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Retraction notice to "Protein dynamics by neutron scattering" [Biophysical Chemistry 182 (2013) 16-22].

Biophysical chemistry

[No authors listed]
PMID: 26806666
Biophys Chem. 2016 Feb;209:56. doi: 10.1016/j.bpc.2015.12.001.

No abstract available.

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Retraction notice to "Protein dynamics by neutron scattering" [Biophysical Chemistry 182 (2013) 16-22]. Biophys Chem. 2016;209:56doi: 10.1016/j.bpc.2015.12.001.
(2016). Retraction notice to "Protein dynamics by neutron scattering" [Biophysical Chemistry 182 (2013) 16-22]. Biophysical chemistry, 20956. https://doi.org/10.1016/j.bpc.2015.12.001
"Retraction notice to "Protein dynamics by neutron scattering" [Biophysical Chemistry 182 (2013) 16-22]." Biophysical chemistry vol. 209 (2016): 56. doi: https://doi.org/10.1016/j.bpc.2015.12.001
Retraction notice to "Protein dynamics by neutron scattering" [Biophysical Chemistry 182 (2013) 16-22]. Biophys Chem. 2016 Feb;209:56. doi: 10.1016/j.bpc.2015.12.001. PMID: 26806666.
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Retraction of the article "Protein dynamics by neutron scattering" published in Biophysical Chemistry 2013, 182, 16-22.

Biophysical chemistry

Benedetto A.
PMID: 24411202
Biophys Chem. 2014 Jan;185:108. doi: 10.1016/j.bpc.2013.12.002. Epub 2013 Dec 17.

No abstract available.

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Benedetto A. Retraction of the article "Protein dynamics by neutron scattering" published in Biophysical Chemistry 2013, 182, 16-22. Biophys Chem. 2013;185:108doi: 10.1016/j.bpc.2013.12.002.
Benedetto, A. (2014). Retraction of the article "Protein dynamics by neutron scattering" published in Biophysical Chemistry 2013, 182, 16-22. Biophysical chemistry, 185108. https://doi.org/10.1016/j.bpc.2013.12.002
Benedetto, Antonio. "Retraction of the article "Protein dynamics by neutron scattering" published in Biophysical Chemistry 2013, 182, 16-22." Biophysical chemistry vol. 185 (2014): 108. doi: https://doi.org/10.1016/j.bpc.2013.12.002
Benedetto A. Retraction of the article "Protein dynamics by neutron scattering" published in Biophysical Chemistry 2013, 182, 16-22. Biophys Chem. 2014 Jan;185:108. doi: 10.1016/j.bpc.2013.12.002. Epub 2013 Dec 17. PMID: 24411202.
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Functional immobilisation of the nicotinic acetylcholine receptor in tethered lipid membranes.

Biophysical chemistry

Sevin-Landais A, Rigler P, Tzartos S, Hucho F, Hovius R, Vogel H.
PMID: 10961502
Biophys Chem. 2000 Jul 15;85(2):141-52. doi: 10.1016/s0301-4622(00)00114-9.

The nicotinic acetylcholine receptor from Torpedo was immobilised in tethered membranes. Surface plasmon resonance was used to quantify the binding of ligands and antibodies to the receptor. The orientation and structural integrity of the surface-reconstituted receptor was probed using...

