Results 11 to 20 of about 305,158 (217)
Texture and Cofactor Zeros of the Neutrino Mass Matrix [PDF]
JHEP 1409:013,2014, 2013 We study Majorana neutrino mass matrices that have two texture zeros, or two cofactor zeros, or one texture zero and one cofactor zero. The two texture/cofactor zero conditions give four constraints, which in conjunction with the five measured oscillation parameters completely determine the nine independent real parameters of the neutrino mass matrix ...
Liao, Jiajun, Marfatia, D., Whisnant, K.
arxiv +3 more sources
Non-Hamiltonian systems separable by Hamilton-Jacobi method [PDF]
, 2007 We show that with every separable calssical Stackel system of Benenti type on a Riemannian space one can associate, by a proper deformation of the metric tensor, a multi-parameter family of non-Hamiltonian systems on the same space, sharing the same trajectories and related to the seed system by appropriate reciprocal transformations.
Beltrami +20 more
arxiv +3 more sources
Taylor Expansion Proof of the Matrix Tree Theorem - Part I [PDF]
arXiv, 2013 The Matrix-Tree Theorem states that the number of spanning trees of a graph is given by the absolute value of any cofactor of the Laplacian matrix of the graph. We propose a very short proof of this result which amounts to comparing Taylor expansions.
Zernik, Amitai
arxiv +2 more sources
Count and cofactor matroids of highly connected graphs [PDF]
Journal of Combinatorial Theory, Series B, 2024, 2022 We consider two types of matroids defined on the edge set of a graph $G$: count matroids ${\cal M}_{k,\ell}(G)$, in which independence is defined by a sparsity count involving the parameters $k$ and $\ell$, and the (three-dimensional generic) cofactor matroid $\mathcal{C}(G)$, in which independence is defined by linear independence in the cofactor ...
arxiv +1 more source
The CoFactor database: organic cofactors in enzyme catalysis [PDF]
Bioinformatics, 2010 Abstract Motivation: Organic enzyme cofactors are involved in many enzyme reactions. Therefore, the analysis of cofactors is crucial to gain a better understanding of enzyme catalysis. To aid this, we have created the CoFactor database. Results: CoFactor provides a web interface to access hand-curated data extracted from ...
Gemma L. Holliday +2 more
openaire +3 more sources
Peroxisomal Cofactor Transport [PDF]
Biomolecules, 2020 Peroxisomes are eukaryotic organelles that are essential for growth and development. They are highly metabolically active and house many biochemical reactions, including lipid metabolism and synthesis of signaling molecules. Most of these metabolic pathways are shared with other compartments, such as Endoplasmic reticulum (ER), mitochondria, and ...
Anastasija Plett +2 more
openaire +3 more sources
Biosynthesis of Nitrogenase Cofactors [PDF]
Chemical Reviews, 2020 Nitrogenase harbors three distinct metal prosthetic groups that are required for its activity. The simplest one is a [4Fe-4S] cluster located at the Fe protein nitrogenase component. The MoFe protein component carries an [8Fe-7S] group called P-cluster and a [7Fe-9S-C-Mo-R-homocitrate] group called FeMo-co.
Stefan Burén +3 more
openaire +4 more sources
Identification of YdhV as the first molybdoenzyme binding a Bis-Mo-MPT cofactor in escherichia coli [PDF]
, 2019 The oxidoreductase YdhV in Escherichia coli has been predicted to belong to the family of molybdenum/tungsten cofactor (Moco/Wco)-containing enzymes. In this study, we characterized the YdhV protein in detail, which shares amino acid sequence homology ...
Dau, Holger +7 more
core +1 more source
Studies on the changes in protein fluorescence and enzymic activity of aspartate aminotransferase on binding of pyridoxal 5'-Phosphate [PDF]
, 1974 1. The a and ,B subforms of aspartate aminotransferase were purified from pig heart. 2. The a subform contained 2mol of pyridoxal 5'-phosphate. The apo-(a subform) could be fully reactived by combination with 2mol of cofactor. 3.
Evans, RW, Holbrook, J
core +2 more sources
Journal of Biological Chemistry, 2013 The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase.
openaire +3 more sources