H. Clark Hyde

ORCID: 0000-0002-3796-6365
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About
Contact & Profiles
Research Areas
  • Ion channel regulation and function
  • Lipid Membrane Structure and Behavior
  • Electron Spin Resonance Studies
  • Neuroscience and Neuropharmacology Research
  • Biotin and Related Studies
  • Cardiac electrophysiology and arrhythmias
  • Electrochemical Analysis and Applications
  • Molecular Junctions and Nanostructures
  • Spectroscopy and Quantum Chemical Studies
  • Nanoparticle-Based Drug Delivery
  • Plant and Biological Electrophysiology Studies
  • Computational Drug Discovery Methods
  • Lanthanide and Transition Metal Complexes
  • RNA and protein synthesis mechanisms
  • Advanced Fluorescence Microscopy Techniques
  • Monoclonal and Polyclonal Antibodies Research
  • Advanced biosensing and bioanalysis techniques
  • Protein Kinase Regulation and GTPase Signaling

University of Chicago
2008-2016

Significance Voltage sensors are integral membrane protein domains that regulate ion channels and enzymes by transporting electrically charged residues across a narrow constriction focuses the electrical field. Here, we investigated how this constriction, also called “gating pore,” controls transport studying effects of large number point mutations. Our analysis indicates presence nonambiguous statistical correlations between specific amino acid lateral-chain physicochemical properties...

10.1073/pnas.1406161111 article EN Proceedings of the National Academy of Sciences 2014-04-29

The prokaryotic KcsA channel is gated at the helical bundle crossing by intracellular protons and inactivates extracellular selectivity filter. C-terminal transmembrane helix has to undergo a conformational change for potassium ions access central cavity. Whereas partial opening of tetrameric suggested be responsible subconductance levels ion channels, including KcsA, cooperative 4 subunits postulated as final step. In this study, we used single-channel fluorescence spectroscopy directly...

10.1073/pnas.0807056106 article EN Proceedings of the National Academy of Sciences 2008-12-13

Distance determination from an echo intensity modulation obtained by pulsed double electron–electron resonance (DEER) experiment is a mathematically ill-posed problem. Tikhonov regularization yields distance distributions that can be difficult to interpret, especially in system with multiple discrete distributions. Here, we show using geometric fit constraints symmetric homo-oligomeric protein systems, were able increase the accuracy of model-based solution based on sum Rice Our approach was...

10.1021/ja3069038 article EN Journal of the American Chemical Society 2012-09-04

Significance Large-conductance Ca 2+ - and voltage-activated K + (BK) channels play many physiological roles, ranging from the maintenance of smooth muscle tone to modulation alcohol tolerance. In most cases, this versatility BK channel is due association pore-forming α-subunit with β-subunits. Therefore, it importance know what structural consequences are. Here, using lanthanide-based resonance energy transfer, we were able determine extracellular position transmembrane segments S0–S2...

10.1073/pnas.1606381113 article EN Proceedings of the National Academy of Sciences 2016-05-23

Proteins may undergo multiple conformational changes required for their function. One strategy used to estimate target-site positions in unknown structural conformations involves single-pair resonance energy transfer (RET) distance measurements. However, interpretation of inter-residue distances is difficult when applied three-dimensional rearrangements, especially homomeric systems. We developed a positioning method using inverse trilateration/triangulation map target sites within protein...

10.1016/j.str.2012.08.022 article EN publisher-specific-oa Structure 2012-10-01

10.1016/j.bpj.2009.12.1722 article EN publisher-specific-oa Biophysical Journal 2010-01-01
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