Zobrazeno 1 - 10
of 205
pro vyhledávání: '"G. McLendon"'
Publikováno v:
Food Science & Nutrition
Food Science & Nutrition, Vol 9, Iss 5, Pp 2658-2667 (2021)
Food Science & Nutrition, Vol 9, Iss 5, Pp 2658-2667 (2021)
Samples of 23 seafood products were obtained internationally in processing plants and subjected to controlled decomposition to produce seven discrete quality increments. A sensory expert evaluated each sample for decomposition, using a scale of 1–1
Publikováno v:
Journal of Food Safety. 39
Autor:
G McLendon, J Feitelson
Publikováno v:
Biochemistry. 30:5051-5055
It has previously been shown that the rates and activation energies for migration molecules of different sizes through myoglobin are very similar. The results were interpreted in terms of conformational changes in the protein structure that facilitat
Publikováno v:
Journal of molecular biology. 247(4)
The bacteriophage Mu Com protein is a small "zinc finger-like" protein that binds a specific site in com-mom operon mRNA and activates translation of the mom open-reading-frame. Com contains six cysteine and five histidine residues that have the pote
Publikováno v:
Journal of molecular biology. 236(3)
High resolution three-dimensional structures for the N52I and N52I-Y67F yeast iso-l-cytochrome c variants have been completed in both oxidation states. The most prominent structural difference observed in both mutant proteins is the displacement of a
Autor:
G, McLendon, J, Feitelson
Publikováno v:
Methods in enzymology. 232
Publikováno v:
Journal of molecular biology. 224(3)
Theoretical methods for correlation of sequence changes and redox potential of electron transport proteins are examined using the Asn52----Ile mutation in cytochrome c as a test case. The first approach uses the protein dipoles Langevin dipoles (PDLD
Autor:
G. McLendon
Publikováno v:
Long-Range Electron Transfer in Biology ISBN: 9783540532606
Some of the factors which control molecular recognition and binding between electron transfer proteins have been elucidated from studies of the interaction between cytochrome c and its redox partners, particularly cytochrome c peroxidase (ccp). Data
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b39728abdc70d5f71c59921685e505a
https://doi.org/10.1007/3-540-53260-9_6
https://doi.org/10.1007/3-540-53260-9_6
Picosecond Transient Phase Grating Studies of the Energetics and Structure Dynamics of Heme Proteins
Publikováno v:
Ultrafast Phenomena.
Large amplitude motions in proteins and biopolymers is a fundamental feature of the biological function of these systems. The mechanism of energy transduction from a stimulus, such as ligand binding or dissociation, to a specific protein motion assoc
Publikováno v:
Inorganic Chemistry. 14:2322-2326