|
|
|
|
| LEADER |
00000cam a2200000Mi 4500 |
| 001 |
SCIDIR_ocn959428700 |
| 003 |
OCoLC |
| 005 |
20231120112132.0 |
| 006 |
m d |
| 007 |
cr ||||||||||| |
| 008 |
160912t20162016ne af o 001 0 eng d |
| 040 |
|
|
|a IDEBK
|b eng
|e rda
|c IDEBK
|d YDX
|d N$T
|d BUF
|d EBLCP
|d OPELS
|d CASUM
|d OCLCF
|d QCL
|d UPM
|d OCLCO
|d OCLCQ
|d OCLCA
|d NLE
|d ANS
|d OCLCO
|d AU@
|d OCLCA
|d SOI
|d OCLCQ
|d OCLCO
|d OCLCQ
|d OCLCA
|d OCLCO
|d OCLCQ
|
| 015 |
|
|
|a GBB7C1344
|2 bnb
|
| 019 |
|
|
|a 957557862
|a 957614433
|a 957680453
|a 957738339
|a 960214398
|a 1052108714
|a 1058368924
|
| 020 |
|
|
|a 0128054344
|q (ebk)
|
| 020 |
|
|
|a 9780128054345
|
| 020 |
|
|
|z 0128053801
|
| 020 |
|
|
|z 9780128053805
|
| 035 |
|
|
|a (OCoLC)959428700
|z (OCoLC)957557862
|z (OCoLC)957614433
|z (OCoLC)957680453
|z (OCoLC)957738339
|z (OCoLC)960214398
|z (OCoLC)1052108714
|z (OCoLC)1058368924
|
| 050 |
|
4 |
|a QP601
|
| 072 |
|
7 |
|a SCI
|x 007000
|2 bisacsh
|
| 082 |
0 |
4 |
|a 574.1925
|2 23
|
| 245 |
0 |
0 |
|a Methods in enzymology :
|b peptide, protein and enzyme design /
|c edited by Vincent L. Pecoraro, Department of Chemistry University of Michigan, Ann Arbor MI, United States.
|
| 264 |
|
1 |
|a Amsterdam, Netherlands :
|b Academic Press,
|c 2016.
|
| 264 |
|
4 |
|c �2016
|
| 300 |
|
|
|a 1 online resource (686 pages, 19 unnumbered pages of plates) :
|b illustrations.
|
| 336 |
|
|
|a text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a computer
|b c
|2 rdamedia
|
| 338 |
|
|
|a online resource
|b cr
|2 rdacarrier
|
| 347 |
|
|
|a data file
|2 rda
|
| 490 |
1 |
|
|a Methods in enzymology ;
|v volume 580
|
| 504 |
|
|
|a Includes bibliographical references and indexes.
|
| 505 |
0 |
|
|a Front Cover; Peptide, Protein and Enzyme Design; Copyright; Contents; Contributors; Preface; References; Chapter One: Chemical Posttranslational Modification with Designed Rhodium(II) Catalysts; 1. Introduction; 2. Synthesis of Rhodium(II) Conjugates as Protein Modification Catalysts; 2.1. Discussion; 2.2. Materials and General Considerations; 2.2.1. Preparation of Metalation Buffer; 2.3. Protocol 1: Preparation of Rh2(OAc)3(tfa)1; 2.4. Protocol 2: Preparation of Rhodium(II) Conjugates in Organic Solution; 2.4.1. Preparation of a Metalated FKBP Inhibitor (Coughlin et al., 2014).
|
| 505 |
8 |
|
|a 2.5. Protocol 3: Preparation of Rhodium(II) Conjugates in Aqueous Solution2.5.1. Preparation of the Metallopeptide S2ERh; 3. Modification of an SH3 Domain and Gel-Based Visualization Thereof; 3.1. Discussion; 3.2. Materials and General Considerations; 3.2.1. Preparation of 1X Transfer Buffer; 3.2.2. Preparation of Protein Modification Buffer; 3.2.3. Preparation of MALDI-MS Matrix; 3.3. Protocol 4: Rhodium(II)-Catalyzed Protein Modification; 3.3.1. Modification of SH3 Domain of Yes Kinase in Mammalian Cell Lysate (Vohidov, Coughlin, & Ball, 2015).
