| 000 | 03536nam a22003975i 4500 | ||
|---|---|---|---|
| 999 |
_c393476 _d393476 _x1 |
||
| 001 | 393476 | ||
| 003 | ES-MaUEC | ||
| 005 | 20240429180312.0 | ||
| 006 | a||||fo|||| 00| 0 | ||
| 007 | cr nn 008mamaa | ||
| 008 | 130923s2014 xxu| fo |||| 0|eng d | ||
| 020 | _a9781627036580 | ||
| 024 | 7 |
_a10.1007/978-1-62703-658-0 _2doi |
|
| 040 |
_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC |
||
| 050 | 4 |
_aQP551 _b2014 EB |
|
| 245 | 0 | 0 |
_aProtein Dynamics : _bMethods and Protocols _cedited by Dennis R. Livesay |
| 250 | _a1st edition 2014 | ||
| 264 | 1 |
_aTotowa, NJ _bHumana Press _c2014 |
|
| 300 |
_a1 recurso en línea (XIV, 285 páginas) _b82 ilustraciones, 56 ilustraciones a color |
||
| 336 |
_atexto _btxt _2rdacontent |
||
| 337 |
_aelectrónico _bc _2rdamedia |
||
| 338 |
_arecurso electrónico _bcr _2rdacarrier |
||
| 347 |
_aarchivo de texto _bPDF |
||
| 490 | 0 |
_aMethods in Molecular Biology _x1940-6029 _v1084 |
|
| 505 | 0 | _aMonitoring Side-Chain Dynamics of Proteins Using 2H Relaxation -- CPMG Relaxation Dispersion -- Confocal Single-Molecule FRET for Protein Conformational Dynamics -- Protein Structural Dynamics Revealed by Site-directed Spin Labeling and Multifrequency EPR -- Probing Backbone Dynamics With Hydrogen/Deuterium Exchange Mass Spectrometry -- Carbon-Deuterium Bonds as Non-perturbative Infrared Probes of Protein Dynamics, Electrostatics, Heterogeneity, and Folding -- Balancing Bond, Nonbond and Gō-like Terms in Coarse Grain Simulations of Conformational Dynamics -- Tutorial on Building Markov State Models with MSMBuilder and Coarse-graining them with BACE -- Analysis of Protein Conformational Transitions Using Elastic Network Model -- Geometric Simulation of Flexible Motion in Proteins -- Principal Component Analysis: A Method for Determining the Essential Dynamics of Proteins -- A Case Study Comparing Quantitative Stability/Flexibility Relationships Across Five Metallo-β-Lactamases Highlighting Differences within NDM-1 -- Towards Comprehensive Analysis of Protein Family Quantitative Stability/Flexibility Relationships using Homology Models -- Using the COREX/BEST Server to Model the Native State Ensemble -- Morphing Methods to Visualize Coarse-grained Protein Dynamics. | |
| 520 | _aIn Protein Dynamics: Methods and Protocols, expert researchers in the field detail both experimental and computational methods to interrogate molecular level fluctuations. Chapters detail best-practice recipes covering both experimental and computational techniques, reflecting modern protein research. Written in the highly successful Methods in Molecular Biology™ series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Protein Dynamics: Methods and Protocols describes the most common and powerful methods used to characterize protein dynamics. . | ||
| 988 | _aSpringer_Protocols_2014 | ||
| 650 | 7 |
_2embne _9242917 _aProteínas _xAnálisis |
|
| 776 | 0 | 8 |
_iPrinted edition: _z9781627036597 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781627036573 |
| 776 | 0 | 8 |
_iPrinted edition: _z9781493963072 |
| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-1-62703-658-0 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid) |
| 942 |
_2lcc _cLE |
||
| 998 |
_b02/2024 _dz _ean _zSI |
||