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_a10.1007/978-981-15-5530-5 _2doi |
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_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC |
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| 050 | 4 |
_aQD431.25.A53 _b2020 EB |
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| 245 | 0 | 0 |
_aFrontiers in Protein Structure, Function, and Dynamics _cedited by Dev Bukhsh Singh, Timir Tripathi |
| 250 | _aFirst edition | ||
| 264 | 1 |
_aSingapore _bSpringer _c2020 |
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| 300 |
_a1 recurso en línea (XII, 452 páginas) _b71 ilustraciones, 54 ilustraciones a color |
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| 336 |
_2rdacontent _aTexto _btxt |
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_2rdamedia _aelectrónico _bc |
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| 338 |
_2rdacarrier _arecurso electrónico _bcr |
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| 347 |
_aArchivo de texto _bPDF |
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| 490 | 0 | _aBiomedical and Life Sciences (SpringerNature-11642) | |
| 490 | 0 | _aBiomedical and Life Sciences (R0) (SpringerNature-43708) | |
| 505 | 0 | _aChapter 1. Protein Purification, Estimation, Storage and Effect on Structure, Function and Dynamics -- Chapter 2. Experimental and Computational Methods to Determine Protein Structure and Stability -- Chapter 3. Wet-Lab Approaches to Determine Three-Dimensional Structures of Proteins -- Chapter 4. Use of Group Specific Reagents in Active Site Functional Group Elucidation I: Cys, Ser, Tyr and Trp Residues -- Chapter 5. Use of Group Specific Reagents in Active Site Functional Group Elucidation II: Asp, Glu, Arg, Lys and His residues -- Chapter 6. Protein-Protein Interactions Modeling: From Dry to Wet Lab -- Chapter 7. Thermodynamics of Protein-Ligand Binding -- Chapter 8. SynergisticEffects of Hydration Sites in Protein Stability: A Theoretical Water Thermodynamics Approach -- Chapter 9. Molecular Dynamics Simulation: Methods and Application -- Chapter 10. Protein Folding, Dynamics and Aggregation at Single Molecule Resolution -- Chapter 11. Protein Misfolding and Neurodegenerative Diseases -- Chapter 12. Management of Insulin Through Co-Solute Engineering: A Therapeutic Approach -- Chapter 13. Structural and Functional Aspects of Muscarinic Receptors in Correlation with Anticholinergic Drugs -- Chapter 14. Dopamine Β Hydroxylase: An Enzyme with Therapeutic Potential to Combat Neural and Cardiovascular Diseases -- Chapter 15. Molecular Motors: Subdomain Dynamics and Mechanochemistry -- Chapter 16. Structural and Functional Dynamics of Lysosomal Cysteine Proteases with Particular Reference to Cathepsin B and Cathepsin H -- Chapter 17. An Insight into the Importance of Ferritins in the Physiology of Mycobacterium tuberculosis: Unique Structural and Functional Properties. | |
| 520 | _aThis book discusses a broad range of basic and advanced topics in the field of protein structure, function, folding, flexibility, and dynamics. Starting with a basic introduction to protein purification, estimation, storage, and its effect on the protein structure, function, and dynamics, it also discusses various experimental and computational structure determination approaches; the importance of molecular interactions and water in protein stability, folding and dynamics; kinetic and thermodynamic parameters associated with protein-ligand binding; single molecule techniques and their applications in studying protein folding and aggregation; protein quality control; the role of amino acid sequence in protein aggregation; muscarinic acetylcholine receptors, antimuscarinic drugs, and their clinical significances. Further, the book explains the current understanding on the therapeutic importance of the enzyme dopamine beta hydroxylase; structural dynamics and motions in molecular motors; role of cathepsins in controlling degradation of extracellular matrix during disease states; and the important structure-function relationship of iron-binding proteins, ferritins. Overall, the book is an important guide and a comprehensive resource for understanding protein structure, function, dynamics, and interaction. | ||
| 988 | _aSpringer_Biomedlife_03082020 | ||
| 650 | 7 |
_2embne _aProteínas _xEstructura _9669891 |
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| 700 | 1 |
_aSingh, Dev Bukhsh _eeditor literario _4http://id.loc.gov/vocabulary/relators/edt _9675280 |
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| 700 | 1 |
_aTripathi, Timir _eeditor literario _4http://id.loc.gov/vocabulary/relators/edt _9675281 |
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| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-981-15-5530-5 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid) |
| 942 |
_2lcc _cLE |
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| 998 |
_b08/2020 _dz _ek _zSI |
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