Y Nakamura, M Matsuda, T Honma, I Tomita, N Shibata, T Warashina, T Noro, Y Hara
{"title":"Chemical constituents of mainly active component fractionated from the aqueous tea non-dialysates, an antitumor promoter.","authors":"Y Nakamura, M Matsuda, T Honma, I Tomita, N Shibata, T Warashina, T Noro, Y Hara","doi":"10.1007/978-1-4615-4139-4_35","DOIUrl":"https://doi.org/10.1007/978-1-4615-4139-4_35","url":null,"abstract":"","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"66 ","pages":"629-41"},"PeriodicalIF":0.0,"publicationDate":"1999-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-1-4615-4139-4_35","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"21647528","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Understanding water: molecular dynamics simulations of myoglobin.","authors":"W Gu, A E Garcia, B P Schoenborn","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Molecular dynamics simulations were performed on CO myoglobin to evaluate the stability of the bound water molecules as determined in a neutron diffraction analysis. The myoglobin structure derived from the neutron analysis provided the starting coordinate set used in the simulation. The simulations show that only a few water molecules are tightly bound to protein atoms, while most solvent molecules are labile, breaking and reforming hydrogen bonds. Comparison between myoglobin in solution and in a single crystal highlighted some of the packing effects on the solvent structure and shows that water solvent plays an indispensable role in protein dynamics and structural stability. The described observations explain some of the differences in the experimental results of protein hydration as observed in NMR, neutron and X-ray diffraction studies.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"289-98"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20043570","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"High-level expression and deuteration of sperm whale myoglobin. A study of its solvent structure by X-ray and neutron diffraction methods.","authors":"F Shu, V Ramakrishnan, B P Schoenborn","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Neutron diffraction has become one of the best ways to study light atoms, such as hydrogens. Hydrogen however has a negative coherent scattering factor, and a large incoherent scattering factor, while deuterium has virtually no incoherent scattering, but a large positive coherent scattering factor. Beside causing high background due to its incoherent scattering, the negative coherent scattering of hydrogen tends to cancel out the positive contribution from other atoms in a neutron density map. Therefore a fully deuterated sample will yield better diffraction data with stronger density in the hydrogen position. On this basis, a sperm whale myoglobin gene modified to include part of the A c11 protein gene has been cloned into the T7 expression system. Milligram amounts of fully deuterated holo-myoglobin have been obtained and used for crystallization. The synthetic sperm whale myoglobin crystallized in P2(1) space group isomorphous with the native protein crystal. A complete X-ray diffraction dataset at 1.5A has been collected. This X-ray dataset, and a neutron data set collected previously on a protonated carbon-monoxymyoglobin crystal have been used for solvent structure studies. Both X-ray and neutron data have shown that there are ordered hydration layers around the protein surface. Solvent shell analysis on the neutron data further has shown that the first hydration layer behaves differently around polar and apolar regions of the protein surface. Finally, the structure of per-deuterated myoglobin has been refined using all reflections to a R factor of 17%.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"309-23"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19988972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Theoretical description of biomolecular hydration. Application to A-DNA.","authors":"A E Garcia, G Hummer, D M Soumpasis","doi":"10.1007/978-1-4615-5847-7_26","DOIUrl":"https://doi.org/10.1007/978-1-4615-5847-7_26","url":null,"abstract":"<p><p>The local density of water molecules around a biomolecule is constructed from calculated two- and three-points correlation functions of polar solvents in water using a Potential-of-Mean-Force (PMF) expansion. As a simple approximation, the hydration of all polar (including charged) groups in a biomolecule is represented by the hydration of water oxygen in bulk water, and the effect of non-polar groups on hydration are neglected, except for excluded volume effects. Pair and triplet correlation functions are calculated by molecular dynamics simulations. We present calculations of the structural hydration for ideal A-DNA molecules with sequences [d(CG)5]2 and [d(C5G5)]2. We find that this method can accurately reproduce the hydration patterns of A-DNA observed in neutron diffraction experiments on oriented DNA fibers (P. Langan et al. J. Biomol. Struct. Dyn., 10, 489 (1992)).</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"299-308"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19989071","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Neutrons in biology. A perspective.","authors":"R B Knott, B P Schoenborn","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"1-15"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19990329","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Neutron diffraction studies of amphipathic helices in phospholipid bilayers.","authors":"J P Bradshaw, K C Duff, P J Gilchrist, A M Saxena","doi":"10.1007/978-1-4615-5847-7_17","DOIUrl":"https://doi.org/10.1007/978-1-4615-5847-7_17","url":null,"abstract":"<p><p>The structural feature which is thought to facilitate the interaction of many peptides with phospholipid bilayers is the ability to fold into an amphipathic helix. In most cases the exact location and orientation of this helix with respect to the membrane is not known, and may vary with factors such as pH and phospholipid content of the bilayer. The growing interest in this area is stimulated by indications that similar interactions can contribute to the binding of certain hormones to their cell-surface receptors. We have been using the techniques of neutron diffraction from stacked phospholipid bilayers in an attempt to investigate this phenomenon with a number of membrane-active peptides. Here we report some of our findings with three of these: the bee venom melittin; the hormone calcitonin; and a synthetic peptide representing the ion channel fragment of influenza A M2 protein.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"191-202"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19989068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
