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Protein structure, stability, and interactions
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Protein structure, stability, and interactions

Author: John W Shriver
Publisher: New York, N.Y. : Humana, ©2009.
Series: Springer protocols.; Methods in molecular biology (Clifton, N.J.), v. 490.
Edition/Format:   Book : EnglishView all editions and formats
Summary:

Supporting and up-dating previous volumes, this text focuses on theory and practical applications for both established methods and new procedures. The volume presents an overview of many techniques  Read more...

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Genre/Form: Aufsatzsammlung
Material Type: Internet resource
Document Type: Book, Internet Resource
All Authors / Contributors: John W Shriver
ISBN: 9781588299543 1588299546 9781597453677 1597453676
OCLC Number: 236120178
Description: x, 359 p. : ill. ; 27 cm.
Contents: Microcalorimetry of proteins and their complexes / Peter L. Privalov --
Determining the conformational stability of a protein using urea denaturation curves / Kevin L. Shaw ... [et al.] --
Defining the stability of multimeric proteins / John W. Shriver and Stephen P. Edmondson --
Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation / Walter F. Stafford, III --
Monitoring molecular interactions by NMR / James M. Lipchock and J. Patrick Loria --
Ligand-binding interactions and stability / John W. Shriver and Stephen P. Edmondson --
A method for direct measurement of protein stability in vivo / Zoya Ignatova and Lila M. Gierasch --
Quantifying the roles of water and solutes (denaturants, osmolytes, and Hofmeister salts) in protein and model processes using the solute partitioning mode / Laurel M. Pegram and M. Thomas Record, Jr. --
Molecular crowding and solvation : direct and indirect impact on protein reactions / Jörg Rösgen --
Defining the role of salt bridges in protein stability / Ilian Jelesarov and Andrey Karshikoff --
Protein stabilization by the rational design of surface charge-charge interactions / Katerina L. Schweiker and George I. Makhatadze --
NMR analysis of native-state protein conformational flexibility by hydrogen exchange / Griselda Hernández and David M. LeMaster --
Single-molecule fluorescence studies of protein folding / G. Ulrich Nienhaus --
Experimental characterization of the denatured state ensemble of proteins / Jae-Hyun Cho and Daniel P. Raleigh.
Series Title: Springer protocols.; Methods in molecular biology (Clifton, N.J.), v. 490.
Responsibility: edited by John W. Shriver.
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From the reviews: "Protein Structure, Stability, and Interactions covers a thorough list of biophysical methods as applied to proteins and their environments in vivo, in vitro, and sometimes in Read more...

 
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