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  • 1
    Electronic Resource
    Electronic Resource
    Interparticle interactions and structural changes of nucleosome core particles in low-salt solution (1988)
    s.l. : American Chemical Society
    Biochemistry 27 (1988), S. 7924-7931 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00420a051
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  • 2
    Electronic Resource
    Electronic Resource
    Essential role of arginine residues in the folding of deoxyribonucleic acid into nucleosome cores (1982)
    s.l. : American Chemical Society
    Biochemistry 21 (1982), S. 5329-5334 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00264a032
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  • 3
    Electronic Resource
    Electronic Resource
    Induced cotton effects of tRNA-acridine orange complex and tRNA conformation (1972)
    New York : Wiley-Blackwell
    Biopolymers 11 (1972), S. 1583-1592 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Circular dichroism spectra of acridine orange bound to E. coli tRNA were studied at varying tRNA phosphate-to-dye (P/D) ratios for both unfractionated and purified materials in the absence of Mg++. From the rather discrete features exhibited in the circular dichroism spectra three types of interactions were observed: (1) A high P/D ratio such as 75.2 or 49.8 indicates the interaction between the nucleotide base and dye molecule. The spectra with a large positive peak at 515 mμ are, however, quite different from that of DNA-AO complex under similar conditions. (2) With an intermediate P/D ratio (26.5 to 9.6) dye molecules bound strongly to the polynucleotide chain. (3) With low P/D ratios (≤7.5) the interaction appears to be due to the stacked dye molecules in the single-stranded part of tRNA. The spectra of the third group have an isobestic point at 477 mμ. Below a P/D ratio of 4 the spectrum shows one positive and two negative bands which may be the characteristics of circular dichroism of stacked dyes in polynucleotide chain.Although no drastic change in the conformation of tRNA itself was detectable in the presence of Mg++ in the ultraviolet region, a dramatic change was observed in the circular dichroism of tRNA-acridine orange complex when Mg++ concentration was increased to 10-3M. It was inferred that certain conformational changes other than simple hydrogen bond formation occured in tRNA molecules at this high Mg++ concentration, so that the amount of bound dye in the stacking condition was increased through the transition.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1972.360110805
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of charge density of cationic polyelectrolytes on complex formation with DNA (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 1993-2004 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The interaction between DNA and ionen polymers, -[N+(CH3)2(CH2)mN+(CH3)2(CH2)n]l-, with m-n of 3-3, 6-6, and 6-10 were examined in order to know how the binding behavior of cationic polymers with DNA depends on the charge density of polycation. The ionen polymer has no bulky side chain and the binding forces with DNA would be attributed mainly to electrostatic interaction. When 3-3 ionen polymers were added to DNA solution, precipitable complexes with the ratio of cationic residue to DNA phosphate (+/-) of 1/1 and the free DNA molecules were segregated, while 6-6 and 6-10 ionen polymers formed soluble complexes with DNA molecules up to (+/-) = 0.5. This suggests that 3-3 ionen polymers bind cooperatively with DNA while 6-6 and 6-10 ionen polymers bind noncooperatively. The cooperative binding of 3-3 ionen polymer and the noncooperative binding of 6-6 ionen polymer were also supported by the thermal melting and recooling profiles from the midpoint between first and second meltings. It was concluded that the charge density of DNA phosphate is a critical value determining whether the ionen polymers bind to DNA by a cooperative or by a noncooperative binding, since the distance between successive cationic charges of 3-3 ionen polymer is shorter than that between successive phosphate charges on DNA double helix and those of 6-6 and 6-10 ionen polymers are longer.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360160913
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  • 5
    Electronic Resource
    Electronic Resource
    Induced circular dichroism of acridine orange bound to double-stranded RNA and transfer RNA (1976)
    New York : Wiley-Blackwell
    Biopolymers 15 (1976), S. 1693-1699 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The induced circular dichroism (CD) in the visible region of acridine orange bound to the double-stranded RNA from cytoplasmic polyhedrosis virus and to yeast tRNA has been measured as a function of RNA phosphate-to-dye ratio (P/D), under the conditions of 0.01 M Na+ at pH 7.0. The shape of the CD spectrum of acridine orange bound to the double-stranded RNA was quite different from the spectrum of the dye bound to DNA. The CD spectral features of acridine orange bound to the double-stranded regions in tRNA closely resembled those of the double-stranded RNA-dye complex, suggesting that the dyes bind similarly to the two RNA's. It was further found that the CD spectrum of the tRNA-dye complex at sufficiently high P/D ratios, which is assignable to monomeric, intercalated dye to the base-paired parts in tRNA, is also distinct from the corresponding spectrum of the DNA-dye complex.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1976.360150907
