Neutrons in Biology PDF
Preview Neutrons in Biology
Neutrons in Biology BASIC LIFE SCIENCES Alexander Hollaender, General Editor Associated Universities, Inc., Washington, D.C. Recent volumes in the series: Volume 18 • TRENDS IN THE BIOLOGY OF FERMENTATIONS FOR FUELS AND CHEMICALS Edited by Alexander Hollaender, Robert Rabson, Palmer Rogers, Anthony San Pietro, Raymond Valentine, and Ralph Wolfe Volume 19 • GENETIC ENGINEERING OF MICROORGANISMS FOR CHEMICALS Edited by Alexander Hollaender, Ralph D. DeMoss, Samuel Kaplan, Jordan Konisky, Dwayne Savage, and Ralph S. Wolfe Volume 20 • MOLECULAR AND CELLULAR MECHANISMS OF MUTAGENESIS Edited by J. F. Lemontt and W. M. Generoso Volume 21 • GENETIC TOXICOLOGY: An Agricultural Perspective Edited by Raymond A. Fleck and Alexander Hollaender Volume 22 • PLANT CELL CULTURE IN CROP IMPROVEMENT Edited by S. K. Sen and Kenneth L. Giles Volume 23 • INDUCED MUTAGENESIS: Molecular Mechanisms and Their Implications for Environmental Protection Edited by Christopher W. Lawrence Volume 24 • ORGAN AND SPECIES SPECIFICITY IN CHEMICAL CARCINOGENESIS Edited by Robert Langenbach, Stephen Nesnow, and Jerry M. Rice Volume 25 • BASIC BIOLOGY OF NEW DEVELOPMENTS IN BIOTECHNOLOGY Edited by Alexander Hollaender, Allen I. Laskin, and Palmer Rogers Volume 26 • GENETIC ENGINEERING OF PLANTS: An Agricultural Perspective Edited by Tsune Kosuge, Carole P. Meredith, and Alexander Hollaender Volume 27 • NEUTRONS IN BIOLOGY Edited by Benno P. Schoenborn A Continuation Order Plan is available for this series. A continuation order will bring delivery of each new volume immediately upon publication. Volumes are billed only upon actual shipment. For further information please contact the publisher. Neutrons in Biology Edited by Benno P. Schoenborn Brookhaven National Laboratory Associated Universities, Inc. Upton, New York Springer Science+Business Media, LLC Library of Congress Cataloging in Publication Data Main entry under title: Neutrons in biology. (Basic life sciences; v. 27) "Proceedings of the 32nd Brookhaven symposium in biology, held June 1-4, 1982, at Brookhaven National Laboratory, Upton, New York"—T.p. veerso. Includes bibliographical references and index. 1. Neutrons—Scattering—Congresses. 2. Biology—Methodology—Congresses. I. Schoenborn, Benno P. II. Brookhaven National Laboratory. III. Series. QH324.9.N48N48 1984 574.8/8/028 83-24708 ISBN 978-1-4899-0377-8 ISBN 978-1-4899-0375-4 (eBook) DOI 10.1007/978-1-4899-0375-4 Proceedings of the 32nd Brookhaven Symposium in Biology, held June 1-4, 1982, at Brookhaven National Laboratory, Upton, New York © Springer Science+Business Media New York 1984 Originally published by Plenum Press, New York in 1984 Softcover reprint of the hardcover 1st edition 1984 All rights reserved No part of this book may be reproduced, stored in a retrieval system, or transmitted, in any form or by any means, electronic, mechanical, photocopying, microfilming, recording, or otherwise, without written permission from the Publisher PREFACE AND ACKNOWLEDGEMENTS This second symposium on the use of neutron scattering analysis of biological structures is dedicated to the memory of Sir James Chadwick, who discovered the neutron just 50 years ago. The first symposium covering this new application of neutron physics was held here at Brookhaven National Laboratory seven years ago and was characterized by a lot of enthusiasm and expectation. Now, seven years later, the field has matured, and some of the expectations, particularly in small-angle scattering, have been fulfilled, while expectations on dynamic studies have not. The prospects of future