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Crystal structure of plant photosystem I
Oxygenic photosynthesis is the principal producer of both oxygen and organic matter on Earth. The conversion of sunlight into chemical energy is driven by two multisubunit membrane protein complexes… Expand
Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the… Expand
The a/ hydrolase fold
Method and apparatus for performing 2-bit, non-restore, look-ahead, binary division for a digital processor wherein 2 quotient bits are generated simultaneously during one adder cycle; the cycle… Expand
Halophilic enzymes: proteins with a grain of salt.
Halophilic enzymes, while performing identical enzymatic functions as their non-halophilic counterparts, have been shown to exhibit substantially different properties, among them the requirement for… Expand
The alpha/beta hydrolase fold.
We have identified a new protein fold--the alpha/beta hydrolase fold--that is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each… Expand
Structure of a unique twofold symmetric haem-binding site
Bacterioferritin of Escherichia coli, also known as cytochrome b1, is a hollow, nearly spherical shell made up of 24 identical protein subunits and 12 haems. We have solved this structure in a… Expand
Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin
- F. Frolow, Michal Harel1, J. Sussman, M. Mevarech, M. Shoham
- Chemistry, Medicine
- Nature Structural Biology
- 1 May 1996
Haloarcula marismortui is an archaebacterium that flourishes in the world's saltiest body of water, the Dead Sea. The cytosol of this organism is a supersaturated salt solution in which proteins are… Expand
NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii.
- Y. Korkhin, A. Kalb(gilboa), M. Peretz, O. Bogin, Y. Burstein, F. Frolow
- Chemistry, Medicine
- Journal of molecular biology
- 22 May 1998
We have determined the X-ray structures of the NADP(H)-dependent alcohol dehydrogenase of Clostridiim beijerinckii (CBADH) in the apo and holo-enzyme forms at 2.15 A and 2.05 A resolution,… Expand
Molecular Basis of the High Insecticidal Potency of Scorpion α-Toxins*
Scorpion α-toxins are similar in their mode of action and three-dimensional structure but differ considerably in affinity for various voltage-gated sodium channels (NaChs). To clarify the molecular… Expand
Crystal structure of the human mitochondrial chaperonin symmetrical football complex
- S. Nisemblat, O. Yaniv, A. Parnas, F. Frolow, A. Azem
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 27 April 2015
Significance The human mitochondrial chaperonin is vital for proper cell function because it assists in folding of mitochondrial proteins. Additionally, it participates in extramitochondrial… Expand