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Sevin-Landais A, Rigler P, Tzartos S, et al. Functional immobilisation of the nicotinic acetylcholine receptor in tethered lipid membranes. Biophys Chem. 2000;85(2):141-52doi: 10.1016/s0301-4622(00)00114-9.
Sevin-Landais, A., Rigler, P., Tzartos, S., Hucho, F., Hovius, R., & Vogel, H. (2000). Functional immobilisation of the nicotinic acetylcholine receptor in tethered lipid membranes. Biophysical chemistry, 85(2), 141-52. https://doi.org/10.1016/s0301-4622(00)00114-9
Sevin-Landais, et al. "Functional immobilisation of the nicotinic acetylcholine receptor in tethered lipid membranes." Biophysical chemistry vol. 85,2 (2000): 141-52. doi: https://doi.org/10.1016/s0301-4622(00)00114-9
Sevin-Landais A, Rigler P, Tzartos S, Hucho F, Hovius R, Vogel H. Functional immobilisation of the nicotinic acetylcholine receptor in tethered lipid membranes. Biophys Chem. 2000 Jul 15;85(2):141-52. doi: 10.1016/s0301-4622(00)00114-9. PMID: 10961502.
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Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis.

Biophysical chemistry

Wohnsland F, Schmitz AA, Steinmetz MO, Aebi U, Vergeres G.
PMID: 10961504
Biophys Chem. 2000 Jul 15;85(2):169-77. doi: 10.1016/s0301-4622(00)00113-7.

The members of the MARCKS protein family, MARCKS (an acronym for myristoylated alanine-rich C kinase substrate) and MARCKS-related protein (MRP), interact with membranes, protein kinase C, and calmodulin via their effector domain, a highly basic segment composed of 24-25...

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Wohnsland F, Schmitz AA, Steinmetz MO, et al. Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis. Biophys Chem. 2000;85(2):169-77doi: 10.1016/s0301-4622(00)00113-7.
Wohnsland, F., Schmitz, A. A., Steinmetz, M. O., Aebi, U., & Vergeres, G. (2000). Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis. Biophysical chemistry, 85(2), 169-77. https://doi.org/10.1016/s0301-4622(00)00113-7
Wohnsland, et al. "Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis." Biophysical chemistry vol. 85,2 (2000): 169-77. doi: https://doi.org/10.1016/s0301-4622(00)00113-7
Wohnsland F, Schmitz AA, Steinmetz MO, Aebi U, Vergeres G. Influence of the effector peptide of MARCKS-related protein on actin polymerization: a kinetic analysis. Biophys Chem. 2000 Jul 15;85(2):169-77. doi: 10.1016/s0301-4622(00)00113-7. PMID: 10961504.
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The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride.

Biophysical chemistry

Guo Y, Kammerer RA, Engel J.
PMID: 10961505
Biophys Chem. 2000 Jul 15;85(2):179-86. doi: 10.1016/s0301-4622(00)00119-8.

A high thermal stability is observed for the five-stranded alpha-helical coiled-coil domain of cartilage oligomeric matrix protein COMP. It does not unfold in non-denaturing buffer between 0 and 100 degrees C and thermal denaturation is only achieved at high...

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Guo Y, Kammerer RA, Engel J. The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride. Biophys Chem. 2000;85(2):179-86doi: 10.1016/s0301-4622(00)00119-8.
Guo, Y., Kammerer, R. A., & Engel, J. (2000). The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride. Biophysical chemistry, 85(2), 179-86. https://doi.org/10.1016/s0301-4622(00)00119-8
Guo, et al. "The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride." Biophysical chemistry vol. 85,2 (2000): 179-86. doi: https://doi.org/10.1016/s0301-4622(00)00119-8
Guo Y, Kammerer RA, Engel J. The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride. Biophys Chem. 2000 Jul 15;85(2):179-86. doi: 10.1016/s0301-4622(00)00119-8. PMID: 10961505.
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A time-resolved fluorescence study of 4',6'-diamidine-2-phenylindole dihydrochloride binding to polynucleotides.

Biophysical chemistry

Cavatorta P, Masotti L, Szabo AG.
PMID: 17007778
Biophys Chem. 1985 Jun;22(1):11-6. doi: 10.1016/0301-4622(85)80021-1.

At phosphate/dye (P/D) ratios greater than 30 the quantum yield of 4',6'-diamidine-2-phenylindole dihydrochloride (DAPI)-DNA and DAPI-poly(d(A-T)) complexes was found to be 0.62 and 0.66, respectively. Contrary to earlier reports a fluorescence enhancement of DAPI-poly(d(G-C)) complexes was observed with a...