D L Worcester, K Hamacher, H Kaiser, R Kulasekere, J Torbet
{"title":"Intercalation of small hydrophobic molecules in lipid bilayers containing cholesterol.","authors":"D L Worcester, K Hamacher, H Kaiser, R Kulasekere, J Torbet","doi":"10.1007/978-1-4615-5847-7_20","DOIUrl":"https://doi.org/10.1007/978-1-4615-5847-7_20","url":null,"abstract":"<p><p>Partitioning of small hydrophobic molecules into lipid bilayers containing cholesterol has been studied using the 2XC diffractometer at the University of Missouri Research Reactor. Locations of the compounds were determined by Fourier difference methods with data from both deuterated and undeuterated compounds introduced into the bilayers from the vapor phase. Data fitting procedures were developed for determining how well the compounds were localized. The compounds were found to be localized in a narrow region at the center of the hydrophobic layer, between the two halves of the bilayer. The structures are therefore intercalated structures with the long axis of the molecules in the plane of the bilayer.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"215-26"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19989070","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Neutron anatomy.","authors":"G E Bacon","doi":"10.1007/978-1-4615-5847-7_2","DOIUrl":"https://doi.org/10.1007/978-1-4615-5847-7_2","url":null,"abstract":"<p><p>The familiar extremes of crystalline material are single-crystals and random powders. In between these two extremes are polycrystalline aggregates, not randomly arranged but possessing some preferred orientation and this is the form taken by constructional materials, be they steel girders or the bones of a human or animal skeleton. The details of the preferred orientation determine the ability of the material to withstand stress in any direction. In the case of bone the crucial factor is the orientation of the c-axes of the mineral content-the crystals of the hexagonal hydroxyapatite- and this can readily be determined by neutron diffraction. In particular it can be measured over the volume of a piece of bone, utilising distances ranging from 1 mm to 10 mm. The major practical problem is to avoid the intense incoherent scattering from the hydrogen in the accompanying collagen; this can best be achieved by heat-treatment and it is demonstrated that this does not affect the underlying apatite. These studies of bone give leading anatomical information on the life and activities of humans and animals-including, for example, the life history of the human femur, the locomotion of sheep, the fracture of the legs of racehorses and the life-styles of Neolithic tribes. We conclude that the material is placed economically in the bone to withstand the expected stresses of life and the environment. The experimental results are presented in terms of the magnitude of the 0002 apatite reflection. It so happens that for a random powder the 0002, 1121 reflections, which are neighbouring lines in the powder pattern, are approximately equal in intensity. The latter reflection, being of manifold multiplicity, is scarcely affected by preferred orientation so that the numerical value of the 0002/1121 ratio serves quite accurately as a quantitative measure of the degree of orientation of the c-axes in any chosen direction, for a sample of bone.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"17-27"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19990330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
W Fuller, V T Forsyth, A Mahendrasingam, P Langan, W J Pigram, S A Mason, C C Wilson
{"title":"DNA hydration studied by neutron fiber diffraction.","authors":"W Fuller, V T Forsyth, A Mahendrasingam, P Langan, W J Pigram, S A Mason, C C Wilson","doi":"10.1007/978-1-4615-5847-7_30","DOIUrl":"https://doi.org/10.1007/978-1-4615-5847-7_30","url":null,"abstract":"<p><p>The development of neutron high angle fiber diffraction to investigate the location of water around the deoxyribonucleic acid (DNA) double-helix is described. The power of the technique is illustrated by its application to the D and A conformations of DNA using the single crystal diffractometer, D19, at the Institut Laue-Langevin. Grenoble and the time of flight diffractometer, SXD, at the Rutherford Appleton ISIS Spallation Neutron Source. These studies show the existence of bound water closely associated with the DNA. The patterns of hydration in these two DNA conformations are quite distinct and are compared to those observed in X-ray single crystal studies of two-stranded oligodeoxynucleotides. Information on the location of water around the DNA double-helix from the neutron fiber diffraction studies is combined with that on the location of alkali metal cations from complementary X-ray high angle fiber diffraction studies at the Daresbury Laboratory SRS using synchrotron radiation. These analyses emphasize the importance of viewing DNA, water and ions as a single system with specific interactions between the three components and provide a basis for understanding the effect of changes in the concentration of water and ions in inducing conformational transitions in the DNA double-helix.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"345-58"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19988975","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"In situ shape and distance measurements in neutron scattering and diffraction.","authors":"S Fujiwara, R A Mendelson","doi":"10.1007/978-1-4615-5847-7_33","DOIUrl":"https://doi.org/10.1007/978-1-4615-5847-7_33","url":null,"abstract":"<p><p>Neutron scattering combined with selective isotopic labeling and contrast matching is useful for obtaining in situ structural information about a selected particle, or particles, in a macromolecular complex. The observed intensities, however, may be distorted by inter-complex interference and by scattering-length-density fluctuations of the (otherwise) contrast-matched portions. Methods have been proposed to cancel out such distortions (Hoppe's method, the Statistical Labeling Method, and the Triple Isotopic Substitution Method). With these methods as well as related unmixed-sample methods, structural information about the selected particle(s) can be obtained without these distortions. We have generalized these methods so that, in addition to globular particles in solution, they can be applied to in situ structures of systems having underlying symmetry and/or net orientation as well. The information obtainable from such experiments is discussed.</p>","PeriodicalId":8697,"journal":{"name":"Basic life sciences","volume":"64 ","pages":"385-95"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19988978","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}