An introduction to biological NMR spectroscopy# Dominique Marion ...
Biological NMR spectroscopy
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} } < < Book Review Biological NMR Spectroscopy. Edited by John L. Markley and Stanley J. Opella, Oxford University Press, New York, 1997, 376 pp; 140 illus.; $65.00, ISBN 0-19-509468-9. This volume constitutes a useful collection of papers covering the field of biological NMR spec- troscopy from its inception until 1995, the fiftieth anniversary of the discovery of the NMR phe- nomena. The text grew from a symposium held at Stanford University in March 1994, in honor of one of the pioneers in biological NMR, Oleg Jardetzky. The book may serve as an effective reference work with a potpourri of collected pa- pers divided into four sections covering historical aspects; protein structural studies, including fold- ing, dynamics, and specificity; nucleic acid studies; and in ¤ i ¤ o spectroscopy. The historical section is brief and incorporates four papers from key figures in the early days of the field: Oleg Jardetzky, Mildred Cohn, Robert Shulman, and the William D. Phillips Memorial Lecture presented by Joe Ackerman, at the XVth International Conference on Magnetic Reso- nance in Biological Systems, held in the Nether- lands in 1994. This section serves as a useful introduction to the major part of the text, which is a contemporary overview of protein structural studies using NMR spectroscopy. The protein section begins with two chapters on the trp repressor, a DNA binding protein. Each paper balances the other, as one focuses more on discussion of the protein itself and the other more on technical aspects of the experi- ments. A chapter on the design of novel hemoglobins illustrates the huge chemical shifts seen with iron-bearing proteins, with examples of proton spectra having resonances at 80 ppm and y20 ppm. The proton spectra of large proteins, in excess of 150,000 Da, have been simplified by selective deuteration of aromatic amino acids. From 2 H spectra of these proteins, effective cor- relation times in solution have been derived, and in addition, side-chain mobility has been studied in the solid-state. A solid-state NMR study is Ž. Ž . Concepts in Magnetic Resonance, Vol. 10 1 57]58 1998 Q 1998 John Wiley & Sons, Inc. CCC 1043-7347r98r010057-02 reported of peptides in aligned membrane sys- tems that has resulted in well resolved 3D spectra that may remove the need for specific labeling. Studies of protein folding are described using a number of techniques and complemented by 1 H 2 H exchange and solution NMR experiments. A further study using temperature and pressure jumps to study folding, presents interesting 2D spectra of folded vs. unfolded states. In order to investigate the energetics of cis: trans isomeriza- tion of proline linkages in a staphylococcal nucle- ase, a model peptide was studied and the effect of mutagenesis on stability and folding was investi- gated. Several studies of ligand binding are presented, including antibodies and enzymes. The binding of mastoparan to calmodulin is given as an example of a peptide-receptor interaction studied using NMR spectroscopy. The structure and dynamics of antibodies, antibody complexes, template en- zymes, and major histocompatibility complex Ž . MHC molecules have been studied by NMR in conjunction with x-ray diffraction and are dis- cussed. Structural studies of proteins too large for detailed solution state NMR experiments may be supplemented by diffraction, and in the nucleic acid section, a neutron study of an RNA-protein complex is analyzed. The design and characteriza- tion of DNA ligands is discussed and the study utilized an x-ray structure of the ligand. However, the NMR study of the complex was able to iden- tify five different forms in solution. In another chapter, rotating frame T relaxation, NOESY 1 and ROESY experiments of a DNA segment, were able to identify conformational transitions and study mobility and hydration properties. Examples of in ¤ i ¤ o spectroscopy include pro- ton spectra from the brain used to study en- cephalopathy in patients with AIDS-related de- mentia. NMR spectroscopy was used to study brain metabolism and the effect of drugs used in treatment. In other work, 13 C and 31 P NMR spec- troscopy was used to study metabolism in cancer cells and extended to studies in mice using sur- face coils. Multinuclear NMR studies, 31 P, 1 H, and 19 F of rat brain slices were carried out in order to determine metabolic changes in response 57
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Transcript of Biological NMR spectroscopy
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Book ReviewBiological NMR Spectroscopy.Edited by John L. Markley and Stanley J. Opella,Oxford University Press, New York, 1997, 376 pp;140 illus.; $65.00, ISBN 0-19-509468-9.
