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Your search keyword '"Kim, Judy"' showing total 8 results
Start Over Author "Kim, Judy" Journal biochemistry
8 results on '"Kim, Judy"'

1. Wavelength dependent Cis-Trans isomerization in vision

Author

Kim, Judy E., Tauber, Michael J., and Mathies, Richard A.

Subjects
Rhodopsin -- Physiological aspects, Vision research -- Analysis, Retinoids -- Physiological aspects, Quantum chemistry -- Research, Biological sciences, Chemistry
Abstract

Research reveals that the quantum yield in vision, which is mediated by the light-driven cis-trans isomerization of the 11-cis-retinal chromophore of G-protein coupled rhodopsin, is wavelength independent. Data suggest that the 200 femtoseconds photoisomerization is a result of a nonstationary excited-state vibrational wave packet dynamics.

Published
2001

2. Fluorescence and UV resonance raman study of peptide-vesicle interactions of human cathelicidin LL-37 and its F6W and F17W mutants

Author

Gable, Jonathan E., Schlamadinger, Diana E., Cogen, Anna L., Gallo, Richard L., and Kim, Judy E.

Subjects
Cathelicidins -- Chemical properties, Cathelicidins -- Structure, Fluorescence -- Analysis, Gene mutations -- Analysis, Hydrogen bonding -- Analysis, Indole -- Chemical properties, Indole -- Structure, Indole -- Optical properties, Raman spectroscopy -- Usage, Tryptophan -- Chemical properties, Biological sciences, Chemistry
Abstract

Steady-state fluorescence and UV resonance Raman spectroscopy of the single-tryptophan mutants, F6W and F17W were performed to gain insight into their molecular details and kinetics which are effective at killing bacteria and disrupting membranes as the native, tryptophan-free LL-37 peptide. The results supported carpeting or toroidal pore mechanisms of membrane disruption by LL-37 and demonstrated that combination of tryptophan mutants and sensitive spectroscopic tools might provide important molecular clues about antimicrobial action.

Published
2009

3. Resonance Raman studies of the (His)[(Cys).sub.3] 2Fe-2S cluster of MitoNEET: comparison to the [(Cys).sub.4] mutant and implications of the effects of pH on the labile metal center

Author

Tirrell, Timothy F., Paddock, Mark L., Conlan, Andrea R., Smoll, Eric J., Nechushtai, Rachel, Jennings, Patricia A., and Kim, Judy E.

Subjects
Histidine -- Chemical properties, Iron compounds -- Chemical properties, Iron compounds -- Structure, Mutation (Biology) -- Analysis, Raman spectroscopy -- Usage, Biological sciences, Chemistry
Abstract

The resonance Raman spectra of naturally occurring [Fe.sub.2][S.sub.2](His)[(Cys).sub.3] protein was determined to assess local structural changes associated with cluster lability. Systematic pH-dependent resonance Raman spectral changes observed in spectral region mitoNEET influenced by the Fe-His87 moiety revealed that the Fe-N(His87) interaction which is modulated within the physiological pH range might be critical to the function of mitoNEET.

Published
2009

4. Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: lessons from the transmembrane protein OmpA

Author

Sanchez, Katheryn M., Gable, Jonathan E., Schlamadinger, Diana E., and Kim, Judy E.

Subjects
Fluorescence -- Evaluation, Membrane proteins -- Structure, Membrane proteins -- Chemical properties, Protein folding -- Analysis, Tryptophan -- Chemical properties, Biological sciences, Chemistry
Abstract

Refolding curves of the integral membrane protein outer membrane protein A (OmpA) are measured in order to determine the conformational stabilities of the model system for membrane protein folding. The dynamic light scattering results have complemented the fluorescence studies and have shown the important effects of vesicle size on protein conformational stability.

Published
2008

5. Picosecond dynamics of G-protein coupled receptor activation in rhodopsin from time-resolved UV resonance Raman Spectroscopy

Author

Kim, Judy E., Pan, Duohai, and Mathies, Richard A.

Subjects
Rhodopsin -- Analysis, Photochemical research -- Analysis, Resonance -- Measurement, G proteins -- Influence, Biological sciences, Chemistry
Abstract

Research describes mode-specific alterations of specific aromaic residues in rhodopsin on photoexcitation as measured by picosecond UV resonance Raman spectroscopy. Data indicate that chromophore isomerization is initiated by a visible pulse, while a UV pulse selectively enhances scattering from aromatic amino acids of rhodopsin.

Published
2003

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