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  • Chemistry
  • Life and Medical Sciences
  • Polymer and Materials Science
  • American Association for the Advancement of Science (AAAS)  (53)
  • 1985-1989  (47)
  • 1975-1979  (6)
  • 1970-1974
  • 1900-1904
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  • 1
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    Characterization of a helical protein designed from first principles (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-19
    Description: The question of how the primary amino acid sequence of a protein determines its three-dimensional structure is still unanswered. One approach to this problem involves the de novo design of model peptides and proteins that should adopt desired three-dimensional structures. A systematic approach was aimed at the design of a four-helix bundle protein. The gene encoding the designed protein was synthesized and the protein was expressed in Escherichia coli and purified to homogeneity. The protein was shown to be monomeric, highly helical, and very stable to denaturation by guanidine hydrochloride (GuHCl). Thus a globular protein has been designed that is capable of adopting a stable, folded structure in aqueous solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Regan, L -- DeGrado, W F -- New York, N.Y. -- Science. 1988 Aug 19;241(4868):976-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. du Pont de Nemours & Company, Central Research & Development Department, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3043666" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chemical Phenomena ; Chemistry ; Chromatography, Gel ; Escherichia coli/genetics ; Molecular Sequence Data ; Plasmids ; *Protein Conformation ; *Proteins/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Sequence-specific peptide cleavage catalyzed by an antibody (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-03-03
    Description: Monoclonal antibodies have been induced that are capable of catalyzing specific hydrolysis of the Gly-Phe bond of peptide substrates at neutral pH with a metal complex cofactor. The antibodies were produced by immunizing with a Co(III) triethylenetetramine (trien)-peptide hapten. These antibodies as a group are capable of binding trien complexes of not only Co(III) but also of numerous other metals. Six peptides were examined as possible substrates with the antibodies and various metal complexes. Two of these peptides were cleaved by several of the antibodies. One antibody was studied in detail, and cleavage was observed for the substrates with the trien complexes of Zn(II), Ga(III), Fe(III), In(III), Cu(II), Ni(II), Lu(III), Mg(II), or Mn(II) as cofactors. A turnover number of 6 x 10(-4) per second was observed for these substrates. These results demonstrate the feasibility of the use of cofactor-assisted catalysis in an antibody binding site to accomplish difficult chemical transformations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Iverson, B L -- Lerner, R A -- New York, N.Y. -- Science. 1989 Mar 3;243(4895):1184-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2922606" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antibodies, Monoclonal ; Antigens/immunology ; Binding Sites, Antibody ; Catalysis ; Chemical Phenomena ; Chemistry ; Cobalt/immunology/metabolism ; Glycine/metabolism ; Haptens/immunology ; Hydrogen-Ion Concentration ; Hydrolysis ; Immunization ; Metals/metabolism ; Mice ; Molecular Sequence Data ; Molecular Structure ; Oligopeptides/*metabolism ; Phenylalanine/metabolism ; Trientine/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Molecular mechanisms and forces involved in the adhesion and fusion of amphiphilic bilayers (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: The surface forces apparatus technique was used for measuring the adhesion, deformation, and fusion of bilayers supported on mica surfaces in aqueous solutions. The most important force leading to the direct fusion of bilayers is the hydrophobic interaction, although the occurrence of fusion is not simply related to the force law between bilayers. Bilayers do not need to "overcome" some repulsive force barrier, such as hydration, before they can fuse. Instead, once bilayer surfaces come within about 1 nanometer of each other, local deformations and molecular rearrangements allow them to "bypass" these forces.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helm, C A -- Israelachvili, J N -- McGuiggan, P M -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):919-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814514" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Lipid Bilayers ; Models, Biological ; Models, Structural ; Phosphatidylcholines ; Phosphatidylethanolamines
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    "Chemzymes" mimic biology in miniature (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-07-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldrop, M M -- New York, N.Y. -- Science. 1989 Jul 28;245(4916):354-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2756423" target="_blank"〉PubMed〈/a〉
    Keywords: *Catalysis ; Chemical Phenomena ; Chemistry ; *Enzymes ; Technology, Pharmaceutical
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Molecular recognition and metal ion template synthesis (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-26
    Description: Methods for the design and synthesis of ligands intended to be specific for a metal ion have been a recent chemical development. This article describes how this process can be inverted so that the specifics of the coordination environment around the metal ion can be used as a template in large-scale ligand synthesis. The synthesis of macrobicyclic ligands for ferric ion has been accomplished by using active esters of catechol ligands in which catecholate coordination to iron is a prelude to the organic chemical reactions that link the coordination subunits together into one ligand system surrounding a central metal ion coordination site. The lanthanide(III) ions, which are among the most labile metal ions known, have coordination numbers of 8 or higher, and thus their encapsulation into a macrobicyclic structure is a challenging problem. Lanthanide amine complexes have been used as metal templates in the synthesis of such macrobicyclic lanthanide complexes. There is evidence that such a complex is inert to exchange in aqueous solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McMurry, T J -- Raymond, K N -- Smith, P H -- New York, N.Y. -- Science. 1989 May 26;244(4907):938-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Radiation Oncology Branch, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2658057" target="_blank"〉PubMed〈/a〉
