Proteins peptide interaction

Jain, S., Kumar, C.V., Kalonia, D.S. (1992). Protein-peptide interactions as probed by tryptophan fluorescence Serum albumins and enkephalin metabolites. Pharm. Res., 9, 990-992. 

RQA were thermal stability, protein-peptide interactions, and folding behavior. 

Discovery of Small Molecule Ligands Inhibiting Protein-Peptide Interactions Through SAR-by-NMR. 

Johnson, M. A. and Pinto, B. M. (2004) NMR spectroscopic and molecular modeling studies of protein-carbohydrate and protein-peptide interactions. Carbohydr. Res. 339, 907-928. 

The formation of a /3-sheet has been frequently observed in protein-peptide interactions, such as substrate recognition by certain serine proteases (Tong et at, 1998) and peptide recognition by the PTB and PDZ domains (Kuriyan and Cowbum, 1997). Detailed analysis further revealed that the central portion of the receptor peptide (P 2> Po>... 

Pi positions) is more twisted than a regular /3-strand to possess the polyproline II (PPII) helix conformation. The PPII conformation is also frequently used in protein-peptide interactions such as those seen in the peptide recognition by SH3 domains (Lim et at, 1994) and class II MHC molecules (Stem et at, 1994). This conformation allows the peptide chain to twist in order to maximize the interaction of its side chains with a protein surface. As a consequence, large proportions of the side chains at the P 2 Po 3.nd Pi positions of the receptor peptides are buried at the TRAF2 interface. Therefore, in the case of TRAF2-receptor interactions, the main chain hydrogen bonds and the PPII conformation maximize both main chain and side chain interactions with the TRAF2 surface. 

Binding Free Energies Using Continuum Methods Application to MHC Class I Protein-Peptide Interactions. 

Varadarajan, R., Connelly, P. R., Stur-tevant, J. M., and Richards, F. M. (1992) Heat capacity changes for protein-peptide interactions in the ribonuclease S System. Biochemistry 31, 1421-1426. 

Mikuni J et al (2010) A fluorescence correlation spectroscopy-based assay for fragment screening of slowly inhibiting protein-peptide interaction inhibitors. Anal Biochem 402(1) 26-31... 

M. Yang, Z. Wu, S. Fields, Protein-peptide interactions analyzed with the yeast two-hybrid system, Nucleic Acids Res. 1995, 23,... 

Froloff, N., Windemuth, A., and Flonig, B. (1997). On the calculation of binding free energies using continuum methods Application to MHC class 1 protein-peptide interactions. Protein Sci. 6(6), 1293-1301. 

The yeast two-hybrid system detects protein-protein or protein-peptide interactions in vivo. The target or bait protein and the ligand library are fused to either the DNA-binding domain or the transcription activation domain. Yeast cells are transformed with both plasmids and only the transformants expressing the protein-ligand interaction are selected (Y2). The main advantage is the one-step in vivo screening however, the library size is limited to about lO because of the transformation efficiency of the cells. 

So far, NECEEM was used to study the interaction between several proteins and DNA such as an Escherichia coli single-stranded DNA-binding protein (SSB) and a fluorescently labeled oligonucleotide (ssDNA), Taq DNA polymerase and its aptamer, thrombin and its aptamer, Tau protein and single-stranded and double-stranded DNA, protein farnesyltransferase (PFTase) and its aptamer, MutS protein and its aptamer, h-Ras protein and its aptamer, and Mef2c protein and double-stranded DNA it naturally binds. It has also been used to study protein-peptide interactions. ... 

R 452 M. A. Johnson and B. M. Pinto, NMR Spectroscopic and Molecular Modeling Studies of Protein-Carbohydrate and Protein-Peptide Interactions , Carbohyd. Res., 2004,339,907... 

R. Varadaraj P. Connelly, J. Sturtevant, and F. Richards, Biochenustry, 31,1421 (1992). Heat Capadty Changes for Protein-Peptide Interactions in the Ribonuclea e-S System. 

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