DOI: 10.1016/s0003-2697(02)00255-5. Surface plasmon resonance measurement of pH-induced responses of immobilized biomolecules: conformational change or electrostatic interaction effects?

Surface plasmon resonance measurement of pH-induced responses of immobilized biomolecules: conformational change or electrostatic interaction effects?

10.1016/s0003-2697(02)00255-5

Crossref journal-article

Elsevier BV

Analytical Biochemistry (78)

Bibliography

Paynter, S., & Russell, D. A. (2002). Surface plasmon resonance measurement of pH-induced responses of immobilized biomolecules: conformational change or electrostatic interaction effects? Analytical Biochemistry, 309(1), 85â95.

Authors 2

Sally Paynter (first)
David A Russell (additional)

References 34 Referenced 44

10.1039/C39900001526 / J. Chem. Soc., Chem. Commun. / A novel hydrogel matrix on gold surfaces in surface plasmon resonance sensors for fast and efficient covalent immobilization of ligands by Löfås (1990)
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10.1016/S0006-3495(96)79681-9 / Biophys. J. / Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor. I. A computer simulation of the influence of mass transport by Schuck (1996)
10.1002/(SICI)1099-1352(199909/10)12:5<293::AID-JMR472>3.0.CO;2-M / J. Mol. Recog. / The influence of transport on the kinetics of binding to surface receptors: application to cells and BIAcore by Goldstein (1999)
10.1021/ac9504023 / Anal. Chem. / A self-assembled monolayer for the binding and study of histidine-tagged proteins by surface plasmon resonance by Sigal (1996)
10.1046/j.1432-1327.1999.00445.x / Eur. J. Biochem. / Tyrosine hydroxylase binds tetrahydrobiopterin cofactor with negative cooperativity, as shown by kinetic analyses and surface plasmon resonance by Flatmark (1999)
10.1006/abio.1999.4406 / Anal. Biochem. / Biosensor analysis of drug-target interactions: direct and competitive binding assays for investigation of interactions between thrombin and thrombin inhibitors by Karlsson (2000)
10.1021/bi951741t / Biochemistry / Human interleukin 4 receptor complex: neutralization effect of two monoclonal antibodies by Taremi (1996)
10.1021/bi9730792 / Biochemistry / Recognition properties of a sequence-specific DNA binding antibody by LeBlanc (1998)
10.1016/S0956-5663(01)00244-5 / Biosens. Bioelectr. / Epitope mapping analysis of apolipoprotein B-100 using a surface plasmon resonance-based biosensor by Robbio (2001)
10.1021/ac9613141 / Anal. Chem. / An optical method for evaluating ion selectivity for calcium signaling pathways in the cell by Ozawa (1997)
10.1021/bi001930y / Biochemistry / How can Ca2+ selectively activate recoverin in the presence of Mg2+? Surface plasmon resonance and FT-IR spectroscopic studies by Ozawa (2000)
10.1271/bbb.64.710 / Biosci. Biotechnol. Biochem. / Monitoring the irradiation-induced conformational changes of ovalbumin by using monoclonal antibodies and surface plasmon resonance by Masuda (2000)
10.1016/S0006-3495(95)80225-0 / Biophys. J. / Photobleaching of the photoactive yellow protein from Ectothiorhodospira halophila promotes binding to lipid bilayers: evidence from surface plasmon resonance spectroscopy by Salamon (1995)
10.1016/0022-1759(95)00221-9 / J. Immunol. Methods / Binding kinetics of an antibody against HIV p24 core protein measured with real-time biomolecular interaction analysis suggest a slow conformational change in antigen p24 by Glaser (1996)
10.1063/1.1150128 / Rev. Sci. Instrum. / High resolution surface plasmon resonance spectroscopy by Tao (1999)