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Cavatorta P, Masotti L, Szabo AG. A time-resolved fluorescence study of 4',6'-diamidine-2-phenylindole dihydrochloride binding to polynucleotides. Biophys Chem. 1985;22(1):11-6doi: 10.1016/0301-4622(85)80021-1.
Cavatorta, P., Masotti, L., & Szabo, A. G. (1985). A time-resolved fluorescence study of 4',6'-diamidine-2-phenylindole dihydrochloride binding to polynucleotides. Biophysical chemistry, 22(1), 11-6. https://doi.org/10.1016/0301-4622(85)80021-1
Cavatorta, P, et al. "A time-resolved fluorescence study of 4',6'-diamidine-2-phenylindole dihydrochloride binding to polynucleotides." Biophysical chemistry vol. 22,1 (1985): 11-6. doi: https://doi.org/10.1016/0301-4622(85)80021-1
Cavatorta P, Masotti L, Szabo AG. A time-resolved fluorescence study of 4',6'-diamidine-2-phenylindole dihydrochloride binding to polynucleotides. Biophys Chem. 1985 Jun;22(1):11-6. doi: 10.1016/0301-4622(85)80021-1. PMID: 17007778.
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Photoacoustic spectroscopy of purple membrane fragments. Evidence for disorder during photocycle.

Biophysical chemistry

Slifkin MA, Bakarudin I, Caplan SR.
PMID: 17007799
Biophys Chem. 1986 Jul;24(2):169-71. doi: 10.1016/0301-4622(86)80010-2.

A strong band at 412 nm has been observed in the photoacoustic spectrum of partially dried purple membrane, peaking sharply at a modulation frequency of about 70 Hz. This may be explained in terms of a disorder-order transition.

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Slifkin MA, Bakarudin I, Caplan SR. Photoacoustic spectroscopy of purple membrane fragments. Evidence for disorder during photocycle. Biophys Chem. 1986;24(2):169-71doi: 10.1016/0301-4622(86)80010-2.
Slifkin, M. A., Bakarudin, I., & Caplan, S. R. (1986). Photoacoustic spectroscopy of purple membrane fragments. Evidence for disorder during photocycle. Biophysical chemistry, 24(2), 169-71. https://doi.org/10.1016/0301-4622(86)80010-2
Slifkin, M A, et al. "Photoacoustic spectroscopy of purple membrane fragments. Evidence for disorder during photocycle." Biophysical chemistry vol. 24,2 (1986): 169-71. doi: https://doi.org/10.1016/0301-4622(86)80010-2
Slifkin MA, Bakarudin I, Caplan SR. Photoacoustic spectroscopy of purple membrane fragments. Evidence for disorder during photocycle. Biophys Chem. 1986 Jul;24(2):169-71. doi: 10.1016/0301-4622(86)80010-2. PMID: 17007799.
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Steady-state fluorescence polarization in planar lipid membranes. Experimental and theoretical analysis of the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-Diphenyl-1,3,5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids.

Biophysical chemistry

Frehland E, Kreikenbohm R, Pohl WG.
PMID: 17000423
Biophys Chem. 1982 Apr;15(1):73-86. doi: 10.1016/0301-4622(82)87018-x.

In continuation of earlier work, the steady-state fluorescence polarization in a globally oriented system of planar lipid membranes was analyzed experimentally and theoretically for the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-diphenyl-1,3, 5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids. The theoretical analyses of experiments...

