Results 281 to 290 of about 27,575 (332)
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NMR Spectroscopy of Paramagnetic Metalloproteins
ChemBioChem, 2005AbstractThis article deals with the solution structure determination of paramagnetic metalloproteins by NMR spectroscopy. These proteins were believed not to be suitable for NMR investigations for structure determination until a decade ago, but eventually novel experiments and software protocols were developed, with the aim of making the approach ...
José Malanho Silva +2 more
exaly +5 more sources
Moving metals: How microbes deliver metal cofactors to metalloproteins
Molecular Microbiology, 2023First row d‐block metal ions serve as vital cofactors for numerous essential enzymes and are therefore required nutrients for all forms of life. Despite this requirement, excess free transition metals are toxic.
D. E. Kunkle, Eric P. Skaar
semanticscholar +1 more source
Cross-talk Between (Hydrogen)Sulfite and Metalloproteins: Impact on Human Health.
Chemistry, 2022Sulfite is a potent toxic substance causing harm to multi-organ in human. Despite toxicity, it is widely used as preservative, anti-browning and anti-oxidant in foods, beverages, and pharmaceuticals, which cause easy admission of sulfite in human ...
Biplab K. Maiti
semanticscholar +1 more source
Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers
Chemical Reviews, 2014 Redox reactions play important roles in almost all biological processes, including photosynthesis and respiration, which are two essential energy processes that sustain all life on earth.
Saumen Chakraborty +2 more
exaly +2 more sources
Multiscale Quantum Refinement Approaches for Metalloproteins.
Journal of Chemical Theory and Computation, 2021Biomolecules with metal ion(s) (e.g., metalloproteins) play many important biological roles. However, accurate structural determination of metalloproteins, particularly those containing transition metal ion(s), is challenging due to their complicated ...
Zeyin Yan, Xin Li, L. Chung
semanticscholar +1 more source
An efficient, step-economical strategy for the design of functional metalloproteins
Nature Chemistry, 2019 The bottom-up design and construction of functional metalloproteins remains a formidable task in biomolecular design. Although numerous strategies have been used to create new metalloproteins, pre-existing knowledge of the tertiary and quaternary protein
Jonathan Rittle +2 more
exaly +2 more sources
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
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.
K.K. Rao, D.O. Hall, R. Cammack
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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
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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
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