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Comparison of the experimentally observed retention times with those predicted from the summated hydrophobicity coefficients suggests that these approaches can in some special circumstances provide a reasonably accurate estimation of the elution profile. Various amino acid hydrophobicity coefficient scales derived from both chromatographic and octanol-water partition studies are listed in Table 3. Such prediction schemes have been used successfully to identify antigenic recognition sites at the surface of proteins of unknown three-dimensional structures. Statistical surveys on the exposure to solvent of amino acid side chains in globular proteins have been used to arrive at special amino acid hydrophobicity scales, which in turn can be used to predict the exposure of peptide segments in proteins of unknown structure. (1982) The structural dependence of amino acid hydrophobicity parameter.
#Hydrophobic amino acids in membrane free
ProTherm (16) is a large collection of thermodynamic data on protein stability, which has information on 1) protein sequence and stmcture (2) mutation details ( wild-type and mutant amino acid hydrophobic to polar, charged to hydrophobic, aliphatic to aromatic, etc.), 3) thermodynamic data obtained from thermal and chemical denaturation experiments ( free energy change, transition temperature, enthalpy change, heat capacity change, etc.), 4) experimental methods and conditions (pH, temperature, buffer and ions, measurement and method, etc.), 5) functionality ( enzyme activity, binding constants, etc.), and 6) literature. Other sites of tissue factor expression include activated monocytes, activated endothelial cells, and atherosclerotic plaques. The tissue factor molecule consists of a 219 amino acid hydrophilic extracellular domain, a 23 amino acid hydrophobic region that spans the membrane, and a 21 amino acid cytoplasmic tail that anchors the molecule to the cell membrane (15,16). An intact endothelium normally shields the circulating blood from exposure to tissue factor. Tissue factor is a transmembrane glycoprotein, which is normally expressed by subendothelial fibroblast-like cells, which surround the blood vessel. The extrinsic pathway of coagulation is activated when circulating factor VII encounters tissue factor. Physicochemical basis of amino acid hydrophobicity scales Evaluation of four new scales of amino acid hydrophobicity coefficients derived from RP-HPLC of peptides. Wilce, M.C J., Aguilar, M.-L, and Heam, T.W. Hydrophobic amino acids are known to produce a bitterness. It displays a tyrosine kinase domain, which includes several tyrosine autophosphorylation sites, and an actin-binding domain that may facilitate interaction with the cell cytoskeleton.īitterness of 0- Aminoacyl Sugars Containing Hydrophobic Amino Acids. The receptor cytoplasmic region contains some 542 amino acids. A 23 amino acid hydrophobic domain spans the plasma membrane.
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It displays two cysteine-rich regions, between which the ligand-binding domain is located. The N-terminal, extracellular region of the receptor contains 622 amino acids. Amino acid hydrophobic Figure 10.7 The EGF receptor.