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
    A computer modeling postulated mechanism for angiotensin II receptor activation (1995)
    Springer
    The protein journal 14 (1995), S. 381-398 
    Details
    ISSN: 1573-4943
    Keywords: Angiotensin II (AII) ; AII receptor ; peptide ligand ; non-peptide antagonists ; binding site ; activation mechanism ; molecular modeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The angiotensin II receptor of the AT1-type has been modeled starting from the experimentally determined three-dimensional structure of bacteriorhodopsin as the template. Intermediate 3D structures of rhodopsin andβ 2-adrenergic receptors were built because no direct sequence alignment is possible between the AT1 receptor and bacteriorhodopsin. Docking calculations were carried out on the complex of the modeled receptor with AII, and the results were used to analyze the binding possibilities of DuP753-type antagonistic non-peptide ligands. We confirm that the positively charged Lys199 on helix 5 is crucial for ligand binding, as in our model; the charged side chain of this amino acid interacts strongly with the C-terminal carboxyl group of peptide agonists or with the acidic group at the 2′-position of the biphenyl moiety of DuP753-type antagonists. Several other receptor residues which are implicated in the binding of ligands and the activation of receptor by agonists are identified, and their functional role is discussed. Therefore, a plausible mechanism of receptor activation is proposed. The three-dimensional docking model integrates most of the available experimental observations and helps to plan pertinent site-directed mutagenesis experiments which in turn may validate or modify the present model and the proposed mechanism of receptor activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886795
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Local interactions favor the native 8-residue disulfide loop in the oxidation of a fragment corresponding to the sequence Ser-50-Met-79 derived from bovine pancreatic ribonuclease A (1988)
    Springer
    The protein journal 7 (1988), S. 377-398 
    Details
    ISSN: 1573-4943
    Keywords: RNase A ; protein fragment ; disulfide-loop formation ; native-like conformation ; protein folding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A 30-residue peptide was obtained from ribonuclease A by chemical cleavage with cyanogen bromide, subsequent sulfitolysis with concomitant S-sulfonation, and finally enzymatic cleavage withStaphylococcus aureus protease. The peptide was converted to the free thiol form by reductive cleavage of the S-sulfo-protecting groups withd,l-dithiothreitol. This peptide consisted of residues 50–79 of the native sequence of ribonuclease A, with the exception that methionine-79 had been converted to homoserine. Included in this sequence are residues cysteine-65 and cysteine-72, which form a disulfide bond in the native enzyme, as well as cysteine-58. This molecule may form one of three possible intramolecular disulfide bonds upon thiol oxidation, viz. one loop of 15 and 2 of 8 residues each. These isomeric peptides were prepared by oxidation with cystamine, 2-aminoethanethiolation of residual thiols, and fractionation by reverse-phase high-performance liquid chromatography. Disulfide pairings were established by mapping the tryptic fragments and confirming their composition by amino acid analysis. After protracted incubation under oxidizing conditions at 25.0°C andp H 8.0, the 26-member ring incorporating the native disulfide bond between residues 65 and 72 is the dominant product. Assuming that equilibrium is established, we infer that local interactions in the sequence of ribonuclease A significantly stabilize the native 8-residue disulfide loop with respect to the non-native 8-residue loop (ΔG°=−1.1±0.1 kcal mole−1). The implications of this observation for the oxidative folding of the intact protein are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024887
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    A proposal of standard conventions and nomenclature for the description of polypeptide conformations (1966)
    New York : Wiley-Blackwell
    Biopolymers 4 (1966), S. 1149-1150 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1966.360041010
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Influence of temperature on the helix sense of several polyamino acids (1969)
    New York : Wiley-Blackwell
    Biopolymers 8 (1969), S. 21-27 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An increase in temperature causes an increase in the amplitudes of intramolecular and intermolecular motions and mainfests itself as an increase in the effective radii of the various atoms, especially hydrogen atoms. If one uses a Lennard-Jones 6-12 potential function to account for nonbonded interactions, this increase in the radius of the hydrogen atom is equivalent to a modification of the coefficient of the repulsive part of the Lennard-Jones potential. Accordingly, this effect of increasing temperature on the helix sense of several polyamino acids is computed by allowing the effective radius of the hydrogen atom to increase. It is found that the preferred sense of several polyamino acid helices changes from right- to left-handed as the temperature is increased. This accounts for recent experimental observations of changes in helix sense with temperature.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1969.360080103
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Helix-coil stability constants for the naturally occuring amino acids in water. XIV. Methionine parameters from random poly(hydroxypropylglutamine,L-Methionine) (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 2447-2467 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Water-soluble, random copolymers containing L-methionine and N5-(3-hydroxypropyl)-L-glutamine have been prepared, fractionated, and characterized. The thermally induced helix-coil transitions of these copolymers in water have been investigated, and it has been found that incorporation of L-methionine increases the helix content of the polymers at all temperatures in the range of 0-60°C. The Zimm-Bragg parameters σ and s for the helix-coil transition in poly(L-methionine) in water were deduced from an analysis of the melting curves of the copolymers using the methods described in earlier papers.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360161109