|
| 505 |
8 |
|
|a 3.4. Protocol 5: Visualization of an Alkyne-Tagged Protein by Chemical Blotting3.4.1. Fluorescent ``Chemical Blot�� Analysis of a Modified SH3 Domain; References; Chapter Two: Cell-Binding Assays for Determining the Affinity of Protein-Protein Interactions: Technologies and Considera ... ; 1. Introduction; 2. General Binding Theory and Relevance of Kd; 3. General Pitfalls in Cell-Based Binding Assays; 3.1. Time to Equilibrium; 3.2. Ligand Depletion; 4. Measuring Binding on the Surface of Yeast; 4.1. Materials; 4.1.1. Yeast Cells; 4.1.2. Solutions and Media; 4.1.3. Proteins/Antibodies.
|
| 505 |
8 |
|
|a 4.2. Method5. Measuring Binding on the Surface of Mammalian Cells; 5.1. Direct Binding; 5.2. Competition Binding; 6. Other Methods of Measuring Binding: Kinetic Exclusion Assay and Surface Plasmon Resonance; 6.1. Kinetic Exclusion Assay; 6.2. Surface Plasmon Resonance; 6.3. Comparison; 7. Summary; Acknowledgments; References; Chapter Three: Protein and Antibody Engineering by Phage Display; 1. Introduction; 2. Equipment; 3. Materials; 3.1. Cell Lines; 3.1.1. Protocol 1: Production of SS320 Cells (Modified from Tonikian, Zhang, Boone, & Sidhu, 2007).
|
| 505 |
8 |
|
|a 3.1.2. Protocol 2: Production of XL1-Blue Cells3.2. M13KO7 Helper Phage; 3.2.1. Protocol 3: Production of M13KO7 Helper Phage (Modified from Tonikian et al., 2007); 3.3. Phagemid Considerations; 3.4. Reagents; 3.4.1. Media; 3.4.2. Buffers (Filter Sterilize); 3.4.3. Solutions; 3.4.4. Antibiotics (Filter Sterilize); 3.4.5. Other Reagents; 4. Phage Display and Library Design; 4.1. Humanization of a Murine SUDV Antibody (Chen et al., 2014); 4.2. Mapping Hotspot Residues of Protein-Protein Interfaces (Frei et al., 2015; Stewart et al., 2013); 4.2.1. Protocol 4: Cloning into HP153.
|
| 650 |
|
0 |
|a Peptides.
|
| 650 |
|
0 |
|a Enzymes.
|
| 650 |
|
2 |
|a Peptides
|0 (DNLM)D010455
|
| 650 |
|
2 |
|a Enzymes
|0 (DNLM)D004798
|
| 650 |
|
6 |
|a Peptides.
|0 (CaQQLa)201-0006528
|
| 650 |
|
6 |
|a Enzymes.
|0 (CaQQLa)201-0002557
|
| 650 |
|
7 |
|a enzyme.
|2 aat
|0 (CStmoGRI)aat300212647
|
| 650 |
|
7 |
|a SCIENCE
|x Life Sciences
|x Biochemistry.
|2 bisacsh
|
| 650 |
|
7 |
|a Enzymes.
|2 fast
|0 (OCoLC)fst00913605
|
| 650 |
|
7 |
|a Peptides.
|2 fast
|0 (OCoLC)fst01057564
|
| 700 |
1 |
|
|a Pecoraro, Vincent L.,
|e editor.
|
| 776 |
0 |
8 |
|i Print version:
|t Peptide, protein and enzyme design.
|d Cambridge, MA : Academic Press, 2016
|z 9780128053805
|z 0128053801
|w (OCoLC)950449929
|
| 830 |
|
0 |
|a Methods in enzymology ;
|v v. 580.
|
| 856 |
4 |
0 |
|u https://sciencedirect.uam.elogim.com/science/bookseries/00766879/580
|z Texto completo
|
