Small hydrophobic protein

Five fused water pentagons forming a clathrate-like structure are the predominant feature in the hydration of crambin, a small hydrophobic protein of molecular weight 4720 [811, 844]. 

Fuentes S, Tran KC, Futhra P et al (2007) Function of the respiratory syncytial virus small hydrophobic protein. J Virol 81 8361-8366... 

It should be mentioned that the single-stranded ENA genome of the plant virus, cowpea mosaic virus has also been found to be covalently linked to a small, hydrophobic protein (G. Bruening, personal communication). 

Rixon HW, Brown G, Murray JT et al (2005) The respiratory syncytial virus small hydrophobic protein is phosphorylated via a mitogenactivated protein kinase p38-dependent tyrosine kinase activity during virus infection. 1 Gen Virol 86 375-384 Robin V, Irurzun A, Amoros M et al (2001) AntipoUovirus flavonoids from Psiadia dentata. Antivir Chem Chemother 12 283-291... 

Godovac-Zimmerman, J. The structural motif of p-lactoglobulin and retinol-binding protein a basic framework for binding and transport of small hydrophobic molecules Trends Biochem. Sci. 

Ionic interactions between solutes and Superose are negligible at ionic strengths above 50 mM. However, some hydrophobic interactions have been observed with small hydrophobic peptides, membrane proteins, and lipopro-... 

However, analysis of protein mixtures derived from cells, tissues, and body fluids by 2D PAGE by no means represents a comprehensive picture of the proteins in the mixture. Proteins with extreme isoelectric points, large proteins, small proteins, and hydrophobic proteins are commonly not amenable to 2D PAGE and hence can be easily missed. Furthermore, low abundant proteins are often not detected in 2D gels when proteins of high abundance are present. This limitation is particularly relevant when analyzing serum or other body fluids, where protein amounts vary by ten orders of magnitude (Anderson and Anderson 1998). 

In the digestive system trypsin, chymotrypsin, and elastase work as a team. They are all endopeptidases, which means that they cleave protein chains at internal peptide bonds, but each preferentially hydrolyses bonds adjacent to a particular type of amino acid residue (fig. 8.4). Trypsin cuts just next to basic residues (lysine or arginine) chymotrypsin cuts next to aromatic residues (phenylalanine, tyrosine, or tryptophan) elastase is less discriminating but prefers small, hydrophobic residues such as alanine. 

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