Results 211 to 220 of about 14,121 (262)
A supramolecular assembly enables discrimination between metalloproteins and non-metalloproteins
Chemical Communications, 2018 A supramolecular assembly yields turn-on fluorescence response for non-metalloproteins and turn-off response for metalloproteins.
Aafrin M, Pettiwala, Prabhat K, Singh
openaire +3 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Inorganic Chemistry, 2004
One of the most intriguing problems in the biological sciences is the question of how to predict protein structure and function based on knowledge of a gene sequence. While significant progress has been made toward this goal during the past decade, fundamental challenges remain, such as understanding important post-translational modifications.
Bren, Kara L. +2 more
openaire +3 more sources
One of the most intriguing problems in the biological sciences is the question of how to predict protein structure and function based on knowledge of a gene sequence. While significant progress has been made toward this goal during the past decade, fundamental challenges remain, such as understanding important post-translational modifications.
Bren, Kara L. +2 more
openaire +3 more sources
Proteomic tools for the analysis of transient interactions between metalloproteins
FEBS Journal, 2011 Metalloproteins play major roles in cell metabolism and signalling pathways. In many cases, they show moonlighting behaviour, acting in different processes, depending on the physiological state of the cell.
Jonathan Martinez-Fabregas +2 more
exaly +2 more sources
2013
Paramagnetic metalloproteins are proteins containing one or more paramagnetic metal ions, which are characterized by the presence of at least one unpaired electron. As in every molecule, unpaired electrons sizably perturb the NMR parameters relative to the protein nuclei, changing their relaxation, chemical shift, and motional averaging so that ...
BERTINI, IVANO, PARIGI, GIACOMO
openaire +2 more sources
Paramagnetic metalloproteins are proteins containing one or more paramagnetic metal ions, which are characterized by the presence of at least one unpaired electron. As in every molecule, unpaired electrons sizably perturb the NMR parameters relative to the protein nuclei, changing their relaxation, chemical shift, and motional averaging so that ...
BERTINI, IVANO, PARIGI, GIACOMO
openaire +2 more sources
, 1992 With the success of chemical syntheses and purification of large polypeptides ( > 50 amino acid residues) attention now focuses on developing protocols to correctly fold these products to generate species with high levels of bioactivity.
John M. Tomich, John H. Richards
openaire +2 more sources
Current Opinion in Biotechnology, 1996
The rational design of novel proteins offers a new method of studying structure and function, and makes possible the construction of new biomaterials. The richness of metal chemistry, the relative ease of creating stable complexes, and the remarkable degree of subtle, highly specific control of reactivity imposed by the protein matrix upon the metal ...
openaire +2 more sources
The rational design of novel proteins offers a new method of studying structure and function, and makes possible the construction of new biomaterials. The richness of metal chemistry, the relative ease of creating stable complexes, and the remarkable degree of subtle, highly specific control of reactivity imposed by the protein matrix upon the metal ...
openaire +2 more sources
Predicting cracks in metalloproteins
Nature Machine Intelligence, 2019Loss-of-function mutations in metal-binding proteins are heavily implicated with numerous diseases, and identifying such ‘cracks’ will be valuable to biologists and medical doctors in the study and treatment of disease. A deep learning approach has been developed to tackle this challenging task.
Yuan Liu, Chu Wang
openaire +1 more source
Metalloproteins in the evolution of photosynthesis
Biosystems, 1981Certain metalloproteins are common to all photosynthetic electron transfer chains. These include soluble proteins such as ferredoxins and cytochromes of the c2 type, and membrane-bound components such as cytochrome b, c1 and the Rieske iron-sulphur protein.
R, Cammack, K K, Rao, D O, Hall
openaire +2 more sources