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| 008 | 100301s2006 xxu| o |||| 0|eng d | ||
| 020 | _a9781597451895 | ||
| 024 | 7 |
_a10.1385/1597451894 _2doi |
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_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC |
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| 050 | 4 |
_aQP551 _b2006 EB |
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| 245 | 0 | 0 |
_aProtein Folding Protocols _cedited by Yawen Bai |
| 250 | _a1st edition 2006 | ||
| 264 | 1 |
_aTotowa, NJ _bHumana Press _c2006 |
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| 300 |
_a1 recurso en línea (XIV, 328 páginas) _b111 ilustraciones |
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| 336 |
_atexto _btxt _2rdacontent |
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| 337 |
_aelectrónico _bc _2rdamedia |
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| 338 |
_arecurso electrónico _bcr _2rdacarrier |
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| 347 |
_aarchivo de texto _bPDF |
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| 490 | 0 |
_aMethods in Molecular Biology _x1940-6029 _v350 |
|
| 505 | 0 | _aInfrared Temperature-Jump Study of the Folding Dynamics of ?-Helices and ?-Hairpins -- The Use of High-Pressure Nuclear Magnetic Resonance to Study Protein Folding -- Characterization of Denatured Proteins Using Residual Dipolar Couplings -- Characterizing Residual Structure in Disordered Protein States Using Nuclear Magnetic Resonance -- Population and Structure Determination of Hidden Folding Intermediates by Native-State Hydrogen Exchange-Directed Protein Engineering and Nuclear Magnetic Resonance -- Characterizing Protein Folding Transition States Using ?-Analysis -- Advances in the Analysis of Conformational Transitions in Peptides Using Differential Scanning Calorimetry -- Application of Single Molecule Förster Resonance Energy Transfer to Protein Folding -- Single Molecule Studies of Protein Folding Using Atomic Force Microscopy -- Using Triplet-Triplet Energy Transfer to Measure Conformational Dynamics in Polypeptide Chains -- A Hierarchical Protein Folding Scheme Based on the Building Block Folding Model -- Replica Exchange Molecular Dynamics Method for Protein Folding Simulation -- Estimation of Folding Probabilities and ? Values From Molecular Dynamics Simulations of Reversible Peptide Folding -- Packing Regularities in Biological Structures Relate to Their Dynamics -- Intermediates and Transition States in Protein Folding -- Thinking the Impossible. | |
| 520 | _aProtein Folding Protocols presents protocols for studying and characterizing protein folding from the unfolded to the folded state. Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. Protein Folding Protocols also provides sample approaches toward the prediction of protein structure starting from the amino acid sequence, in the absence of overall homologous sequences. These approaches have tremendous implications, ranging from drug design, functional assignment, comprehension of the nature of regulation, understanding molecular machines, viral entry into cells, and putting together cellular pathways and their dynamics. | ||
| 988 | _aSpringer_Protocols_2006 | ||
| 650 | 7 |
_2embne _9139861 _aProteínas _vManuales de laboratorio |
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| 776 | 0 | 8 |
_iPrinted edition: _z9781617376764 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781588296221 |
| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1597451894 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid) |
| 942 |
_2lcc _cLE |
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| 998 |
_b12/2023 _dz _eu _zSI |
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