771490-16-5

Basic information

• Product Name: 3-(4-hydroxy-phenyl)-2-(2-mercapto-acetylamino)-N-methyl-propionamide
• Synonyms: 3-(4-hydroxy-phenyl)-2-(2-mercapto-acetylamino)-N-methyl-propionamide
• CAS NO: 771490-16-5
• Molecular Weight: 268.337
• Mol File: 771490-16-5.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 3-(4-hydroxy-phenyl)-2-(2-mercapto-acetylamino)-N-methyl-propionamide(CAS DataBase Reference)
• NIST Chemistry Reference: 3-(4-hydroxy-phenyl)-2-(2-mercapto-acetylamino)-N-methyl-propionamide(771490-16-5)
• EPA Substance Registry System: 3-(4-hydroxy-phenyl)-2-(2-mercapto-acetylamino)-N-methyl-propionamide(771490-16-5)

Safety Data

• Hazardous Substances Data: 771490-16-5(Hazardous Substances Data)

Upstream product

• 2365-48-2 Methyl thioglycolate 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 934740-49-5 [2-(4-tert-butoxy-phenyl)-1-methylcarbamoyl-ethyl]-carbamic acid 9H-fluoren-9-ylmethyl ester 
• 101363-71-7 2-amino-3-(4-tert-butoxy-phenyl)-N-methyl-propionamide 
• 934740-57-5 3-(4-tert-butoxy-phenyl)-N-methyl-2-(2-tritylsulfanyl-acetylamino)-propionamide 

Downstream Products

• 2365-48-2 Methyl thioglycolate 

Relevant articles and documents

Side-chain pairing preferences in the parallel coiled-coil dimer motif: Insight on ion pairing between core and flanking sites

A new strategy for rapid evaluation of sequence-stability relationships in the parallel coiled-coil motif is described. The experimental design relies upon thiol-thioester exchange equilibria, an approach that is particularly well suited to examination of heterodimeric systems. Our model system has been benchmarked by demonstrating that it can quantitatively reproduce previously reported trends in interhelical a-a′ side-chain pairing preferences at the coiled-coil interface. This new tool has been used to explore the role of Coulombic interactions between a core position on one helix and a flanking position on the other helix (a-g′). This type of interhelical contact has received relatively little attention to date. Our results indicate that such interactions can influence coiled-coil partner preferences.

Stabilizing and destabilizing effects of phenylalanine → F 5-phenylalanine mutations on the folding of a small protein

We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe → F5-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe → F5-Phe mutations are interesting because aryl-perfluoroaryl interactions of optimal geometry are intrinsically more favorable than aryl-aryl interactions and because perfluoroaryl units are more hydrophobic than are analogous aryl units. One mutant, Phe-10 → F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability. Copyright