cached image

Colin David Heyes, Ph.D. - Publications

Affiliations: 
2008- Chemistry and Biochemistry University of Arkansas, Little Rock, AR 
Area:
Single Molecule Spectroscopy, Nanomaterials
Website:
http://comp.uark.edu/~cheyes/

30 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Gao F, Bajwa P, Nguyen A, Heyes CD. Shell-Dependent Photoluminescence Studies Provide Mechanistic Insights into the Off-Grey-On Transitions of Blinking Quantum Dots. Acs Nano. PMID 28221750 DOI: 10.1021/Acsnano.6B08040  0.313
2016 Henderson RC, Gao F, Jayanthi S, Kight A, Sharma P, Goforth RL, Heyes CD, Henry RL, Suresh Kumar TK. Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle. Biophysical Journal. 111: 1151-62. PMID 27653474 DOI: 10.1016/J.Bpj.2016.08.004  0.314
2016 Omogo B, Gao F, Bajwa P, Kaneko M, Heyes CD. Reducing Blinking in Small Core-Multishell Quantum Dots by Carefully Balancing Confinement Potential and Induced Lattice Strain: The "Goldilocks" Effect. Acs Nano. PMID 27058120 DOI: 10.1021/Acsnano.5B06994  0.316
2016 Morris KM, Henderson R, Suresh Kumar TK, Heyes CD, Adams PD. Intrinsic GTP Hydrolysis is Observed For a Switch 1 Variant of Cdc42 in the Presence of a Specific GTPase Inhibitor. Small Gtpases. 0. PMID 26828437 DOI: 10.1080/21541248.2015.1123797  0.31
2015 Gao F, Kight AD, Henderson R, Jayanthi S, Patel P, Murchison M, Sharma P, Goforth RL, Kumar TK, Henry RL, Heyes CD. Regulation of Structural Dynamics within a Signal Recognition Particle Promotes Binding of Protein Targeting Substrates. The Journal of Biological Chemistry. 290: 15462-74. PMID 25918165 DOI: 10.1074/Jbc.M114.624346  0.336
2015 Gao F, Kight AD, Henderson RC, Jayanthi S, Patel P, Goforth RL, Kumar T, Henry RL, Heyes CD. Role of Structural Flexibility of cpSRP43 in Binding Substrates during Post-Translational Targeting Biophysical Journal. 108: 61a. DOI: 10.1016/J.Bpj.2014.11.367  0.36
2013 Omogo B, Aldana JF, Heyes CD. Radiative and Non-Radiative Lifetime Engineering of Quantum Dots in Multiple Solvents by Surface Atom Stoichiometry and Ligands. The Journal of Physical Chemistry. C, Nanomaterials and Interfaces. 117: 2317-2327. PMID 23543893 DOI: 10.1021/Jp309368Q  0.316
2013 Mandal G, Darragh M, Wang YA, Heyes CD. Cadmium-free quantum dots as time-gated bioimaging probes in highly-autofluorescent human breast cancer cells. Chemical Communications (Cambridge, England). 49: 624-6. PMID 23223513 DOI: 10.1039/C2Cc37529J  0.305
2013 Howard AA, Webb N, Kumar T, Heyes CD. Using Homo-Polypeptides to Study Charge-Charge Interactions in Biomolecules Biophysical Journal. 104: 217a. DOI: 10.1016/J.Bpj.2012.11.1225  0.323
2012 Gao F, Ross CM, Brown J, Henry RL, Goforth R, Heyes CD. Structural Dynamics in Chloroplast Signal Recognition Particle (cpSRP) Proteins Studied with Single Molecule Fluorescence Biophysical Journal. 102: 167a. DOI: 10.1016/J.Bpj.2011.11.907  0.354
2011 Durisic N, Godin AG, Walters D, Grütter P, Wiseman PW, Heyes CD. Probing the "dark" fraction of core-shell quantum dots by ensemble and single particle pH-dependent spectroscopy. Acs Nano. 5: 9062-73. PMID 22023370 DOI: 10.1021/Nn203272P  0.324
2009 Breus VV, Heyes CD, Tron K, Nienhaus GU. Zwitterionic biocompatible quantum dots for wide pH stability and weak nonspecific binding to cells. Acs Nano. 3: 2573-80. PMID 19719085 DOI: 10.1021/Nn900600W  0.335
2009 Durisic N, Wiseman PW, Grütter P, Heyes CD. A common mechanism underlies the dark fraction formation and fluorescence blinking of quantum dots. Acs Nano. 3: 1167-75. PMID 19385605 DOI: 10.1021/Nn800684Z  0.348
2007 Heyes CD, Groll J, Möller M, Nienhaus GU. Synthesis, patterning and applications of star-shaped poly(ethylene glycol) biofunctionalized surfaces. Molecular Biosystems. 3: 419-30. PMID 17533455 DOI: 10.1039/B700055N  0.305
