ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Sugar-water interaction from diffusion measurements (1985)
    Springer
    Journal of solution chemistry 14 (1985), S. 27-34 
    Details
    ISSN: 1572-8927
    Keywords: Diffusion coefficient ; partial molar volume ; Stokes-Einstein relation ; equatorial hydroxy group ; deoxyribose ; ribose ; carbohydrates ; hydration ; conformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The diffusion coefficients of deoxyribose and ribose in water were measured at 25°C. The Stokes-Einstein relation for mono-, di-, and tri-saccharides are discussed. The diffusion coefficient at infinite dilution Do for deoxyribose was the largest among these sugars. It appears that the deoxyribose breaks local water structure but the ribose hardly affects the structure. Do correlates well with the mean number of e-OH groups in the sugar molecule. It is suggested that the mean number of e-OH groups is a good parameter to describe the properties of sugar hydration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00646727
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Determination of thermodynamic functions from scanning calorimetry data. II. For the system that includes self-dissociation / association process (1988)
    New York : Wiley-Blackwell
    Biopolymers 27 (1988), S. 271-297 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The basic relations between the molar fractions and the scanning calorimetry data for the system that includes self-dissociation/association process such as \documentclass{article}\pagestyle{empty}\begin{document}$$ m_0 {\rm A}_{\rm 0} \mathbin{\lower.3ex\hbox{$\buildrel\textstyle\rightarrow\over {\smash{\leftarrow}\vphantom{_{\vbox to.5ex{\vss}}}}$}} m_1 {\rm A}_{\rm 1} \mathbin{\lower.3ex\hbox{$\buildrel\textstyle\rightarrow\over {\smash{\leftarrow}\vphantom{_{\vbox to.5ex{\vss}}}}$}} m_2 {\rm A}_{\rm 2} \mathbin{\lower.3ex\hbox{$\buildrel\textstyle\rightarrow\over {\smash{\leftarrow}\vphantom{_{\vbox to.5ex{\vss}}}}$}} ... \mathbin{\lower.3ex\hbox{$\buildrel\textstyle\rightarrow\over {\smash{\leftarrow}\vphantom{_{\vbox to.5ex{\vss}}}}$}} m_n {\rm A}_n $$\end{document} are presented, where mi is the stoichiometric coefficient of the ith state Ai. The relations are described for each state j as \documentclass{article}\pagestyle{empty}\begin{document}$$ \frac{d}{{dT}}\left[{- m_j \log f_j (T) + \sum\limits_i {m_i f_i (T)}} \right] = \Delta H_j (T)/RT^2 $$\end{document} where fj(T) is the molar fraction function of state j and ΔHj(T) is the difference enthalpy function of the system referred to the state j, which can be obtained by scanning calorimetry; R is the gas constant; and T is the absolute temperature. By these relations, scanning calorimetry data can be deconvoluted in order to determine the thermodynamic functions by means of single and double deconvolution. The concentration dependence of the data is analyzed by a method presented in this paper. The nonlinear least squares fitting method for the determination of the functions is discussed. For an example of the application of this method to the actual scanning calorimetry data, thermodynamic data of multistate thermal transition of Vibrio parahaemolyticus hemolysin are analyzed.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360270208
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Solution structure of human growth hormone-releasing factor fragment (1-29) by CD: Characteristic conformational change on phospholipid membrane (1991)
    New York : Wiley-Blackwell
    Biopolymers 31 (1991), S. 869-876 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformations of synthetic human growth hormone-releasing factor fragment (1-29) in the presence and the absence of l, 2-dimyristoyl-sn-glycero-3-phosphorylglycerol liposome as well as in aqueous 2, 2, 2-trifluoroethanol solution were investigated by CD spectroscopy. The secondary structure of the peptide in each solution was analyzed by two methods. Both results show that the peptide has an unordered structure in the aqueous solution. whereas it folds into helical structure in the aqueous alcohol and in the phospholipid solution. In addition, although the peptide exists as almost complete helix in the 50 vol % aqueous alcohol (80-90% helicity), it does not reach full helicity even in the solution containing excess amount of phospholipid liposome (maximum 65-70% helicity). The conformational difference is explained by the characteristic amphipathy of the peptide, i.e., the necessity to twist the separated amphipathic helical parts in the interaction with the phospholipid membrane probably makes the helicity of the peptide decrease.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360310707
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    α-Helical assembly of biologically active peptides and designed helix bundle protein (1994)
    New York : Wiley-Blackwell
    Biopolymers 34 (1994), S. 481-488 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The formation of α-helical assembly by complexing biologically active peptides with de novo designed protein is described. The de novo designed protein described here is a cystinelinked 4-helix bundle protein constructed with 80 amino acid residues and forms a hydrophobic core region surrounded by 4 helices in an aqueous solution. The biologically active peptides, such as melittin and human growth hormone releasing factor, contain the sequences that are able to form amphiphilic helices. These peptides alone do not form the α-helix structure in a diluted solution with low ion strength. But on mixing with the designed helix bundle protein, the peptides are strongly bound to the protein with the induction of α-helical structure in the biologically active peptides. The content of induced α-helix is in accord with that estimated from the amphiphilic sequence. The results mean that a novel architecture composed of α-helices is formed. Fluorescent and temperature-scanning measurement revealed that the α-helical assembly is constructed with hydrophobic interaction. Also, it is shown by means of fluorescence depolarization that the assembly has a compact globular form corresponding to 1 : 1 complex. © 1994 John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360340405
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...