10.1021/ac990947n / Anal. Chem. / High-resolution multiwavelength surface plasmon resonance spectroscopy for probing conformational and electronic changes in redox proteins by Boussaad (2000)
10.1016/S0022-0728(99)00019-4 / J. Electroanal. Chem. / Characterization of protein monolayers by surface plasmon resonance combined with cyclic voltammetry ‘in situ’ by Schlereth (1999)
10.1093/oxfordjournals.jbchem.a002818 / J. Biochem. / Monitoring of the refolding process for immobilized firefly luciferase with a biosensor based on surface plasmon resonance by Zako (2001)
10.1006/abio.2001.5163 / Anal. Biochem. / Use of surface plasmon resonance for real-time measurements of the global conformational transition in human phenylalanine hydroxylase in response to substrate binding and catalytic activation by Flatmark (2001)
10.1021/ac0105888 / Anal. Chem. / Using receptor conformational change to detect low molecular weight analytes by surface plasmon resonance by Gestwicki (2001)
10.1021/ac9713666 / Anal. Chem. / Detection of conformational changes in an immobilized protein using surface plasmon resonance by Sota (1998)
{'key': '10.1016/S0003-2697(02)00255-5_BIB23', 'series-title': 'Bioseparation Engineering', 'first-page': '125', 'author': 'Mannen', 'year': '2000'} / Bioseparation Engineering by Mannen (2000)
10.1016/S0006-3495(89)82683-9 / Biophys. J. / Surface pH controls purple-to-blue transition of bacteriorhodopsin by Szundi (1989)
10.1016/S0003-2670(00)80554-1 / Anal. Chim. Acta / Possibilities and limitations of direct detection of protein charges by means of an immunological field-effect transistor by Schasfoort (1990)
10.1021/bi00207a018 / Biochemistry / Classification of acid denaturation of proteins: intermediates and unfolded states by Fink (1994)
10.1016/0003-2697(91)90424-R / Anal. Biochem. / Immobilisation of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors by Johnsson (1991)
10.1021/ja01852a006 / J. Am. Chem. Soc. / Studies on cytochrome c. II. The optical properties of pure cytochrome c and some of its derivatives by Theorell (1941)
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10.1016/S0065-2318(08)60220-6 / Adv. Carbohydr. Chem. Biochem. / The lectins: carbohydrate-binding proteins of plants and animals by Goldstein (1978)
10.1021/jp9732219 / J. Phys. Chem. B / Imaging the molecular dimensions and oligomerization of proteins at liquid/solid interfaces by Waner (1998)
10.1021/ac980959t / Anal. Chem. / A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study by Lahiri (1999)
10.1002/bip.360301310 / Biopolymers / Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α-, β- and random coil conformations by Venyaminov (1990)
{'key': '10.1016/S0003-2697(02)00255-5_BIB34', 'series-title': 'Biochemistry', 'author': 'Stryer', 'year': '1988'} / Biochemistry by Stryer (1988)

Dates

Type	When
Created	22 years, 10 months ago (Oct. 16, 2002, 8:53 a.m.)
Deposited	6 years, 4 months ago (April 8, 2019, 5:25 a.m.)
Indexed	4 months, 3 weeks ago (April 9, 2025, 1:38 a.m.)
Issued	22 years, 10 months ago (Oct. 1, 2002)
Published	22 years, 10 months ago (Oct. 1, 2002)
Published Print	22 years, 10 months ago (Oct. 1, 2002)

Funders 0

None

BibTeX

@article{Paynter_2002, title={Surface plasmon resonance measurement of pH-induced responses of immobilized biomolecules: conformational change or electrostatic interaction effects?}, volume={309}, ISSN={0003-2697}, url={http://dx.doi.org/10.1016/s0003-2697(02)00255-5}, DOI={10.1016/s0003-2697(02)00255-5}, number={1}, journal={Analytical Biochemistry}, publisher={Elsevier BV}, author={Paynter, Sally and Russell, David A}, year={2002}, month=oct, pages={85–95} }

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