Surface interaction with proteins

Karlsson R, Fait A (1997) Experimental design for kinetic analysis of protein-protein interactions with surface plasmon resonance biosensors. J Immunol Methods 200(1—2) 121—133... 

WALTON and KOLTISKO Protein Interaction with Surfaces... 

Szott LM, Horbett TA. Protein interactions with surfaces cellular responses, complement activation, and newer methods. Curr Opin Chem Biol 2011 15(5) 677-82. 

Szott, L. M., Horbett, T. A. (2011). Protein interactions with surfaces Computational approaches and repellency. Current Opinion in Chemical Biology, 15, 683-689. http //dx.doi.org/ 0.1016/j. cbpa.2011.04.016. 

Biomolecules interact with one another through molecular surfaces that are structurally complementary. How can various proteins interact with molecules as different as simple ions, hydrophobic lipids, polar but uncharged carbohydrates, and even nucleic acids ... 

In the nucleosome, the DNA is supercoiled in a left-handed helix over the surface of the disk-shaped histone octamer (Figure 36-2). The majority of core histone proteins interact with the DNA on the inside of the supercoil without protruding, though the amino terminal tails of all the histones probably protrude outside of this structure and are available for regulatory covalent modifications (see Table 36-1). 

New developments in immobilization surfaces have lead to the use of SPR biosensors to monitor protein interactions with lipid surfaces and membrane-associated proteins. Commercially available (BIACORE) hydrophobic and lipophilic sensor surfaces have been designed to create stable membrane surfaces. It has been shown that the hydrophobic sensor surface can be used to form a lipid monolayer (Evans and MacKenzie, 1999). This monolayer surface can be used to monitor protein-lipid interactions. For example, a biosensor was used to examine binding of Src homology 2 domain to phosphoinositides within phospholipid bilayers (Surdo et al., 1999). In addition, a lipophilic sensor surface can be used to capture liposomes and form a lipid bilayer resembling a biological membrane. 

Maurel, D., Kniazeff, J., Mathis, G., Trinquet, E., Pin, J. P. and Ansanay, FI. (2004). Cell surface detection of membrane protein interaction with homogeneous time-resolved fluorescence resonance energy transfer technology. Anal. Biochem. 329, 253-62. 

Brockman JM, Fmtos AG, Com RM (1999) A multistep chemical modification procedure to create DNA arrays on gold surfaces for the study of protein-DNA interactions with surface plasmon resonance imaging. J Am Chem Soc 121 8044-8051... 

In the PPA-a-AI 1 complex, a flexible loop of the enzyme, which would normally contact the substrate, is pushed outward to allow entry of the inhibitor, and one of the key aspartate residues is held in a conformation similar to that observed in the free enzyme. Therefore, some changes relative to the carbohydrate complex are required in order to accommodate the inhibitor. The structurally mimetic interactions within the catalytic site are supplemented by other specific protein-protein interactions, with a substantial buried surface area at the interface, involving 50 residues of the enzyme [171]. 

Protein molecules have a high propensity to interact with surfaces, making them susceptible to adsorption and denaturation at air-liquid, vial-liquid, and liquid-liquid... 

F1GURE 5-22 Structure of a human class I MHC protein, (a) This model is derived in part from the known structure of the extracellular portion of the protein (PDB ID 1 DDH). The a chain of MHC is shown in gray the small /3 chain is blue the disulfide bonds are yellow. A bound ligand, a peptide derived from HIV, is shown in red. (b) Top view of the protein, showing a surface contour image of the site where peptides are bound and displayed. The HIV peptide (red) occupies the site. This part of the class I MHC protein interacts with T-cell receptors. 

---