advances in dynamic study are, however, high, and observations on polymers suggest that present instruments do have adequate resolving power for the study of bio polymers. Many of the advances presented in this volume rest on isotopic substitution studies and efficient position-sensitive detectors, developments that were highlighted in the last symposium and that were perfected during the last seven years. The Committee wishes to thank the speakers and chairmen for their participation. The Committee also wishes to express appreciation to the Dr. Alexander Hollaender Fund and the U. S. Department of Energy for support of this meeting. We thank the referees who reviewed the papers, and we particularly wish to thank Margaret Dienes, Helen Z. Kondratuk, Kathryn Kissel, and Susan Lamm for preparing the papers for printing. This 32nd Brookhaven Symposium in Biology was held under the auspices of the U. S. Department of Energy. Symposium Committee Benno P. Schoenborn, Chairman R. Douglas Carlson Anthony A. Kossiakoff Anand M. Saxena Dieter K. Schneider v CONTENTS SESSION I Plenary Lecture: Comments on Some Present and Future Problems in Protein Structure........................................ 1 F.M. Richards SESSION II. Chair: D.E. Engelman Structural Elements of the 50 S Subunit of E. Coli Ribosomes •••••••••••••.••••••••••••••••••••••••••••• 25 - R.P. May, H.B. Stuhrmann, and K.H. Nierhaus Neutron Scattering Studies of the H2a-H2b and (H3-H4)2 Histone Complexes.................................. 47 R. D. Carlson Symposium Lecture: Neutron Scattering and the 30 S Ribosomal Subunit of E. Co 11. • • • • • • • • • • • • • • • • • • • • • • • • . • • . • • • • • • • • • • • • • • • • • • • • • 73 P~B. Moore, D.M. Engelman, J.A. Langer, V.R. Ramakrishnan, D.G. Schindler, B.P. Schoenborn, I-Y. Sillers, and S. Yabuki The Solution Structures of Transfer RNA and Ribonuclease in Different Solvents •••••••••••••••••••••••••• 93 G. Zaccai SESSION III. Chair: W.C. Koehler The Crystal Structure of the Nucleosome Core Particle by Contrast Variation ••••••••••••••••••••••••••••••••••••••• 105 G.A. Bentley, J.T. Finch, A. Lewit-Bentley, and M. Roth A New Neutron Small-Angle Diffraction Instrument at the Brookhaven High Flux Beam Reactor ••••••••••••••••••••••••••• 119 D.K. Schneider and B.P. Schoenborn Neutron Optics with Multilayer Monochromators ••••••••••••••••• 143 A.M. Saxena and C.F. Majkrzak vii viii CONTENTS SESSION IV. Chair: V. James and D.L.D. Caspar Membranes and Cellular Biology: Questions of Detail or Framework......................................... * D. Worcester Neutron Diffraction Studies on Incorporation of Hexane into Oriented Lipid Bilayers ••••••••••••••••••••••••• 159 G.I. King, N.-M. Chao, and S.H. White Symposium Lecture: Neutron Scattering Studies of Virus Structure ••••••••••••••• 173 S. Cusack Specific Deuteration and Membrane Structures •••••••••••••••••• 189 G. B6ldt SESSION V. Chair: D. Worcester Neutron Diffraction and the Decomposition of Membrane Scattering Profiles into the Scattering Profiles of Their Molecular Components •••••••••••••••••••••• 201 J.K. Blasie, J.M. Pachence, and L.G. Herbette Structural Studies of Plasma Lipoproteins ••••••••••••••••••••• 211 D. Atkinson and G.G. Shipley Neutron Diffraction Studies of Bacteriorhodopsin Structure. • . . • . . . . . . . . . . • • • . . . • . • . • . . . . . . • . . . • • • • . . . • • . . . . .