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Total Chemical Synthesis of Proteins.
- Format:
- Book
- Language:
- English
- Subjects (All):
- Proteins--Synthesis.
- Proteins.
- Physical Description:
- 1 online resource (627 pages)
- polychrome
- Place of Publication:
- Newark : John Wiley & Sons, Incorporated, 2021.
- System Details:
- text file
- Contents:
- Cover
- Title Page
- Copyright
- Contents
- Preface
- Chapter 1 Characterization of Protein Molecules Prepared by Total Chemical Synthesis
- 1.1 Introduction
- 1.2 Chemical Protein Synthesis
- 1.3 Comments on Characterization of Synthetic Protein Molecules
- 1.3.1 Homogeneity
- 1.3.2 Amino Acid Sequence
- 1.3.3 Chemical Analogues
- 1.3.4 Limitations of SPPS
- 1.3.5 Folding as a Purification Step
- 1.4 Summary
- References
- Chapter 2 Automated Fast Flow Peptide Synthesis
- 2.1 Introduction
- 2.2 Results
- 2.2.1 Summary
- 2.2.1.1 Mechanical Principles
- 2.2.1.2 Chemical Principles
- 2.2.1.3 User Interface Principles
- 2.2.1.4 Data Analysis Method
- 2.2.1.5 Outcome
- 2.2.2 First-generation Automated Fast Flow Peptide Synthesis
- 2.2.2.1 Key Findings
- 2.2.2.2 Design of First-generation AFPS
- 2.2.2.3 Characterization of First-generation AFPS
- 2.2.3 Second-generation Automated Fast Flow Peptide Synthesis
- 2.2.3.1 Key Findings
- 2.2.3.2 Design of Second-generation AFPS
- 2.2.3.3 Characterization and Use of Second-generation AFPS
- 2.2.4 Third-generation Automated Fast Flow Peptide Synthesis
- 2.2.4.1 Key Findings
- 2.2.4.2 Design of Third-generation AFPS
- 2.2.4.3 Characterization of Third-generation AFPS
- 2.2.4.4 Reagent Stability Study
- 2.2.5 Fourth-generation Automated Fast Flow Peptide Synthesis
- 2.2.5.1 Key Findings
- 2.2.5.2 Effect of Solvent on Fast Flow Synthesis
- 2.2.5.3 Design and Characterization of Fourth-generation AFPS
- 2.3 Conclusions
- Acknowledgments
- Chapter 3 N, S- and N, Se-Acyl Transfer Devices in Protein Synthesis
- 3.1 Introduction
- 3.2 N, S- and N, Se-Acyl Transfer Devices: General Presentation, Reactivity and Statistical Overview of Their Utilization
- 3.2.1 General Presentation of N, S- and N, Se-Acyl Transfer Devices
- 3.2.2 Relative Reactivity of N, S- and N, Se-Acyl Transfer Devices
- 3.2.3 A Statistical Overview of the Synthetic Use of N, S- and N, Se-Acyl Transfer Devices for Protein Total Chemical Synthesis
- 3.3 Preparation of SEA/SeEAoff and SEAlide Peptides
- 3.3.1 Preparation of SEA and SeEA Peptides
- 3.3.2 Preparation of SEAlide Peptides
- 3.4 Redox-controlled Assembly of Biotinylated NK1 Domain of the Hepatocyte Growth Factor (HGF) Using SEA and SeEA Chemistries
- 3.5 The Total Chemical Synthesis of GM2-AP Using SEAlide-based Chemistry
- 3.6 Conclusion
- Chapter 4 Chemical Synthesis of Proteins Through Native Chemical Ligation of Peptide Hydrazides
- 4.1 Introduction
- 4.2 Development of Peptide Hydrazide-based Native Chemical Ligation
- 4.2.1 Conversion of Peptide Hydrazide to Peptide Azide
- 4.2.2 Acyl Azide-based Solid-phase Peptide Synthesis
- 4.2.3 Acyl Azide-based Solution-phase Peptide Synthesis
- 4.2.4 The Transesterification of Acyl Azide
- 4.2.5 Development of Peptide Hydrazide-based Native Chemical Ligation
- Notes:
- Electronic reproduction. Hoboken, N.J. Available via World Wide Web.
- Print version record.
- 4.3 Optimization of Peptide Hydrazide-based Native Chemical Ligation.
- Local Notes:
- Acquired for the Penn Libraries with assistance from the Alumni and Friends Memorial Book Fund.
- Other Format:
- Print version: Brik, Ashraf. Total Chemical Synthesis of Proteins.
- ISBN:
- 9783527823567
- 3527823565
- 9783527823574
- 3527823573
- Publisher Number:
- 99990865716
- Access Restriction:
- Restricted for use by site license.
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