collections on protein structure and folding, these volumes tend to relegate protein misfolding and aggregation to a minor role. Review articles and books focused on the biological role of protein aggregates in diseases have been published recently. Misbehaving Proteins: Protein (Mis)folding, Aggregation, and Stability differs from theseotherrecenteffortsinitsemphasisonfundamentalcomputationalandexperimental studies and in its linkage of disparate consequences of protein misfolding (e.g., from clinical manifestations to manufacturing headaches) to their common causes
Dewey number
  • 572.633
  • 572/.633
http://bibfra.me/vocab/relation/httpidlocgovvocabularyrelatorsedt
  • W7MpVEnFQgg
  • ukUq5wQFj4c
Language note
English
LC call number
QD431-431.7
Literary form
non fiction
Nature of contents
dictionaries
http://library.link/vocab/relatedWorkOrContributorName
  • Murphy, Regina.
  • Tsai, Amos.
http://library.link/vocab/subjectName
  • Proteomics
  • Biochemistry
  • Biochemical engineering
  • Biotechnology
  • Analytical biochemistry
  • Proteomics
  • Biochemistry, general
  • Biochemical Engineering
  • Biotechnology
  • Analytical Chemistry
Label
Misbehaving Proteins : Protein (Mis)Folding, Aggregation, and Stability, edited by Regina Murphy, Amos Tsai, (electronic resource)
Instantiates
Publication
Note
Description based upon print version of record
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
  • cr
Content category
text
Content type code
  • txt
Contents
Protein Folding, Misfolding, Stability, and Aggregation -- Mathematical Models and Computational Methods -- Nonnative Protein Aggregation -- Simulations of Protein Aggregation -- Experimental Methods -- Elucidating Structure, Stability, and Conformational Distributions during Protein Aggregation with Hydrogen Exchange and Mass Spectrometry -- Application of Spectroscopic and Calorimetric Techniques in Protein Formulation Development -- Small-Angle Neutron Scattering as a Probe for Protein Aggregation at Many Length Scales -- Laser Light Scattering as an Indispensable Tool for Probing Protein Aggregation -- X-ray Diffraction for Characterizing Structure in Protein Aggregates -- Glass Dynamics and the Preservation of Proteins -- Fundamental Studies in Model Systems -- Folding and Misfolding as a Function of Polypeptide Chain Elongation -- Determinants of Protein Folding and Aggregation in P22 Tailspike Protein -- Factors Affecting the Fibrillation of ?-Synuclein, a Natively Unfolded Protein -- Molten Globule-Lipid Bilayer Interactions and Their Implications for Protein Transport and Aggregation -- Protein Product Development -- Self-Association of Therapeutic Proteins -- Mutational Approach to Improve Physical Stability of Protein Therapeutics Susceptible to Aggregation
Dimensions
unknown
Edition
1st ed. 2006.
Extent
1 online resource (360 p.)
Form of item
online
Isbn
9780387360638
Media category
computer
Media type code
  • c
Other control number
10.1007/978-0-387-36063-8
Specific material designation
remote
System control number
  • (CKB)1000000000284659
  • (EBL)324077
  • (OCoLC)209918936
  • (SSID)ssj0000771999
  • (PQKBManifestationID)12344480
  • (PQKBTitleCode)TC0000771999
  • (PQKBWorkID)10829041
  • (PQKB)10301333
  • (SSID)ssj0000203468
  • (PQKBManifestationID)11190198
  • (PQKBTitleCode)TC0000203468
  • (PQKBWorkID)10259263
  • (PQKB)10910792
  • (DE-He213)978-0-387-36063-8
  • (MiAaPQ)EBC324077
  • (EXLCZ)991000000000284659
Label
Misbehaving Proteins : Protein (Mis)Folding, Aggregation, and Stability, edited by Regina Murphy, Amos Tsai, (electronic resource)
Publication
Note
Description based upon print version of record
Bibliography note
Includes bibliographical references and index
Carrier category
online resource
Carrier category code
  • cr
Content category
text
Content type code
  • txt
Contents
Protein Folding, Misfolding, Stability, and Aggregation -- Mathematical Models and Computational Methods -- Nonnative Protein Aggregation -- Simulations of Protein Aggregation -- Experimental Methods -- Elucidating Structure, Stability, and Conformational Distributions during Protein Aggregation with Hydrogen Exchange and Mass Spectrometry -- Application of Spectroscopic and Calorimetric Techniques in Protein Formulation Development -- Small-Angle Neutron Scattering as a Probe for Protein Aggregation at Many Length Scales -- Laser Light Scattering as an Indispensable Tool for Probing Protein Aggregation -- X-ray Diffraction for Characterizing Structure in Protein Aggregates -- Glass Dynamics and the Preservation of Proteins -- Fundamental Studies in Model Systems -- Folding and Misfolding as a Function of Polypeptide Chain Elongation -- Determinants of Protein Folding and Aggregation in P22 Tailspike Protein -- Factors Affecting the Fibrillation of ?-Synuclein, a Natively Unfolded Protein -- Molten Globule-Lipid Bilayer Interactions and Their Implications for Protein Transport and Aggregation -- Protein Product Development -- Self-Association of Therapeutic Proteins -- Mutational Approach to Improve Physical Stability of Protein Therapeutics Susceptible to Aggregation
Dimensions
unknown
Edition
1st ed. 2006.
Extent
1 online resource (360 p.)
Form of item
online
Isbn
9780387360638
Media category
computer
Media type code
  • c
Other control number
10.1007/978-0-387-36063-8
Specific material designation
remote
System control number
  • (CKB)1000000000284659
  • (EBL)324077
  • (OCoLC)209918936
  • (SSID)ssj0000771999
  • (PQKBManifestationID)12344480
  • (PQKBTitleCode)TC0000771999
  • (PQKBWorkID)10829041
  • (PQKB)10301333
  • (SSID)ssj0000203468
  • (PQKBManifestationID)11190198
  • (PQKBTitleCode)TC0000203468
  • (PQKBWorkID)10259263
  • (PQKB)10910792
  • (DE-He213)978-0-387-36063-8
  • (MiAaPQ)EBC324077
  • (EXLCZ)991000000000284659

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