• 227 J. Trewhel1a, E. Gogol, G. Zaccai, and D.M. Engelman SESSION VI. Chair: G. Kartha and P.B. Moore The Structure of Bound Water and Refinement of Acid Metmyoglobin ••••••••••••••••••••••••••••••••••••••••••• 247 N.V. Raghavan and B.P. Schoenborn A Protein Structure is Only as Good as the Data ••••••••••••••• 261 B.P. Schoenborn Symposium Lecture: Use of the Neutron Diffraction--H/D Exchange Technique to Determine the Conformational Dynamics of Trypsin ••••••••• 281 A.A. Kossiakoff Hydrogen Bonding and Exchange in Oxymyoglobin ••••••••••••••••• 305 S.E.V. Phillips *No manuscript submitted. CONTENTS ix SESSION VII. Chair: S.E.V. Phillips Deuterium Exchange in Lysozyme at 1.4-i Resolution •••••••••••• 323 S.A. Mason, G.A. Bentley, and G.J. McIntyre The Neutron Structure of the Hydrophobic Plant Protein erambin •••••••••••••.•.••••.•••••••••••••••••••••••• 335 M.M. Teeter and A.A. Kossiakoff Application of Joint Neutron and X-Ray Refinement to the Investigation of the Structure of Ribonuclease A at 2.0-1 Resolution •••••.•••••.••••....••.•••••••.•.•••••••• 349 A. Wlodawer and L. Sj8lin SESSION VIII. Chair: B. Jacrot and G. Zaccai Inelastic Neutron Scattering Studies of Hexokinase in Solution •................................................ 365 D.M. Engelman, A.J. Dianoux, S. Cusack, and B. Jacrot Neutron Spectroscopy of Hydrogenous and Biosynthetically Deuterated Proteins ••••••••••••••••••••••••••••••••••••••••• 381 H.D. Middendorf, J.T. Randall, and H.L. Crespi Inelastic Scattering From Biomolecules: Principles and Prospects............................................... 401 H.D. Middendorf Concluding Remarks •••••••••••••••••••••..••...•••••••••••••••• 437 P.B. Moore ABSTRACTS OF POSTER PRESENTATIONS ••••••••••••••••••••••••••••• 441 PAR.TICIPAN'TS •••••••••••••••••••••••••••••••••••••••••••••••••• 453 INDEX. • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • •• 457 COMMENTS ON SOME PRESENT AND FUTURE PROBLEMS IN PROTEIN STRUCTURE Frederic M. Richards Department of Molecular Biophysics and Biochemistry Yale University New Haven, CT 06511 DIFFRACTION FROM CRYStALS In 1964 some program officers at NIH were seriously, and understandably, concerned that the solution of the myoglobin structure might have been an accident. The intense effort that had been going on in the field of protein crystallography during the previous five years had not produced any additional structures and perhaps would not in the foreseeable future. The dramatic appearance of the lysozyme model in 1965 fortunately put an end to thoughts of major funding shifts that were being discussed. Let us hope some comparable event occurs this year. Today, if a protein can be induced to crystallize, it can be assumed with considerable confidence that the structure will come along in due time, some, of course, more easily than others. The tricks of the trade are being codified and constantly improved. If permitted by the present Government, Brookhaven will have an increasingly important role in the future in providing the possi bility of very rapid data collection and reduction, allowing many more individuals to work out their own structures without exten sive structure laboratories of their own. One hopes the old hands will still be needed to provide solace and advice on the inevi table pitfalls that always arise. The quality of the structure will depend only on the quality of the crystals. Quality in this sense means the precision with which the mean atomic positions can be specified. It should be recognized that our most detailed knowledge of protein structure is based on those systems which provide high quali ty crys tals • This may be a very restricted, albeit con stantly expanding, subset of all proteins, and our impressions of protein structure may thus be biased to an extent at present
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