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  • 6
    Electronic Resource
    Electronic Resource
    Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1 (1981)
    New York : Wiley-Blackwell
    Biopolymers 20 (1981), S. 1103-1112 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The arginine and lysine residues of calf thymus histone H1 were modified with large molar excesses of 2,3-butanedione and O-methylisourea, respectively. Kinetic study of the modification reaction of the arginine residue revealed that the reaction is divided into the two pseudo-first-order processes. About a third (1 Arg) of the total arginine residues of the H1 molecule was rapidly modified without causing any detectable structural change of the molecule, and the slow modification of the remaining arginine residues (2 Arg) led to a loss of the folded structure of H1. In the case of lysine residue modification, 93% (56 Lys) of the total lysine residues of the H1 was modified with the same rate constant, while 7% (4 Lys) of lysine residue remained unmodified. When the reaction was performed in the presence of 6M guanidine-HCl, all of lysine residues were modified. It is concluded that the 2 arginine and 4 lysine residues resistant to modification are buried in interior regions of the H1 molecule and play an important role in the formation of the H1 globular structure, while the other 1 arginine and 56 lysine residues are exposed to solvent.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1981.360200602
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  • 7
    Electronic Resource
    Electronic Resource
    The interaction of 8-anilino-1-naphthalenesulfonate with polylysine and polyarginine (1977)
    New York : Wiley-Blackwell
    Biopolymers 16 (1977), S. 1449-1464 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Comparative studies on the interaction of 8-anilino-1-naphthalenesulfonate (ANS) with polylysine and polyarginine have been made by equilibrium dialysis and fluorescence or circular dichroism measurements, to investigate the structural characteristics of the polypeptides. The results are summarized as follows: (i) ANS binds to either of the polypeptides primarily by electrostatic interaction while hydrophobic interaction partially facilitates the dye binding; both interactions are stronger in the polyarginine-dye binding than the polylysine-dye binding. (ii) The fluorescence of ANS is more intensified when the dye binds to polyarginine than to polylysine regardless of the value of r (number of bound dye per amino-acid residue) of polypeptide-dye complexes, although the intensification depends on the r value and becomes maximum at r = 0.25-0.35 for both cases. (iii) The binding of ANS to each polypeptide is cooperative at r 〈 0.4. (iv) The circular dichroism is more efficiently induced in the spectral region of ANS by binding to polyarginine than to polylysine.From these results, it was concluded that, compared to polylysine, polyarginine suffers some structural change by ANS binding into a more compact molecular configuration having some regularity with a lower dielectric environment.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1977.360160706
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  • 8
    Electronic Resource
    Electronic Resource
    Conformation of poly(L-arginine). II. Complexes with polyanions (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 2783-2798 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Conformaitons of poly(L-arginine)/polyanion complexes were studies by CD measurements. The polyanions were the homoplolypeptides poly(L-glutamic acid) and poly(L-aspartic acid); the synthetic polyelectrolytes and polyethylenesulfonate; and the polynucleotides were native DNA, denatured DNA, and poly(U). It was found that poly(L-arginine) forms the α-helical conformation by interacting with the acidic homopolypeptides and the synthetic anionic polyelectrolytes. In each complex, poly(L-glutamic acid) is in the α-helical conformation, whereas poly(L-aspartic acid) is mostly in the random structure. The poly(L-glutamic acid) complex changed into the β-sheet structure at the transition temperature about 65°C in 0.01M cacodylate buffer (pH 7). Even in the presence of 5M urea, this complex remained in the α-helical conformation at room temperature. The existence of the stable complex of α-helical poly(L-arginine) and α-helical poly(L-glutamic acid) was successfully supported by the model building study of the complex. The α-helix of poly(L-arginine) induced by binding with polyacrylate was the most stable of the poly(L-arginine)-polyanion complexes examined as evidenced by thermal and urea effects. The lower helical content of the polyethylenesulfonate-complexed poly(L-aginine) was explained in terms of the higher charge density of the polyanion. On the other hand, native DNA, denatured DNA, and poly(U) were not effective in stabilizing the helical structure of poly(L-arginine). This may be due to the rigidity of polyanions and to the steric hindrance of bases. Furthermore, the distinitive structual behavior of poly(L-arginine) and poly(L-lysine) regarding polyanion interaction has been noticed throughout the study.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360171204
