The structural basis for how the large ribosomal subunit catalyses peptide bond formation

The structural basis for how the large ribosomal subunit catalyses peptide bond formation

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Bibliographic Details
Other Authors: Steitz, Thomas A. (Speaker)
Format: Electronic Video
Language:English
Published: London : Henry Stewart Talks, 2008.
Series:Henry Stewart talks. Biomedical & life sciences collection. Mechanisms of ribosome function : insights into protein synthesis.
Subjects:
Protein Biosynthesis.
Ribosomal Proteins.
Ribosomes.
Online Access:https://hstalks.com/bs/802/
Series
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028 5 0 |a 1622  |b Henry Stewart Talks 
035 |a (UkLoHST)802 
035 |a (UkLU-K)AC000392176 
040 |a UkLU-K  |b eng  |c UkLU-K 
100 1 |a Steitz, Thomas A.  |4 spk  |9 111991 
245 1 4 |a The structural basis for how the large ribosomal subunit catalyses peptide bond formation  |h [electronic resource] /  |c Thomas A. Steitz. 
260 |a London :  |b Henry Stewart Talks,  |c 2008. 
300 |a 1 online resource (1 streaming video file (42 min.) :  |b color, sound). 
490 1 |a The mechanisms of ribosome function : insights into protein synthesis,  |x 2056-452X 
500 |a Animated audio-visual presentation with synchronized narration. 
500 |a Title from title frames. 
505 0 |a Contents: Overview of protein synthesis by the ribosome -- Nature of the polypeptide exit tunnel in the large subunit -- The ribosome is a ribozyme -- Substrate induced fit at the peptidyl transferase center -- Proton shuttle mechanism and transition state stabilization -- Substrate interactions at the large subunit E-site -- Movie of the peptidyl transferase reaction. 
506 |a Access restricted to subscribers. 
538 |a Mode of access: World Wide Web. 
650 2 |a Protein Biosynthesis.  |9 111992 
650 2 |a Ribosomal Proteins.  |9 111993 
650 2 |a Ribosomes.  |9 111994 
830 0 |a Henry Stewart talks.  |p Biomedical & life sciences collection.  |p Mechanisms of ribosome function : insights into protein synthesis.  |9 111995 
856 4 0 |u https://hstalks.com/bs/802/ 
856 4 2 |u https://hstalks.com/bs/p/285/  |3 Series 
999 |c 216226  |d 216225 

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