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Protein structure, stability, and interactions

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Bibliographic Details
Group Author: Shriver John W.
Published: Humana Springer, distributor],
Publisher Address: New York, N.Y. [London
Publication Dates: c2009.
Literature type: Book
Language: English
Series: Methods in molecular biology ; 490
Subjects:
Proteins > Structure-activity relationships > Research > Methodology.
Proteins > ultrastructure
Proteins > Analysis.
Proteins > Structure > Research > Methodology.
Carrier Form: x, 359 p.: ill. ; 27 cm.
ISBN: 9781588299543 (hbk.)
1588299546 (hbk.)
9781597453677 (ebk.)
1597453676 (ebk.)
Index Number: Q510
CLC: Q510.1
Call Number: Q510.1/P967-4
Contents: Includes bibliographical references and index.
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.

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