    Keywords: Cations ; Chemical Phenomena ; Chemistry ; Iron/metabolism ; *Ligands ; Macromolecular Substances ; Metals/*metabolism ; Metals, Rare Earth/metabolism ; Molecular Structure ; Templates, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Polymer synthesis and organotransition metal chemistry (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-17
    Description: Mechanistic and synthetic studies in organometallic chemistry have provided considerable insight into olefin metathesis and Ziegler-Natta polymerization. New homogeneous olefin metathesis catalysts based on high oxidation state transition metals have opened new opportunities in polymer synthesis by providing unprecedented control in ring-opening polymerization of cyclic alkenes. The recent development of living coordinative polymerization systems has led to the preparation of a number of new, interesting materials, including block copolymers, conducting polymers or precursors, and ionophoric polymeric substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grubbs, R H -- Tumas, W -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):907-15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2645643" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; *Organometallic Compounds ; *Polymers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    DNA binding by proteins (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Study of proteins that recognize specific DNA sequences has yielded much information, but the field is still in its infancy. Already two major structural motifs have been discovered, the helix-turn-helix and zinc finger, and numerous examples of DNA-binding proteins containing either of them are known. The restriction enzyme Eco RI uses yet a different motif. Additional motifs are likely to be found as well. There is a growing understanding of some of the physical chemistry involved in protein-DNA binding, but much remains to be learned before it becomes possible to engineer a protein that binds to a specific DNA sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schleif, R -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1182-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842864" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Binding Sites ; Chemical Phenomena ; Chemistry ; DNA/metabolism ; DNA Restriction Enzymes/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease EcoRI ; Electrochemistry ; Nucleic Acids/metabolism ; Protein Conformation ; Zinc
    Print ISSN: 0036-8075
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  • 8
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    Introduction of nucleophiles and spectroscopic probes into antibody combining sites (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-18
    Description: A general chemical strategy has been developed whereby antibody combining sites can be selectively derivatized with natural or synthetic molecules, such as catalytic groups, drugs, metals, or reporter molecules. Cleavable affinity labels were used to selectively introduce a thiol into the combining site of the immunoglobulin A MOPC 315. This thiol acted both as a nucleophile to accelerate ester thiolysis 60,000-fold and as a handle for selectively derivatizing the antibody with additional functional groups. For example, derivatization of the antibody with a fluorophore made possible a direct spectroscopic assay of antibody-ligand complexation. This chemistry should not only extend our ability to exploit antibody specificity in chemical catalysis, diagnostics, and therapeutics, but may also prove generally applicable to the functional modification of other proteins for which detailed structural information is unavailable.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pollack, S J -- Nakayama, G R -- Schultz, P G -- AI24695-02/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 18;242(4881):1038-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3194752" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Animals ; *Antigen-Antibody Reactions ; *Binding Sites, Antibody ; Chemical Phenomena ; Chemistry ; Dinitrobenzenes ; Immunoglobulin Fab Fragments ; Mice ; Spectrometry, Fluorescence ; Sulfhydryl Compounds
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Picosecond chemical and biological events (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-13
    Description: Picosecond spectroscopy is a relatively new field of science that utilizes ultrashort laser pulses to monitor events taking place in the 10(-12) second regime. The continuing development of picosecond spectroscopy has made possible the detection and measurement of the primary events in many physical and tiological processes. This article describes a currently used picosecond spectroscopy system that is capable of reliably recording picosecond events. Two areas of picosecond research are discussed; one concerns the interaction of electrons in fluids, and the second the primary events in vision.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rentzepis, P M -- New York, N.Y. -- Science. 1978 Oct 13;202(4364):174-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/694523" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Electrons ; *Kinetics ; Lasers ; Protons ; *Retinal Pigments ; *Rhodopsin ; Spectrum Analysis/*methods ; Temperature ; *Vision, Ocular
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Benzo(a)pyrene-7,8-dihydrodiol 9,10-oxide adenosine and deoxyadenosine adducts: structure and stereochemistry (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-12-14
    Description: The structure and absolute stereoconfigurations of four adenosine adducts with (+/-)-7 alpha,8 beta-dihydroxy-9 beta, 10 beta-epoxy-7,8,9,10-tetrahydrobenzo(a)pyrene (BPDE) and their deoxyadenosine analogs have been determined. They result from both cis and trans addition of the N6 amino group of ademine to the 10 position of both enantiomers of BDPE. This was determined from studies of the nuclear magnetic resonance spectra, mass spectra, and circular dichroism spectra, as well as from their pKa values and chemical reactivities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeffrey, A M -- Grzeskowiak, K -- Weinstein, I B -- Nakanishi, K -- Roller, P -- Harvey, R G -- New York, N.Y. -- Science. 1979 Dec 14;206(4424):1309-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/316186" target="_blank"〉PubMed〈/a〉
    Keywords: *Benzopyrenes ; Chemical Phenomena ; Chemistry ; Circular Dichroism ; Dna ; *Deoxyadenosines/analogs & derivatives ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Molecular Conformation ; Mutation ; Stereoisomerism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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