Chapter 1 creation (pages 1–3): F.M. Richards
Chapter 2 The position of Mobility within the Substrate Binding and Catalytic equipment of Enzymes (pages 4–24): Tom Alberi, William A. Gilbert, Dagmar Ringe Ponzi and Gregory A. Petsko
Chapter three Ligand?Induced Conformational adjustments in Proteins (pages 25–46): T. A. Steitz, R. Harrison, I. T. Weber and M. Leahy
Chapter four Mobility and Active?Site Coupling in 2?Oxo Acid Dehydrogenase Complexes (pages 47–71): Gordon C. okay. Roberts, Harry W. Duckworth, Leonard C. Packman and Richard N. Perham
Chapter five The Mobility of Calcium?Trigger Proteins and Its functionality (pages 72–97): B. A. Levine, D. C. Dalgarno, M. P. Esnouf, R. E. Klevit, G. M. M. Scott and R. J. P. Williams
Chapter 6 Mobility and serve as in Elastin and Collagen (pages 98–115): D. A. Torchia, L. S. Batchelder, W. W. Fleming, L. W. Jelinski, S. ok. Sarkar and C. E. Sullivan
Chapter 7 Flexibility in Tobacco Mosaic Virus (pages 116–138): okay. C. Holmes
Chapter eight The Molecular foundation of Muscle Contraction (pages 139–155): ok. C. Holmes and R. S. Goody
Chapter nine Actin?Induced alterations within the Dynamics of Myosin Subfragment?1 Detected by means of Nuclear Magnetic Resonance (pages 156–168): Stefan Highsmith and Oleg Jardetzky
Chapter 10 Rotational Dynamics of Spin?Labelled Muscle Proteins (pages 169–185): David D. Thomas
Chapter eleven Cross?Bridge flow in Muscle and the Conformation of the Myosin Hinge (pages 186–207): William F. Harrington, Hitoshi Ueno and Tian Yow Tsong
Chapter 12 Nuclear Magnetic Resonance reviews on constitution and respiring Dynamics of move RNA (pages 208–225): Brian R. Reid and Dennis R. Hare
Chapter thirteen Triplet Anisotropy Decay Measurements of DNA inner movement (pages 226–245): Michael Hogan, Johnny Wang and R. H. Austin
Chapter 14 Conformations and Flexibilities of Histones and excessive Mobility staff (HMG) Proteins in Chromatin constitution and serve as (pages 246–270): E. Morton Bradbury
Chapter 15 neighborhood and Collective Motions in Protein Dynamics (pages 273–290): M. Karplus, S. Swaminathan, T. Ichiyjz and W. F. Van Gunsteren
Chapter sixteen Soliton thought of Protein Dynamics (pages 291–309): Oleg Jardetzky and Roy King
Chapter 17 Nuclear Magnetic Resonance reports of Mobility in Proteins (pages 310–328): Kurt Wuthrich and Gerhard Wagner
Chapter 18 precis and Outlook (pages 329–343): Hans Frauenfelder
Chapter 19 remaining feedback (pages 344–345): F.M. Richards
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Extra info for Ciba Foundation Symposium 93 - Mobility and Function in Proteins and Nucleic Acids
1982 Mobilig and function in proteins and nucleic acids. Pihnan, London (Ciba Foundation symposium 93) p 47-71 47 48 ROBERTS ET AL enzymes which, as shown in Fig. 1, catalyse successive steps in the overall reaction. FIG. 1 . The reaction mechanism of the 2-0x0 acid dehydrogenase multienzyme complexes. The three component enzymes E l , E2 and E3 are identified in the text.
Some other examples of this kind of conformational change are provided by lactate dehydrogenase (White et a1 1976) and phosphorylase (Madsen et a1 1978). (2) Polypeptide chain end. Ligand binding can dramatically change the conformation of one or the other end of the polypeptide chain of either the subunit to which the ligand is binding or, in some cases, another subunit of an oligomeric protein. It is sometimes the case that the polypeptide is disordered-that is, has many different conformations in the absence of substrate, and becomes more nearly ordered in the presence of the ligand.
Presumably, it is not interacting with the major groove. However, if the repressor is to recognize when it has finally reached the operator sequence, it must be constantly sampling the sequence as it diffuses along the DNA. Possibly as it comes to each base pair it ‘drops down’, protruding its a-helices into the major groove. If the complementarity between the side-chains of the u-helices and the edges of the base pairs in the DNA is not appropriate, it would then remove its helices from the major groove and continue diffusing along the DNA.