This volume constitutes a useful collection ofpapers covering the field of biological NMR spec-troscopy from its inception until 1995, the fiftiethanniversary of the discovery of the NMR phe-nomena. The text grew from a symposium held atStanford University in March 1994, in honor ofone of the pioneers in biological NMR, OlegJardetzky. The book may serve as an effectivereference work with a potpourri of collected pa-pers divided into four sections covering historicalaspects; protein structural studies, including fold-ing, dynamics, and specificity; nucleic acid studies;and in ¨ i o spectroscopy.
The historical section is brief and incorporatesfour papers from key figures in the early days ofthe field: Oleg Jardetzky, Mildred Cohn, RobertShulman, and the William D. Phillips MemorialLecture presented by Joe Ackerman, at the XVthInternational Conference on Magnetic Reso-nance in Biological Systems, held in the Nether-lands in 1994. This section serves as a usefulintroduction to the major part of the text, whichis a contemporary overview of protein structuralstudies using NMR spectroscopy.
The protein section begins with two chapterson the trp repressor, a DNA binding protein.Each paper balances the other, as one focusesmore on discussion of the protein itself and theother more on technical aspects of the experi-ments. A chapter on the design of novelhemoglobins illustrates the huge chemical shiftsseen with iron-bearing proteins, with examples ofproton spectra having resonances at 80 ppm andy20 ppm. The proton spectra of large proteins,in excess of 150,000 Da, have been simplified byselective deuteration of aromatic amino acids.From 2 H spectra of these proteins, effective cor-relation times in solution have been derived, andin addition, side-chain mobility has been studiedin the solid-state. A solid-state NMR study is
Ž . Ž .Concepts in Magnetic Resonance, Vol. 10 1 57]58 1998Q 1998 John Wiley & Sons, Inc. CCC 1043-7347r98r010057-02
reported of peptides in aligned membrane sys-tems that has resulted in well resolved 3D spectrathat may remove the need for specific labeling.
Studies of protein folding are described using anumber of techniques and complemented by1H2 H exchange and solution NMR experiments.A further study using temperature and pressurejumps to study folding, presents interesting 2Dspectra of folded vs. unfolded states. In order toinvestigate the energetics of cis:trans isomeriza-tion of proline linkages in a staphylococcal nucle-ase, a model peptide was studied and the effect ofmutagenesis on stability and folding was investi-gated.
Several studies of ligand binding are presented,including antibodies and enzymes. The binding ofmastoparan to calmodulin is given as an exampleof a peptide-receptor interaction studied usingNMR spectroscopy. The structure and dynamicsof antibodies, antibody complexes, template en-zymes, and major histocompatibility complexŽ .MHC molecules have been studied by NMR inconjunction with x-ray diffraction and are dis-cussed.
Structural studies of proteins too large fordetailed solution state NMR experiments may besupplemented by diffraction, and in the nucleicacid section, a neutron study of an RNA-proteincomplex is analyzed. The design and characteriza-tion of DNA ligands is discussed and the studyutilized an x-ray structure of the ligand. However,the NMR study of the complex was able to iden-tify five different forms in solution. In anotherchapter, rotating frame T relaxation, NOESY1and ROESY experiments of a DNA segment,were able to identify conformational transitionsand study mobility and hydration properties.
Examples of in ¨ i o spectroscopy include pro-ton spectra from the brain used to study en-cephalopathy in patients with AIDS-related de-mentia. NMR spectroscopy was used to studybrain metabolism and the effect of drugs used intreatment. In other work, 13C and 31 P NMR spec-troscopy was used to study metabolism in cancercells and extended to studies in mice using sur-face coils. Multinuclear NMR studies, 31 P, 1H,and 19 F of rat brain slices were carried out inorder to determine metabolic changes in response
57
BOOK REVIEW58
to oxygen deprivation and therapeutics. Theseexamples illustrate that NMR may prove to be auseful tool for evaluation of pharmacologicalagents.
The book has a wide authorship range span-ning three continents and includes a number ofdistinguished researchers and a foreword byRichard Ernst. The additional discussion in somecontributions in comparison to published papers
on related work is welcomed. It is a well-refer-enced and handy text with an excellent overviewof biological NMR spectroscopy.
Frances Separo¨icSchool of Chemistry
Uni ersity of MelbournePark ille VIC 3052
Australia
