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02135nam a22003255i 4500 |
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978-1-59745-367-7 |
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20191026222747.0 |
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cr nn 008mamaa |
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110414s2009 xxu| s |||| 0|eng d |
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|a 9781597453677
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7 |
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|a 10.1007/978-1-59745-367-7
|2 doi
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| 040 |
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|a Sistema de Bibliotecas del Tecnológico de Costa Rica
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| 245 |
1 |
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|a Protein Structure, Stability, and Interactions
|c edited by John W. Shriver.
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| 250 |
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|a 1st ed. 2009.
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| 260 |
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|a Totowa, NJ :
|b Humana Press :
|b Imprint: Humana,
|c 2009.
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| 300 |
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|a X, 360 p. 135 illus.
|b online resource.
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| 336 |
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|a text
|b txt
|2 rdacontent
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| 337 |
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|a computer
|b c
|2 rdamedia
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| 338 |
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|a online resource
|b cr
|2 rdacarrier
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| 490 |
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|a Methods in Molecular Biology,
|v 490
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| 505 |
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|a Microcalorimetry of Proteins and Their Complexes -- Determining the Conformational Stability of a Protein Using Urea Denaturation Curves -- Defining the Stability of Multimeric Proteins -- Protein–Protein and Ligand–Protein Interactions Studied by Analytical Ultracentrifugation -- Monitoring Molecular Interactions by NMR -- Ligand-Binding Interactions and Stability -- A Method for Direct Measurement of Protein Stability In Vivo -- Quantifying the Roles of Water and Solutes (Denaturants, Osmolytes, and Hofmeister Salts) in Protein and Model Processes Using the Solute Partitioning Model -- Molecular Crowding and Solvation: Direct and Indirect Impact on Protein Reactions -- Defining the Role of Salt Bridges in Protein Stability -- Protein Stabilization by the Rational Design of Surface Charge–Charge Interactions -- NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange -- Single-Molecule Fluorescence Studies of Protein Folding -- Experimental Characterization of the Denatured State Ensemble of Proteins.
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| 650 |
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|a Proteins .
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| 650 |
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|a Cell biology.
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| 650 |
1 |
4 |
|a Protein Science.
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| 650 |
2 |
4 |
|a Protein Structure.
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| 650 |
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4 |
|a Cell Biology.
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| 700 |
1 |
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|a Shriver, John W.
|e editor.
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| 710 |
2 |
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|a SpringerLink (Online service)
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| 773 |
0 |
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|t Springer eBooks
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| 856 |
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|u https://doi.org/10.1007/978-1-59745-367-7
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