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  • Wiley-Blackwell  (31)
  • 1
    Electronic Resource
    Electronic Resource
    Dielectric properties of hydrated collagen (1979)
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 35-45 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Dielectric measurements have been carried out on partially hydrated collagen in the frequency ranges 100 kHz-5 MHz, 100 MHz-1 GHz, and 8-23 GHz. In the low-frequency range, a dispersion was observed around 100 kHz which results from inhomogeneous conductivity of the samples. A dielectric relaxation was observed aroud 0.3 GHz using time-domain-spectroscopy techniques. This relaxation can be considered to originate from mobile side chains. Microwave measurements indicate that the water relaxation may extend into the 10-GHz region. An apparent discrepancy between the main water relaxation time and the average rotational correlation time of water as measured by nmr line widths was resolved by the assumption that a fraction of the water molecules is bound to the collagen with residence times on the order of 10-6 sec, whereas the remainder of the water is only weakly bound and exhibits rotational rates on the order of 10-10 sec.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1979.360180105
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  • 2
    Electronic Resource
    Electronic Resource
    Molecular dynamics simulation of the stability of a 22-residue α-helix in water and 30% trifluoroethanol (1993)
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 1159-1166 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A molecular dynamics (MD) simulation was performed on the α-helix H8-HC5, the C-terminal part of myoglobin (residue 132-153), under periodic boundary conditions in two different solutions, water and water with 30% (v/v) 2,2,2-trifluoroethanol (TFE), at 300 K to investigate the stability of the helix. In both simulations, the initial configuration was a canonical right-handed α-helix. In the course of the MD trajectory in water (200 ps), the helix clearly destabilized and began to unfold after 100 ps. In the TFE solution, two stable parts of helical regions were observed after 70 ps of a 200-ps MD simulation, supporting the notion that TFE acts as a structure-forming solvent. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360330802
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  • 3
    Electronic Resource
    Electronic Resource
    Water Relaxation Measurements on Semiquinones of Various Flavoproteins (1982)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 65 (1982), S. 2422-2430 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The water relaxation rates of several flavoproteins in the semiquinone state have been investigated by the spin echo technique. The results indicate a rather unspecific interaction between water and the protein-bound flavosemiquinones. An average interaction distance of 0.3-0.5 nm has been estimated. From the temperature dependence of the rate constants the free energy of activation for proton exchange is calculated to be about 17 kJ/mol. The rate of proton exchange is around 1011 s-1 for the flavosemiquinones investigated are accessible to water regardless of their ionic state.The large difference in relaxation rates of water protons between D- and L- amino-acid oxidases is noticeable. Oxynitrilase exhibits the highest whereas Azotobacter vinelandii flavodoxin shows the lowest water relaxation rate of the flavoproteins studied. The results are discussed in relation to the visible-light absorption properties of the flavoproteins.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19820650807
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  • 4
    Electronic Resource
    Electronic Resource
    The chemistry of drugs part IVPart III, see [1]., Configurations of antimalarials derived from qinghaosu: Dihydroqingyhaosu, artemether, and artesunic acid (1984)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 67 (1984), S. 1515-1522 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The structures of the antimalarials dihydroqinghaosu (2), artemether (3), and artesunic acid (7a) derived from qinghaosu were elaborated by 1H-NMR spectroscopy, and supported with X-ray data obtained for 2 and 3. Several new derivatives, useful for the chemical characterization of dihydroqinghaosu (2) and artesunic acid (7a), were prepared.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19840670615
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  • 5
    Electronic Resource
    Electronic Resource
    Detection of nanoscale events in dispersed polymer particles containing a charge-transfer fluorescence probe (1995)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 33 (1995), S. 399-405 
    Details
    ISSN: 0887-624X
    Keywords: polystyrene latex ; fluorescence ; solvent diffusion ; staining ; fluorescent probe ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A probe molecule, which shows an unusually large change in fluorescent properties in response to changes in its environment, was introduced into a monodisperse polystyrene latex. Upon addition of low-molecular-weight compounds, the ensuing swelling process of the latex could be followed via the changes in the fluorescence spectrum of the probe molecule. Polymerization reactions of monomers, introduced into the particles, could also be monitored by means of this approach. Using glycidylmethacrylate as the monomer led to the formation of particles in which two distinctly different surroundings could be detected after such a polymerization. © 1995 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1995.080330307
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  • 6
    Electronic Resource
    Electronic Resource
    Molecular dynamics simulation of the docking of substrates to proteins (1994)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 19 (1994), S. 174-182 
    Details
    ISSN: 0887-3585
    Keywords: molecular dynamics ; docking ; computer simulation ; substrate docking ; immunoglobulin ; rational drug design ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A simple method is described to perform docking of subtrates to proteins or probes to receptor molecules by a modification of molecular dynamics simulations. The method consists of a separation of the center-of-mass motion of the substrate from its internal and rotational motions, and a separate coupling to different thermal baths for both types of motion of the substrate and for the motion of the receptor. Thus the temperatures and the time constants of coupling to the baths can be arbitrarily varied for these three types of motion, allowing either a frozen or a flexible receptor and allowing control of search rate without disturbance of internal structure. In addition, an extra repulsive term between substrate and protein was applied to smooth the interaction. The method was applied to a model substrate docking onto a model surface, and to the docking of phosphocholine onto immunoglobulin McPC603, in both cases with a frozen receptor. Using transrational temperatures of the substrate in the range of 1300-1700 K and room temperature for the internal degrees of freedom of the substrate, an efficient nontrapping exploratory search (“helicopter view”) is obtained, which visits the correct binding sites. Low energy conformations can then be further investigated by separate search or by dynamic simulated annealing. In both cases the correct minima were identified. The possibility to work with flexible receptors is discussed. © 1994 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340190303
