VAL-TRP CAS NO 24587-37-9 C19H18N2O5

Appearance: White or almost white powder 

PURITY: 95% MIN.

WATER CONTENT: 8% MAX

Trp Val is a peptide containing the amino acids tryptophan (Trp) and valine (Val). It has the ability to interact with voltage dependent calcium channels (VDCC) and contribute to vasodilation in vascular muscle cells

The five residues that form Ar/R SF are diverse

The four residues from the TM2 and TM5 helices, as well as the ring LE, form one of the contraction sites in the MIP channel. As the name suggests, this narrow region is composed of aromatic and arginine residues, which contribute to the selectivity of solutes transported through channels. The knowledge of Ar/R SF residues derived from homologous models has been used to derive structural subclasses of MIP channels (Bansal&Sankaramarakrishnan, 2007; Gupta and Sankaramarakrishnan, 2009; Verma et al., 2014b; Wallace&Roberts (2004). The arginine at position 53 is mostly conserved in MIP channels. The mutation at this position in the tonoplast intrinsic protein subfamily of plant MIPs indicates that the residue at position LE.53 plays a critical role (Azad, Yoshikawa, Ishikawa, Sawa,&Shibata, 2012). In another study, it has been shown that site directed mutagenesis at position 5.57 in the MIP channel of Arabidopsis and rice, belonging to the nodulin-26 like endogenous protein (NIPs) family, revealed the crucial role played by this residue in the TM5 helix (Mitani Ueno, Yamaji, Zhao,&Ma, 2011). Both mutation and simulation studies emphasize the Ar/R SF region responsible for hindering proton permeation in the AQP1 channel (Li et al., 2011). Molecular dynamics simulations of AQP1 and AQP4 channels have shown that arginine at the LE.53 position can adopt two different conformational states based on electrostatic potential, thereby regulating the water flux on the membrane (Hub, Aponte-Santamaria，Grubmuller，&de Groot，2010）


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