Protein structure, stability, and interactions
By: edited by John W. Shriver.
Contributors: Shriver, John W.
Series: Springer protocols; Methods in molecular biology -- 490; Methods in molecular biology (Clifton, N.J.) -- v. 490.
Publisher: Humana
Published: 2009
Place of publication: New York, N.Y
Language: eng
Number of pages: 359
ISBN-13: 9781588299543; 9781597453677
Subjects: Proteins -- Structure -- Research -- Methodology; Proteins -- Structure-activity relationships -- Research -- Methodology; Proteins -- ultrastructure; Proteins -- analysis
Notes: Includes bibliographical references and index.
Table of contents: title: Microcalorimetry of proteins and their complexes / Peter L. Privalov; title: Determining the conformational stability of a protein using urea denaturation curves / Kevin L. Shaw ... [et al.]; title: Defining the stability of multimeric proteins / John W. Shriver and Stephen P. Edmondson; title: Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation / Walter F. Stafford, III; title: Monitoring molecular interactions by NMR / James M. Lipchock and J. Patrick Loria; title: Ligand-binding interactions and stability / John W. Shriver and Stephen P. Edmondson; title: A method for direct measurement of protein stability in vivo / Zoya Ignatova and Lila M. Gierasch; title: 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.; title: Molecular crowding and solvation : direct and indirect impact on protein reactions / Jörg Rösgen; title: Defining the role of salt bridges in protein stability / Ilian Jelesarov and Andrey Karshikoff; title: Protein stabilization by the rational design of surface charge-charge interactions / Katerina L. Schweiker and George I. Makhatadze; title: NMR analysis of native-state protein conformational flexibility by hydrogen exchange / Griselda Hernández and David M. LeMaster; title: Single-molecule fluorescence studies of protein folding / G. Ulrich Nienhaus; title: Experimental characterization of the denatured state ensemble of proteins / Jae-Hyun Cho and Daniel P. Raleigh.