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  • 7
    Electronic Resource
    Electronic Resource
    Essential dynamics of proteins (1993)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 17 (1993), S. 412-425 
    Details
    ISSN: 0887-3585
    Keywords: normal modes ; constraint dynamics ; molecular dynamics ; lysozyme ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Analysis of extended molecular dynamics (MD) simulations of lysozyme in vacuo and in aqueous solution reveals that it is possible to separate the configurational space into two subspaces: (1) an “essential” subspace containing only a few degrees of freedom in which anharmonic motion occurs that comprises most of the positional fluctuations; and (2) the remaining space in which the motion has a narrow Gaussian distribution and which can be considered as “physically constrained.” If overall translation and rotation are eliminated, the two spaces can be constructed by a simple linear transformation in Cartesian coordinate space, which remains valid over several hundred picoseconds. The transformation follows from the covariance matrix of the positional deviations. The essential degrees of freedom seem to describe motions which are relevant for the function of the protein, while the physically constrained subspace merely describes irrelevant local fluctuations. The near-constraint behavior of the latter subspace allows the separation of equations of motion and promises the possibility of investigating independently the essential space and performing dynamic simulations only in this reduced space. © 1993 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340170408
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  • 8
    Electronic Resource
    Electronic Resource
    MD simulation of subtilisin BPN′ in a crystal environment (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 14 (1992), S. 451-464 
    Details
    ISSN: 0887-3585
    Keywords: protein force field ; protein crystal ; protein hydration ; Ca2+ binding site ; molecular dynamics ; subtilisin ; computer simulation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In this paper we present a molecular dynamics (MD) simulation of subtilisin BPN′ in a crystalline environment containing four protein molecules and solvent. Con-formational and dynamic properties of the molecules are compared with each other and with respect to the X-ray structure to test the validity of the force field. The agreement between simulated and experimental structure using the GROMOS force field is better than that obtained in the literature using other force fields for protein crystals. The overall shape of the molecule is well preserved, as is the conformation of α-helices and β-strands. Structural differences are mainly found in loop regions. Solvent networks found in the X-ray structure were reproduced by the simulation, which was unbiased with respect to the crystalline hydration structure. These networks seem to play an important role in the stability of the protein; evidence of this is found in the structure of the active site. The weak ion binding site in the X-ray structure of subtilisin BPN′ is occupied by a monovalent ion. When a calcium ion is placed in the initial structure, three peptide ligands are replaced by 5 water ligands, whereas a potassium ion retains (in part) its original ligands. Existing force fields yield a reliable method to probe local structure and short-time dynamics of proteins, providing an accuracy of about 0.1 nm. © 1992 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340140406
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  • 9
    Electronic Resource
    Electronic Resource
    Hydrophobic patches on the surfaces of protein structures (1996)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 25 (1996), S. 389-397 
    Details
    ISSN: 0887-3585
    Keywords: molecular recognition ; molecular surface ; lipophilicity ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A survey of hydrophobic patches on the surface of 112 soluble, monomeric proteins is presented. The largest patch on each individual protein averages around 400 Å2 but can range from 200 to 1,200 Å2. These areas are not correlated to the sizes of the proteins and only weakly to their apolar surface fraction. Ala, Lys, and Pro have dominating contributions to the apolar surface for smaller patches, while those of the hydrophobic amino acids become more important as the patch size Increases. The hydrophilic amino acids expose an approximately constant fraction of their apolar area independent of patch size; the hydrophobic residue types reach similar exposure only in the larger patches. Though the mobility of residues on the surface is generally higher, it decreases for hydrophilic residues with Increasing patch size. Several characteristics of hydrophobic patches catalogued here should prove useful in the design and engineering of proteins. © 1996 Wiley-Liss, Inc.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.10
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  • 10
    Electronic Resource
    Electronic Resource
    Model for secondary nucleation in a suspension crystallizer (1996)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 42 (1996), S. 973-982 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A model that makes it possible to evaluate the secondary nucleation rate in a pilot-scale industrial crystallizer is presented. It relates the secondary nucleation rate directly to the volume rate of attrition of large parent crystals. Two other terms are included in the equality, one that expresses the distribution formed by the attrition fragments, and the other that expresses a survival efficiency accounting for the percentage of attrition fragments that grow out after the attrition step. The model is further tested on a 970-L draft-tube-baffled evaporative crystallizer with ammonium sulfate as the model material used for crystallization and having an on-line crystal size-distribution measuring device.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690420410
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