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- Introduction
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1. From DNA to proteins: the multiple levels of regulation
- Prof. Panagiotis Tsonis
- Chromatin and DNA
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2. Chromatin architecture and alterations in the control of gene regulation
- Prof. Jeffrey Hansen
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3. Nucleosome dynamics and remodeling
- Prof. Jonathan Widom
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4. DNA replication
- Prof. Smita Patel
- Transcription
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6. Mechanisms of transcription: the eukaryotic pre-initiation complex
- Prof. Michael Hampsey
- RNA (I)
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7. Pre-mRNA splicing
- Prof. Timothy Nilsen
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8. Self-splicing intron RNAs: ribozymes, parasites and agents of genomic change
- Prof. Anna Marie Pyle
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10. mRNA capping
- Prof. Aaron Shatkin
- RNA (II)
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13. RNA editing: changing the code in plants, animals and parasites
- Prof. Stephen Hajduk
- Proteins
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14. The principle of translation
- Prof. Joachim Frank
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15. Translation initiation
- Prof. Patrick Linder
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16. Elongation of protein synthesis: structural basis of the process of decoding
- Prof. Marina Rodnina
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17. Elongation of protein synthesis: structural basis of the peptide bond
- Prof. Marina Rodnina
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18. How do proteins fold and why?
- Prof. Walter Englander
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19. Protein degradation
- Prof. Alfred Goldberg
- Understanding Global Gene Expression
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21. Comparing transcriptomes of distant organisms: models of gene expression 2
- Prof. Mark Gerstein
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22. Protein networks and analysis of global gene expression
- Dr. Trey Ideker
- Archived Lectures *These may not cover the latest advances in the field
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23. Chromatin and transcription
- Prof. Roger Kornberg
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24. Nuclear organization and gene expression
- Prof. David Spector
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25. Gene and protein microarrays: tools for gene discovery and function
- Prof. Craig R. Tomlinson
Printable Handouts
Navigable Slide Index
- Introduction
- 70S Ribosome (5.5 angstrom)
- Chemistry of the peptide bond formation
- Peptide bond formation is catalyzed by RNA
- Proteins within 30 angstrom of the PTC
- tRNA binding in the PTC
- C-Pmn as model substrate for binding at the A-site
- CC-Pmn as substrate for binding at the A-site
- Conformational changes folowing substrate binding
- Water exclusion keeps peptidyl-tRNA uninduced
- The 50S subunit with the transition state analogs
- Potential strategies of catalysis
- Enthalpic or entropic catalysis
- Studying the mechanism of peptide bond formation
- Characteristics of uncatalyzed reaction
- Reaction pathway on the 50S subunit
- Measuring kinetics of peptide bond formation
- pH dependence of reaction with Pmn
- Contribution of pH-dependent catalysis
- Aminoacyl-tRNA as A-site substrate
- Reaction with full-size substrate
- Entropic effects in ribosome catalysis
- Role of active-site residues: A2451
- Conservation of peptidyl transferase mechanism
- pH-dependent changes in ribosome structure
- Mutations of inner shell residues
- Replacement of 2' OH of A76 of the P-site tRNA
- Roles of 2' OH of A76 of the P-site tRNA
- Conclusions
- Literature
Topics Covered
- The ribosome
- Chemistry of peptide bond formation
- Structure of the peptidyl transferase center of the ribosome
- Structures of the catalytic subunit with reaction substrates and transition state analogs
- Induced fit in peptide bond formation and peptidyl-tRNA hydrolysis
- Reaction pathways of catalyzed and uncatalyzed reactions
- pH dependence of catalysis
- Entropic catalysis
- Role of active site residues
- Importance of 2' OH of A76 of the tRNA in the P site
- The mechanism of peptide bond formation
Talk Citation
Rodnina, M. (2007, October 1). Elongation of protein synthesis: structural basis of the peptide bond [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved March 30, 2025, from https://doi.org/10.69645/BSDW2080.Export Citation (RIS)
Publication History
- Published on October 1, 2007
Financial Disclosures
- Prof. Marina Rodnina has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Elongation of protein synthesis: structural basis of the peptide bond
Published on October 1, 2007
40 min
A selection of talks on Biochemistry
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