54907-61-8 Usage
Description
IODOACETIC ANHYDRIDE is an organic compound that is primarily used as a reagent in various chemical and biological applications. It is known for its golden flake appearance and is characterized by its ability to act as a linker and reactant in the synthesis of various compounds.
Uses
Used in Chemical Synthesis:
IODOACETIC ANHYDRIDE is used as a reactant for the synthesis of N-iodoacetyl glycosylamine derivatives and converting amino precursors to IA derivatives. It plays a crucial role in the development of reagents used for differential protein quantitation via ion scanning.
Used in Pharmaceutical Industry:
IODOACETIC ANHYDRIDE is used as a linker for linking lysine residues to N-terminal α-amino groups of peptides. This application is significant in the development of new drugs and therapeutic agents.
Used in Biochemical Research:
IODOACETIC ANHYDRIDE is used for capping amines and yielding a thiol reactive iodo-derivative. This property makes it a valuable tool in biochemical research, particularly in the study of protein structure and function.
Used in Protein Modification:
IODOACETIC ANHYDRIDE is employed in the process of iodoacetylation, which involves the modification of proteins by introducing an iodoacetyl group. This modification can be used to study protein interactions, stability, and function.
Check Digit Verification of cas no
The CAS Registry Mumber 54907-61-8 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,4,9,0 and 7 respectively; the second part has 2 digits, 6 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 54907-61:
(7*5)+(6*4)+(5*9)+(4*0)+(3*7)+(2*6)+(1*1)=138
138 % 10 = 8
So 54907-61-8 is a valid CAS Registry Number.
InChI:InChI=1/C4H4I2O3/c5-1-3(7)9-4(8)2-6/h1-2H2
54907-61-8Relevant articles and documents
A superprotein triangle driven by nickel(II) coordination: Exploiting non-natural metal ligands in protein self-assembly
Radford, Robert J.,Tezcan, F. Akif
supporting information; experimental part, p. 9136 - 9137 (2009/12/06)
(Chemical Equation Presented) We previously devised a strategy (metal-directed protein self-assembly, MDPSA) that utilizes the simultaneous stability, lability, and directionality of metal-ligand bonds to drive protein-protein interactions. Here we show that both the structural and functional scopes of MDPSA can be broadened by incorporation of non-natural metal-chelating ligands onto protein surfaces. A cytochrome cb562 variant, MBP-Phen1, which features a covalently attached phenanthroline (Phen) group on its surface, self-assembles into an unusual triangular architecture (Ni3:MBP-Phen13) upon binding Ni as a result of specific Phen-protein interactions. The crystal structure of Ni3:MBP- Phen13 reveals that the Phen group is buried in a small pocket on the protein surface, which results in an unsaturated Ni coordination environment.