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Frehland E, Kreikenbohm R, Pohl WG. Steady-state fluorescence polarization in planar lipid membranes. Experimental and theoretical analysis of the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-Diphenyl-1,3,5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids. Biophys Chem. 1982;15(1):73-86doi: 10.1016/0301-4622(82)87018-x.
Frehland, E., Kreikenbohm, R., & Pohl, W. G. (1982). Steady-state fluorescence polarization in planar lipid membranes. Experimental and theoretical analysis of the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-Diphenyl-1,3,5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids. Biophysical chemistry, 15(1), 73-86. https://doi.org/10.1016/0301-4622(82)87018-x
Frehland, E, et al. "Steady-state fluorescence polarization in planar lipid membranes. Experimental and theoretical analysis of the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-Diphenyl-1,3,5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids." Biophysical chemistry vol. 15,1 (1982): 73-86. doi: https://doi.org/10.1016/0301-4622(82)87018-x
Frehland E, Kreikenbohm R, Pohl WG. Steady-state fluorescence polarization in planar lipid membranes. Experimental and theoretical analysis of the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-Diphenyl-1,3,5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids. Biophys Chem. 1982 Apr;15(1):73-86. doi: 10.1016/0301-4622(82)87018-x. PMID: 17000423.
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Mass-spectrometric investigations on hydration of nucleic acid components in vacuum.

Biophysical chemistry

Alkylated Uracils I, Sukhodu LF, Yanson IK, Shelkovski VS, Wierzchowski KL.
PMID: 17000425
Biophys Chem. 1982 May;15(2):149-55. doi: 10.1016/0301-4622(82)80027-6.

Association reactions between water and alkylated uracils. occurring under field-ionization conditions in a mass spectrometer at the tungsten point emitter surface, were studied at several temperatures. The origin of peaks observed in the mass spectra at m/e ratios corresponding...

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Alkylated Uracils I, Sukhodu LF, Yanson IK, et al. Mass-spectrometric investigations on hydration of nucleic acid components in vacuum. Biophys Chem. 1982;15(2):149-55doi: 10.1016/0301-4622(82)80027-6.
Alkylated Uracils, I., Sukhodu, L. F., Yanson, I. K., Shelkovski, V. S., & Wierzchowski, K. L. (1982). Mass-spectrometric investigations on hydration of nucleic acid components in vacuum. Biophysical chemistry, 15(2), 149-55. https://doi.org/10.1016/0301-4622(82)80027-6
Alkylated Uracils, I, et al. "Mass-spectrometric investigations on hydration of nucleic acid components in vacuum." Biophysical chemistry vol. 15,2 (1982): 149-55. doi: https://doi.org/10.1016/0301-4622(82)80027-6
Alkylated Uracils I, Sukhodu LF, Yanson IK, Shelkovski VS, Wierzchowski KL. Mass-spectrometric investigations on hydration of nucleic acid components in vacuum. Biophys Chem. 1982 May;15(2):149-55. doi: 10.1016/0301-4622(82)80027-6. PMID: 17000425.
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Conformational flexibility of membrane proteins in electric fields. I. Ultraviolet absorbance and light scattering of bacteriorhodopsin in purple membranes.

Biophysical chemistry

Tsuji K, Neumann E.
PMID: 17000437
Biophys Chem. 1983 Mar;17(2):153-63. doi: 10.1016/0301-4622(83)80009-x.

Bacteriorhodopsin of halobacterial purple membranes exhibits conformational flexibility in high electric field pulses (1-30 x 10(5) V m(-1), 1-100 micros). High-field electric dichroism data of purple membrane suspensions indicate two kinetically different structural transitions within the protein; involving a...

