Research Briefings 1986 (1986) / Chapter Skim
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Report of the Research Briefing Panel on Protein Structure and Biological Function
Report of the Research Briefing Panel on Protein Structure and Biological Function
Pages 37-48
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Report of the Research Briefing Panel on Protein Structure and Biological Function
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Don Wiley, Harvard University, Cambridge, Mass. Staff Barbara FiIner, Director, Division of Health Sciences Policy, Institute of Medicine Naomi Hudson, Administrative Secretary Allan R
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Proteins are polymer molecules composed of amino acids that are connected by links known as peptide bonds. An individual protein molecule may contain hundreds 39 or thousands of amino acids arranged in one, or several, polypeptide chains.
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In addition, structural analysis may reveal specific differences in essential enzymes that will enable geneticists to engineer protein sequences, or drug designers to produce reagents, that will selectively counter harmful bacteria or insects without harming the host. RESEARCH GOALS THE FOLDING PROBLEM Inside a cell, amino acids are assembled into peptide chains by a complex system that translates the genetic message into specific amino acid sequences.
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RECENT ADVANCES IN KNOWLEDGE About 300 protein structures are known, and about 10 to 20 new structures are reported each year. In many cases, knowledge of these structures has brought us closer to the goals outlined above understanding folding, stability, ligand binding, signal transmission, and catalytic activity.
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The full benefits of fast synchrotron data collection are not yet being realized because the diffracted intensities are recorded on photographic film. More effective use of synchrotron facilities for protein structure investigations will require a hich-flux area de O J
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Of special note is the recent successful crystallization of integral membrane proteins such as the photosynthetic reaction center and bacterial rhodops~n. NUCLEAR MAGNETIC RESONANCE With a nuclear magnetic resonance (NMR)
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Defining procedures for the precise manipulation of nuclear spin in a moleculespin engineering will continue to play an important role in the development of operating procedures for NMR spectrometers, especially for macromolecules with their complex spin systems. An appropriate sequence of radio-frequency pulses can drastically simplify a complex spectrum, reveal relations between spatially distant atoms, and greatly assist in the essential step of assigning peak signals to portions of the protein structure.
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From page 45... ...
Nonetheless, cloning is not always successful. Degradation of the product can severely reduce the yield; inside the bacterial cell, the chain may not fold to yield the desired, biologically active molecule; and modification of certain amino acids after polymerization of the protein as required for various eukaryotic proteins ("post-translational" modification)
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From page 46... ...
Researchers experienced in one or more aspects of structural biology and general protein chemistry are in high demand at this time, and corporations have attracted much of the presently available talent. Currently available predoctoral training programs may be adequate to provide the necessary graduate student input to this field provided these predoctoral training programs are maintained at a level at least equal to their present levels.
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From page 47... ...
It is essential that a mechanism be found for providing amino acids and nucleotides with a variety of different stable isotope labeling patterns for the research community. Computers The instrumentation needs for theoretical and experimental studies of proteins include increased and predictable access to supercomputers; improved communications between these machines anct remote users through networking; and additional access to high-quality graphics devices, scientific workstations, and special-purpose computers.
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From page 48... ...
Therefore, it is time to plan for the accession and use of the ciata in a computerized central data bank. Computer searches of genetic structure data banks have provided significant new insights into biological phenomena, and a similar outcome can be expected from the protein structure data.
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