AbstractAbstract
[en] Several basic experimental analytical NMR techniques that are frequently used for the qualitative and quantitative analysis of dynamic and exchange processes, focusing on proteins systems, are described: chemical exchange (slow exchange, fast exchange, intermediate exchange), heteronuclear relaxation measurements (relaxation parameters, strategy of relaxation data analysis, experimental results and examples, motional model interpretation of relaxation data, homonuclear relaxation); slow large-scale exchange and hydrogen-deuterium exchange are also studied: mechanisms of hydrogen exchange in a native protein, methods for measuring amide exchange rates by NMR, interpretation of amide exchange rates. 9 fig., 3 tab., 56 ref
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Delpuech, J.J.; Nancy-1 Univ., 54 (France); 587 p; 1994; p. 439-477; John Wiley and Sons; Singapore (Singapore)
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[en] Published in summary form only
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Graz Univ. (Austria); 199 p; 1988; p. 75; 9. European experimental NMR conference; Bad Aussee (Austria); 16-20 May 1988
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[en] Protein G is a member of a class of cell surface bacterial proteins from Streptococcus that bind IgG with high affinity. A fragment of molecular mass 6,988, which retains IgG-binding activity, has been generated by proteolytic digestion and analyzed by 1H NMR. Two-dimenstional DQF-COSY, TOCSY, and NOESY spectra have been employed to assign the 1H NMR spectrum of the peptide. Elements of regular secondary structure have been identified by using nuclear Overhauser enhancement, coupling constant, and amide proton exchange data. The secondary structure consists of a central α-helix (Ala28-Val44), flanked by two portions of β-sheet (Val5-Val26 and Asp45-Lys62). This is a fundamentally different arrangement of secondary structure from that of protein A, which is made up of three consecutive α-helics in free solution. The authors conclude that the molecular mechanisms underlying the association of protein A and protein G with IgG are different
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