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Tsuji K, Neumann E. Conformational flexibility of membrane proteins in electric fields. I. Ultraviolet absorbance and light scattering of bacteriorhodopsin in purple membranes. Biophys Chem. 1983;17(2):153-63doi: 10.1016/0301-4622(83)80009-x.
Tsuji, K., & Neumann, E. (1983). Conformational flexibility of membrane proteins in electric fields. I. Ultraviolet absorbance and light scattering of bacteriorhodopsin in purple membranes. Biophysical chemistry, 17(2), 153-63. https://doi.org/10.1016/0301-4622(83)80009-x
Tsuji, K, and Neumann, E. "Conformational flexibility of membrane proteins in electric fields. I. Ultraviolet absorbance and light scattering of bacteriorhodopsin in purple membranes." Biophysical chemistry vol. 17,2 (1983): 153-63. doi: https://doi.org/10.1016/0301-4622(83)80009-x
Tsuji K, Neumann E. Conformational flexibility of membrane proteins in electric fields. I. Ultraviolet absorbance and light scattering of bacteriorhodopsin in purple membranes. Biophys Chem. 1983 Mar;17(2):153-63. doi: 10.1016/0301-4622(83)80009-x. PMID: 17000437.
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Generalized finite element solution to one-dimensional flux problems.

Biophysical chemistry

Todd GP, Haschemeyer RH.
PMID: 17000440
Biophys Chem. 1983 Jun;17(4):321-6. doi: 10.1016/0301-4622(83)80017-9.

A finite element numerical solution to the general one-dimensional flow equation is derived in a form that provides a convenient and general means to simulate a wide variety of one-dimensional flow techniques of interest to biological scientists, e.g., ultracentrifugation,...

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Todd GP, Haschemeyer RH. Generalized finite element solution to one-dimensional flux problems. Biophys Chem. 1983;17(4):321-6doi: 10.1016/0301-4622(83)80017-9.
Todd, G. P., & Haschemeyer, R. H. (1983). Generalized finite element solution to one-dimensional flux problems. Biophysical chemistry, 17(4), 321-6. https://doi.org/10.1016/0301-4622(83)80017-9
Todd, G P, and Haschemeyer, R H. "Generalized finite element solution to one-dimensional flux problems." Biophysical chemistry vol. 17,4 (1983): 321-6. doi: https://doi.org/10.1016/0301-4622(83)80017-9
Todd GP, Haschemeyer RH. Generalized finite element solution to one-dimensional flux problems. Biophys Chem. 1983 Jun;17(4):321-6. doi: 10.1016/0301-4622(83)80017-9. PMID: 17000440.
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Thermodynamical model for insertion and aggregate binding of caffeine to the homopolymer poly(riboadenylate) and model choice by data analysis.

Biophysical chemistry

Weller K, Schütz H, Petri I.
PMID: 17005144
Biophys Chem. 1984 Jun;19(4):299-310. doi: 10.1016/0301-4622(84)87013-1.

This paper describes the model used to estimate the parameters of caffeine-poly(riboadenylate) (poly(A)) interactions from corresponding 1H-NMR measurements. The model of insertion and aggregate binding describes the non-cooperative insertion of a molecule C into an interspace between two monomers...

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Weller K, Schütz H, Petri I. Thermodynamical model for insertion and aggregate binding of caffeine to the homopolymer poly(riboadenylate) and model choice by data analysis. Biophys Chem. 1984;19(4):299-310doi: 10.1016/0301-4622(84)87013-1.
Weller, K., Schütz, H., & Petri, I. (1984). Thermodynamical model for insertion and aggregate binding of caffeine to the homopolymer poly(riboadenylate) and model choice by data analysis. Biophysical chemistry, 19(4), 299-310. https://doi.org/10.1016/0301-4622(84)87013-1
Weller, K, et al. "Thermodynamical model for insertion and aggregate binding of caffeine to the homopolymer poly(riboadenylate) and model choice by data analysis." Biophysical chemistry vol. 19,4 (1984): 299-310. doi: https://doi.org/10.1016/0301-4622(84)87013-1
Weller K, Schütz H, Petri I. Thermodynamical model for insertion and aggregate binding of caffeine to the homopolymer poly(riboadenylate) and model choice by data analysis. Biophys Chem. 1984 Jun;19(4):299-310. doi: 10.1016/0301-4622(84)87013-1. PMID: 17005144.
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