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  • 9
    Electronic Resource
    Electronic Resource
    Conformation of poly(L-arginine). I. Effects of anions (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 2769-2782 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformational transition of poly(L-agrignine) by binding with various mono-, di-, and polyvalent anions, especially with SO2-4, was studied by CD measurements. The intramolecular random coil-to-α-helix conformational transition and the subsequent transition to the β-turn-like structure was caused by binding with SO2-4. The binding data obtained from equilibrium dialysis experiments showed that the α-helical conformation of poly(L-arginine) is stabilized at a 1:3 stoichiometric ratio of bound SO2-4 to arginine residue; at higher free SO2-4 concentrations, the α-helix converts to the β-turn-like structure accompanied by a decrease in amount of bound SO2-4. The same conformaitonal transition of poly(L-arginine) also occurred in the solutions of other divalent anions (SO2-4, CO2-3, and HPO2-4) and polyvalent anions (P2O4-7, P3O5-10). Among the monovalent anions examined, CIO-4 and dodecyl sulfate were effective in including α-helical conformation, while the other monovalent anions (OH-, Cl-, F-, H2PO-4, HCO-3 and CIO-3) failed to induce poly(L-arginine) to assume the α-helical conformation. Thus, we noticed that, except for dodecyl sufate, the terahedral structure is common to the α-helix-forming anions. A well-defined model to the α-helical poly(L-arginine)/anion complex was proposed, in which both the binding stoichiometry of anions to the arginine residue and the tetrahedral structure of anions were taken into consideration. Based on these results, it was concluded that the tetrahedral-type anions stabilize the α-helical conformation of poly(L-arginine) by crosslinking between two guanidinium groups of nearby side chains on the same α-helix through the ringed structures stabilized by hydrogen bonds as well as by electrostatic interaction. Throughout the study it was noticed that the structural behavior of poly(L-arginine) toward anions is distinct from that of poly(L-lysine).
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360171203
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  • 10
    Electronic Resource
    Electronic Resource
    Conformation of poly(L-homoarginine) (1980)
    New York : Wiley-Blackwell
    Biopolymers 19 (1980), S. 1123-1135 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Poly(L-arginine) assumes the α-helix in the presence of the tetrahedral-type anions or some polyanions by forming the “ringed-structure bridge” between guanidinium groups and anions which is stabilized by a pair of hydrogen bonds and electrostatic interaction [Ichimura, S., Mita, K. & Zama, M. (1978) Biopolymers 17, 2769-2782; Mita, K., Ichimura, S. & Zama, M. (1978) Biopolymers 17, 2783-2798]. This paper describes the parallel CD studies on the conformational effects on poly (L-homoarginine) of various mono-, di-, polyvalent anions and some polyanions, as well as alcohol and sodium dodecylsulfate. The random coil to α-helix transition of poly(L-homoarginine) occurred only in NaClO4 solution or in the presence of high content of ethanol or methanol. The divalent and polyvalent anions of the tetrahedral type (SO42-, HPO42-, and P2O74-), which are strong α-helix-forming agents for poly(L-arginine), failed to induce the α-helical conformation of poly(L-homoarginine). By complexing with poly(L-glutamic acid) or with polyacrylate, which is also a strong α-helix-forming agent for poly(L-arginine), poly(L-homoarginine) only partially formed the α-helical conformation. Monovalent anions (OH-, Cl-, F-, and H2PO4-) did not change poly(L-homoarginine) to the α-helix, and in the range of pH 2-11, the polypeptide remained in an unordered conformation. In sodium dodecylsulfate, poly(L-homoarginine) exhibited the remarkably enlarged CD spectrum of an extended conformation, while poly(L-arginine) forms the α-helix by interacting with the agent. Thus poly(L-homoarginine), compared with poly(L-arginine), has a much lower ability to form the α-helical conformation by interacting with anions. The stronger hydrophobicity of homoarginine residue in comparison with the arginine residue would provide unfavorable conditions to maintain the α-helical conformation.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1980.360190603
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