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Block copolymers of amino acids. I. Synthesis and structure of copolymers of L-alanine or L-phenylalanine with D,L-lysine-d7 or D,L-lysine (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 2005-2028 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Water-soluble block copolymers of the type (A)m-(B)n-(A)p, where (A)m,p was either poly(D,L-lysine-α,β,β,γ,γ,δ,δ-d7) or poly(D,L-lysine) and (B)n was either poly(L-alanine) or poly(L-phenylalanine), were synthesized for conformational studies by proton magnetic resonance spectroscopy. Analytical determination of the amount of the initiator fragment (n-hexylamine) at the C-terminus of the copolymers was used to obtain the number-average degrees of polymerization, DPn, and thereby, together with the amino acid composition, to establish the covalent structures of the polymers. The values of DPn were found to be much lower than those deduced from sedimentation equilibrium or form viscosity measurements. These deviations, which also are thought to have arisen in similar studies reported in the literature, are attributable to intermolecular aggregation; the relation of such aggregation to covalent structure (and its effect on the polymerization reaction) is discussed in terms of the conditions and mechanism of synthesis of block copolymers of amino acids.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360160914
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Helix-coil stability constants for the naturally occurring amino acids in water. XII. Asparagine parameters from random poly(hydroxybutylglutamine-co-L-asparagine) (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 1567-1585 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The synthesis and characterization of water-soluble random copolymers containing L-asparagine with N5-(4-hydroxybutyl)-L-glutamine, and the thermally induced helix-coil transitions of these copolymers in water, are described. The incorporation of L-asparagine was found to decrease the helix content of the polymers in water at all temperatures. The Zimm-Bragg parameters σ and s for the helix-coil transition in poly(L-asparagine) in water were deduced from an analysis of the copolymer melting curves in the manner described in earlier papers. The computed values of s indicate that asparagine destabilizes helical sequences at all temperatures in the range 0-60°C.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360160715
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Infrared spectra of the N-acetyl-N′-methylamides of glycine, L-alanine, and L-leucine in dilute solutions of chloroform and carbon tetrachloride (1979)
    New York : Wiley-Blackwell
    Biopolymers 18 (1979), S. 2507-2521 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We have examined the NH stretching frequencies of N-acetyl-N′-methyl-L-alanineamide (blocked Ala), N-acetyl-N′-methylglycineamide (block Gly), and N-acetyl-N′-methyl-L-leucineamide (blocked Leu) in chloroform using irspectroscopy. Their spectrum of blocked Leu in carbon tetrachloride was also obtained. A major absorption band at 3450 cm-1 is attributed to the unperturbed NH stretching frequency. Another major band at 3437 cm-1 (for Ala) or 3432 cm-1 (for Leu) is attributed to conformations in which the NH stretching frequency is perturbed by the spatial proximity of the Cβ atom. An absorption band between 3300 and 3370 cm-1, which has in the past been assigned to the intramolecular hydrogen-bonded NH in the C7eq conformation, was found to be concentration dependent and could not be observed below 5 × 10-4M in chloroform; thus we find no evidence for a strongly hydrogen-bonded NH in the C7eq conformation in chloroform. An absorption band at 3416 cm-1 was observed in chloroform solutions of blocked Gly, and a similar absorption appeared as a shoulder on the 3437- and 3432-cm-1 bands of blocked Ala and blocked Leu, respectively, in the same solvent. These bands, occurring near 3416 cm-1, may be assigned to extended (C5) conformations [Avignon et al., Biopolymers 8, 69 (1969)]. In CCl4 the spectrum of blocked Leu remained concentration dependent below 2.8 × 10-4M, with the 3300-3370-cm-1 band progressively weakening and shifting to higher frequencies on dilution from higher concentrations. Analysis of the spectra indicates that there is considerable flexibility in the blocked single residues, in agreement with the results of conformational energy calculations.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1979.360181010
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Helix-coil stability constants for the naturally occurring amino acids in water. XXIV. Half-cystine parameters from random poly(hydroxybutylglutamine-CO-S-methylthio-L-cysteine) (1990)
    New York : Wiley-Blackwell
    Biopolymers 30 (1990), S. 121-134 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Water-soluble, random copolymers containing N5-(4-hydroxybutyl)-L-glutamine (host) and S-methylthio-L-cysteine (guest) have been prepared, fractionated, and characterized, with S-methylthio-L-cysteine serving as a model for cystine residues in proteins. From the thermally induced helix-coil transition curves of these copolymers in water at neutral pH, the Zimm-Bragg parameters σ and s for the helix-coil transition of “poly(L-cystine)” were deduced. The results show that the cystine model acts as a weak helix-breaker over the entire temperature range from 0 to 60°C. The implications of this finding are evaluated in the context of a general discussion of the Zimm-Bragg parameters for all the 20 naturally occurring amino acids.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360300113
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    The thermal melting of poly-L-alanine helices in waterThis work was supported at the Weizmann Institute by research grant No. AM 08464, and at Cornell University by research grant No. AM 08465, both from the National Institute of Arthritis and Metabolic Diseases, U. S. Public Health Service. (1966)
    New York : Wiley-Blackwell
    Biopolymers 4 (1966), S. 239-241 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1966.360040211
    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...