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  • Biochemistry  (1,827)
  • Wiley-Blackwell  (1,822)
  • Boston, MA : Springer  (5)
  • American Chemical Society (ACS)
Collection
Keywords
Publisher
Language
Years
  • 1
    Unknown
    Introduction to Ion Beam Biotechnology (2006)
    Boston, MA : Springer
    Details
    Keywords: Biochemistry ; Biotechnology ; Microbiology
    ISBN: 9780387255866
    URL: https://doi.org/10.1007/b135662
    Language: English
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  • 2
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    Synthesis and Characterization of Glycosides (2007)
    Boston, MA : Springer
    Details
    Keywords: Analytical biochemistry ; Biochemistry ; Biotechnology ; Chemical engineering ; Chemistry, Organic
    ISBN: 9780387707921
    URL: https://doi.org/10.1007/978-0-387-70792-1
    Language: English
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  • 3
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    Principles of Fluorescence Spectroscopy (2006)
    Boston, MA : Springer
    Details
    Keywords: Analytical biochemistry ; Biochemistry ; Biomedical engineering ; Biotechnology ; Chemistry, Physical organic ; Microscopy
    Edition: Third Edition
    ISBN: 9780387463124
    URL: https://doi.org/10.1007/978-0-387-46312-4
    Language: English
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  • 4
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    Advanced Organic Chemistry, Part B : Reactions and Synthesis (2007)
    Boston, MA : Springer
    Details
    Keywords: Biochemistry ; Chemistry, Organic
    Description / Table of Contents: Advanced Organic Chemistry has maintained its place as the premier textbook in the field, since its first appearance in 1977. It offers broad coverage of the structure, reactivity and synthesis of organic compounds. As in the earlier editions, the text contains extensive references to both the primary and review literature and provides examples of data and reactions that illustrate and document the generalizations. While the text assumes completion of an introductory course in organic chemistry, it reviews the fundamental concepts for each topic. This two-part, fifth edition has been substantially revised and reorganized for greater clarity. The control of reactivity to achieve specific syntheses is one of the overarching goals of organic chemistry. Part B describes the most general and useful synthetic reactions, organized on the basis of reaction type. It can stand-alone; together, with Part A: Structure and Mechanisms, the two volumes provide a comprehensive foundation for the study in organic chemistry.
    Pages: Online-Ressource (XXX, 1322 Seiten)
    Edition: 5th ed.
    ISBN: 9780387714813
    URL: http://www.springerlink.com/content/978-0-387-68350-8/
    Language: English
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  • 5
    Unknown
    Radiative Decay Engineering (2005)
    Boston, MA : Springer
    Details
    Keywords: Analytical biochemistry ; Biochemistry ; Microscopy
    ISBN: 9780387276175
    URL: https://doi.org/10.1007/0-387-27617-3
    Language: English
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  • 6
    Electronic Resource
    Electronic Resource
    The Solution Structure of the Immunodominant and Cell Receptor Binding Regions of Foot-and-mouth Disease Virus Serotype A, Variant A (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 75-90 
    Details
    ISSN: 1075-2617
    Keywords: FMDV ; structure ; NMR spectrocopy ; NEO constraints ; RGD (Arg-Gly-Asp) ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution structure of a 20 amino acid long peptide corresponding to the region 141-160 of the envelope protein Vp1 from foot-and-mouth disease virus (FMDV) serotype A, variant A, has been determined by a combination of NMR experiments and computer calculations. The peptide contains both the immunodominant epitope as well as the sequence (RGD) used by the virus to bind the cell receptor in the initial stages of infection. These two sites have been shown to partially overlap.One hundred and thirty-five NMR distance constraints were used to obtain a set of 11 structures by distance geometry, minimization and molecular dynamics simulations. These structures were divided into two homogeneous families based upon backbone superimposition. The first and most populated family was characterized by a backbone RMS of 1.5±0.4 Å, the second by a backbone RMS of 0.8±0.2 Å. The two families had similar structural features and differed mainly in the backbone angles of G149. In the larger of the two families these angles favoured the formation of a loop comprising residues 147 to 152 and stabilized by a H-bond between the NH of D147 and the CO of A152. In the second family, where this bond was absent, the peptide adopted in this region the shape of an irregular helix. The C-terminal half of the peptide (152-159) was similar in both families and largely helical. Similar structural features were also found within the VRGDS sequence (144-148) which was assigned to a β-turn type IV. The features of the two families of structures were found to be different from those of the recently published X-ray structure of the antigenic loop of a chemically modified form of FMDV. Proposals accounting for these differences are provided which take into account the dual activity of the 141-160 sequence (i.e. antibody binding and cell invasion through receptor binding).