2007 Heyes CD, Nienhaus GU. Ultrasensitive fluorescence microscopy studies of protein interactions with functionalized surfaces Zeitschrift Fur Physikalische Chemie. 221: 75-93. DOI: 10.1524/Zpch.2007.221.1.75  0.321
2007 Heyes CD, Kobitski AY, Breus VV, Nienhaus GU. Effect of the shell on the blinking statistics of core-shell quantum dots: A single-particle fluorescence study Physical Review B - Condensed Matter and Materials Physics. 75. DOI: 10.1103/Physrevb.75.125431  0.302
2006 Kuzmenkina EV, Heyes CD, Nienhaus GU. Single-molecule FRET study of denaturant induced unfolding of RNase H. Journal of Molecular Biology. 357: 313-24. PMID 16426636 DOI: 10.1016/J.Jmb.2005.12.061  0.314
2005 Kuzmenkina EV, Heyes CD, Nienhaus GU. Single-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions. Proceedings of the National Academy of Sciences of the United States of America. 102: 15471-6. PMID 16221762 DOI: 10.1073/Pnas.0507728102  0.392
2004 Donlan RM, Piede JA, Heyes CD, Sanii L, Murga R, Edmonds P, El-Sayed I, El-Sayed MA. Model system for growing and quantifying Streptococcus pneumoniae biofilms in situ and in real time. Applied and Environmental Microbiology. 70: 4980-8. PMID 15294838 DOI: 10.1128/Aem.70.8.4980-4988.2004  0.614
2004 Amirgoulova EV, Groll J, Heyes CD, Ameringer T, Röcker C, Möller M, Nienhaus GU. Biofunctionalized polymer surfaces exhibiting minimal interaction towards immobilized proteins. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 5: 552-5. PMID 15139230 DOI: 10.1002/Cphc.200400024  0.39
2004 Groll J, Amirgoulova EV, Ameringer T, Heyes CD, Röcker C, Nienhaus GU, Möller M. Biofunctionalized, ultrathin coatings of cross-linked star-shaped poly(ethylene oxide) allow reversible folding of immobilized proteins. Journal of the American Chemical Society. 126: 4234-9. PMID 15053612 DOI: 10.1021/Ja0318028  0.343
2004 Heyes CD, Reynolds KB, El-Sayed MA. Eu3+ binding to europium-regenerated bacteriorhodopsin upon delipidation and monomerization. Febs Letters. 562: 207-10. PMID 15044027 DOI: 10.1016/S0014-5793(04)00182-6  0.499
2004 Heyes CD, Kobitski AY, Amirgoulova EV, Nienhaus GU. Biocompatible surfaces for specific tethering of individual protein molecules Journal of Physical Chemistry B. 108: 13387-13394. DOI: 10.1021/Jp049057O  0.349
2004 Kobitski AY, Heyes CD, Nienhaus GU. Total internal reflection fluorescence microscopy - A powerful tool to study single quantum dots Applied Surface Science. 234: 86-92. DOI: 10.1016/J.Apsusc.2004.05.048  0.308
2003 Heyes CD, El-Sayed MA. Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization. Biophysical Journal. 85: 426-34. PMID 12829497 DOI: 10.1016/S0006-3495(03)74487-7  0.455
2002 Wang J, Link S, Heyes CD, El-Sayed MA. Comparison of the dynamics of the primary events of bacteriorhodopsin in its trimeric and monomeric states. Biophysical Journal. 83: 1557-66. PMID 12202380 DOI: 10.1016/S0006-3495(02)73925-8  0.598
2002 Heyes CD, El-Sayed MA. The role of the native lipids and lattice structure in bacteriorhodopsin protein conformation and stability as studied by temperature-dependent Fourier transform-infrared spectroscopy. The Journal of Biological Chemistry. 277: 29437-43. PMID 12058039 DOI: 10.1074/Jbc.M203435200  0.539
2002 Heyes CD, Wang J, Sanii LS, El-Sayed MA. Fourier transform infrared study of the effect of different cations on bacteriorhodopsin protein thermal stability. Biophysical Journal. 82: 1598-606. PMID 11867472 DOI: 10.1016/S0006-3495(02)75511-2  0.619
2002 Wang J, Heyes CD, El-Sayed MA. Refolding of thermally denatured bacteriorhodopsin in purple membrane Journal of Physical Chemistry B. 106: 723-729. DOI: 10.1021/Jp013131A  0.529
2001 Heyes CD, El-Sayed MA. Effect of temperature, pH, and metal ion binding on the secondary structure of bacteriorhodopsin: FT-IR study of the melting and premelting transition temperatures. Biochemistry. 40: 11819-27. PMID 11570882 DOI: 10.1021/Bi002594O  0.505
Show low-probability matches.