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Your search keyword '"Wood, Matthew"' showing total 10 results
Start Over Author "Wood, Matthew" Journal biochemistry
10 results on '"Wood, Matthew"'

1. Conformational dimorphism and transmembrane orientation of prion protein residues 110-136 in bicelles

Author

Glover, Kerney Jebrell, Whiles, Jennifer A., Wood, Matthew J., Melacini, Giuseppe, Komives, Elizabeth A., and Vold, Regitze R.

Subjects
Prions -- Research, Structure-activity relationships (Biochemistry) -- Analysis, Proteins -- Structure, Conformational analysis -- Research, Membrane proteins -- Research, Biological sciences, Chemistry
Abstract

Results point out that the conformational dimorphism of the prion protein fragment of residues 110-136 is due to the charge state of a single histidine residue. The helical conformation of prion spans the bilayer.

Published
2001

2. Time-resolved circular dichroism studies of protein folding intermediates of cytochrome c

Author

Chen, Eefei, Wood, Matthew J., Fink, Anthony L., and Kliger, David S.

Subjects
Cytochrome c -- Research, Protein folding -- Research, Circular dichroism -- Analysis, Photoabsorption -- Analysis, Photochemical research -- Analysis, Biological sciences, Chemistry
Abstract

The photolysis reaction of CO-bound species was investigated via time resolved absorption and time-resolved circular dichroism (TRCD) methods to determine protein folding intermediates of cytochrome c. Results of TRCD studies revealed four intermediates with two, 50, 225 and 880 microsecond lifetimes. The findings further showed that folding after two microseconds may be controlled by litigation of His26/His33 using Fe(II).

Published
1998

3. A genetically encoded probe for cysteine sulfenic acid protein modification in vivo

Author

Takanishi, Christina L., Li-Hua Ma, and Wood, Matthew J.

Subjects
Cysteine -- Genetic aspects, Cysteine -- Research, Oxidation-reduction reaction -- Analysis, Oxidative stress -- Research, Biological sciences, Chemistry
Abstract

A redox-regulated domain from the Yap1 transcription factor is utilized to trap the proteins that form cysteine sulfenic acid (Cys-SOH) in vivo. The Yap1 probe is found to be extremely efficient for monitoring Cys-SOH in any organism.

Published
2007

4. Thermodynamics basis for redox regulation of the Yap1 signal transduction pathway

Author

Mason, Jeremy T., Sung-Kun Kim, Knaff, David B., and Wood, Matthew J.

Subjects
Cellular signal transduction -- Physiological aspects, Brewer's yeast -- Physiological aspects, Redox potential -- Research, Oxidative stress -- Research, Biological sciences, Chemistry
Abstract

The thermodynamic basis of the disulfide/dithiol couples are examined in the pathway of the Yap1 oxidative stress signal transduction found in Saccharomyces cerevisiae. It is observed that the oxidized basis form of the Yap1 redox domain fragment, derived from the Yap1 transcription factor contains two disulfide bonds, one between Cys303 and Cys598 and one between Cys310 and Cys629.

Published
2006

5. Dynamics of the fragment of thrombomodulin containing the fourth and fifth epidermal growth factor-like domains correlate with function

Author

Prieto, Judith H., Benitez, Benedetta A. Sampoli, Melacini, Giuseppe, Johnson, David A., Wood, Matthew J., and Komives, Elizabeth A.

Subjects
Nuclear magnetic resonance -- Usage, Epidermal growth factor -- Research, Biological sciences, Chemistry
Abstract

The NMR backbone dynamics experiments are carried out on the individual fourth and fifth Epidermal Growth Factor (EGF)-like domains as well as on the wild type, the Met 388 Leu mutant, and the variant in which Met 388 is oxidized. The results presented show that changes at Met 388 cause significant changes in backbone dynamics in both the fourth and fifth EGF-like domains of thrombomodulin (TM).

Published
2005

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