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.49
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  • 7
    Electronic Resource
    Electronic Resource
    The Solution Conformational Features of Two Highly Homologous Antigenic Peptides of Foot-and-mouth Disease Virus Serotype A, Variants A and USA, Correlate with their Serological Properties (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 91-105 
    Details
    ISSN: 1075-2617
    Keywords: FMDV ; NMR spectrocopy ; RGD (Arg-Gly-Asp) ; NEO constraints ; structure-activity correlation ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution structure of a peptide corresponding to the VP1 region 141-160 of foot-and-mouth disease virus (FMDV) serotype A variant USA has been studied by NMR and computer calculations and compared with the results from a study on a highly homologous peptide deriving from serotype A, variant A. The two peptides differ in their serological behaviour and contain the immunodominant epitope of the virus which partly overlaps with its receptor binding region. Distance constraints, derived both from 2D and 3D homonuclear NMR and 2D-heteronuclear NMR experiments, were combined with DG calculations to yield 50 structures. After refinement through EM and restrained molecular dynamics simulations the selected structures shared several general features. In particular the 151-158 region was a helix in all cases while a large loop similar to that found in peptide A but comprising less residues and stabilized by an H-bond between the side chains of D147 and S150 was found in the majority of structures. A further loop, common to all structures, was identified around the RGD sequence (145-147). This was different from that found in the corresponding region of peptide A as were the conformations of the individual residues within the RGDX sequence.The different structural features shown by the two peptides were rationalized in terms of the S148 (peptide A) to F148 (peptide USA) mutation. The second mutation, that at position 153 (L in A, P in USA) did not appear to affect the structure of the peptide significantly although the different dimensions of the loop in the central region and the type of H-bond stabilizing it could be potentially ascribed to this second mutation.All criteria used pointed to different structural features for the two peptides consistent with their serological behaviour.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.50
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  • 8
    Electronic Resource
    Electronic Resource
    Solid-phase Synthesis and Cellular Localization of a C- and/or N-terminal Labelled Peptide (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 125-133 
    Details
    ISSN: 1075-2617
    Keywords: SPPS ; labelled peptides ; cellular localization ; amphipathic peptide ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We report the solid-phase synthesis by the Fmoc strategy of a peptide containing a cysteamide group at its C-terminus. This peptide was subject to further modifications including the linkage of fluorophores, namely lucifer yellow and coumarin respectively, at the C- and/or N-terminals. After incubation with living cultured cells these two probes were localized and it is concluded that the post-synthesis modifications can strongly modify the localization of the peptide.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.58
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  • 9
    Electronic Resource
    Electronic Resource
    Masthead (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996) 
    Details
    ISSN: 1075-2617
    Keywords: Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.310020201
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  • 10
    Electronic Resource
    Electronic Resource
    Effects of End Group and Aggregation on Helix Conformation: Crystal Structure of Ac-(Aib-Val-Ala-Leu)2-Aib- OMe (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 2 (1996), S. 106-116 
    Details
    ISSN: 1075-2617
    Keywords: all parallel helix assemblies ; helix transition ; 310-/Α-HELICES ; two conformers ; water associated with non-polar helices ; X-ray crystallography ; Chemistry ; Biochemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The role of end groups in determining stereochemistry and packing in hydrophobic helical peptides has been investigated using an α-aminosobutyric acid (Aib) containing model nonapeptide sequence. In contrast to the Boc-analogue, Ac-(Aib-Val-Ala-Leu)2-Aib-OMe crystallizes with two independent molecules in a triclinic cell. The cell parameters are: space group P1, a=10.100(2)Å, b=15.194(4) Å, c=19.948(5) Å, α=63.12(2)°, β=88.03(2)°, γ=88.61(2)°, Z=2, R=7.96% for 5140 data where |Fo|〉3σ(F). The two independent molecules alternate in infinite columns formed by head-to-tail hydrogen bonding. The helices in the two independent molecules are quite similar to each other but one molecule is rotated ≍123° about its helix axis with respect to the other. All the helical columns pack parallel to each other in the crystal. Replacement of the bulky Boc group does not lead to any major changes in conformation. Packing characteristics are also similar to those observed for similar helical peptides.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/psc.52
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