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The structure of the pyridine complex has been determined crystallographically. [2] Adducts with other N-heterocycles have also been characterized similarly. [3] Aqueous chromium(VI) oxide peroxide decomposes in a few seconds, turning green as chromium(III) compounds are formed. [4] 2 CrO(O 2) 2 + 7 H 2 O 2 + 6 H + → 2 Cr 3+ + 10 H 2 O + 7 O 2
A protein structure database is a database that is modeled around the various experimentally determined protein structures. The aim of most protein structure databases is to organize and annotate the protein structures, providing the biological community access to the experimental data in a useful way.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
Early attempts at using in-cell NMR to study protein quinary structure were hindered by a limitation caused by the very phenomenon they were trying to understand. Many probe proteins tested in these experiments turned out to produce broad signals, near the detection limit of the method, when measured inside cells of Escherichia coli. In ...
The CCR5 protein belongs to the beta chemokine receptors family of integral membrane proteins. [12] [13] It is a G protein–coupled receptor [12] which functions as a chemokine receptor in the CC chemokine group. CCR5's cognate ligands include CCL3, CCL4 (also known as MIP 1α and 1β, respectively), and CCL3L1.
structure summary In molecular biology, the Cro repressor family is a family of repressor proteins in bacteriophage lambda that includes the Cro repressor. Bacteriophage lambda encodes two repressors: the Cro repressor that acts to turn off early gene transcription during the lytic cycle , and the lambda or cI repressor required to maintain ...
Crystal structure of CRMP-1. CRMP1-5 are between 564 and 572 amino acids and these proteins are found to be approximately 95% conserved between mouse and human. [6] The protein sequence of CRMP1-4 is approximately 75% homologous with each other, while CRMP5 is only 50-51% homologous with each of the other CRMPs. [4]
[2] [3] Each armadillo repeat is composed of a pair of alpha helices that form a hairpin structure. Multiple copies of the repeat form what is known as an alpha solenoid structure. Examples of proteins that contain armadillo repeats include β-catenin, Sarm1 , [4] α-importin, [5] plakoglobin, [6] adenomatous polyposis coli (APC), [7] and many ...