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Journal Abstract Search

441 related items for PubMed ID: 19658436

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  • 2. Use of the novel fluorescent amino acid p-cyanophenylalanine offers a direct probe of hydrophobic core formation during the folding of the N-terminal domain of the ribosomal protein L9 and provides evidence for two-state folding.
    Aprilakis KN, Taskent H, Raleigh DP.
    Biochemistry; 2007 Oct 30; 46(43):12308-13. PubMed ID: 17924662
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  • 3. Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation.
    Taskent-Sezgin H, Marek P, Thomas R, Goldberg D, Chung J, Carrico I, Raleigh DP.
    Biochemistry; 2010 Jul 27; 49(29):6290-5. PubMed ID: 20565125
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  • 4. Surface salt bridges, double-mutant cycles, and protein stability: an experimental and computational analysis of the interaction of the Asp 23 side chain with the N-terminus of the N-terminal domain of the ribosomal protein l9.
    Luisi DL, Snow CD, Lin JJ, Hendsch ZS, Tidor B, Raleigh DP.
    Biochemistry; 2003 Jun 17; 42(23):7050-60. PubMed ID: 12795600
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  • 5. Mutational analysis of the folding transition state of the C-terminal domain of ribosomal protein L9: a protein with an unusual beta-sheet topology.
    Li Y, Gupta R, Cho JH, Raleigh DP.
    Biochemistry; 2007 Jan 30; 46(4):1013-21. PubMed ID: 17240985
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  • 7. Study protein folding and aggregation using nonnatural amino acid p-cyanophenylalanine as a sensitive optical probe.
    Du D, Liu H, Ojha B.
    Methods Mol Biol; 2013 Jan 30; 1081():77-89. PubMed ID: 24014435
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  • 9. Role of the amino acid sequence in domain swapping of the B1 domain of protein G.
    Sirota FL, Héry-Huynh S, Maurer-Stroh S, Wodak SJ.
    Proteins; 2008 Jul 30; 72(1):88-104. PubMed ID: 18186476
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  • 10. Probing protein folding using site-specifically encoded unnatural amino acids as FRET donors with tryptophan.
    Miyake-Stoner SJ, Miller AM, Hammill JT, Peeler JC, Hess KR, Mehl RA, Brewer SH.
    Biochemistry; 2009 Jun 30; 48(25):5953-62. PubMed ID: 19492814
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  • 11. Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability.
    Anil B, Song B, Tang Y, Raleigh DP.
    J Am Chem Soc; 2004 Oct 20; 126(41):13194-5. PubMed ID: 15479052
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  • 13. Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state.
    Wallgren M, Adén J, Pylypenko O, Mikaelsson T, Johansson LB, Rak A, Wolf-Watz M.
    J Mol Biol; 2008 Jun 13; 379(4):845-58. PubMed ID: 18471828
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  • 14. Estimation of Förster's distance between two ends of Dps protein from mycobacteria: distance heterogeneity as a function of oligomerization and DNA binding.
    Chowdhury RP, Chatterji D.
    Biophys Chem; 2007 Jun 13; 128(1):19-29. PubMed ID: 17368913
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  • 18. Advanced approaches for the characterization of a de novo designed antiparallel coiled coil peptide.
    Pagel K, Seeger K, Seiwert B, Villa A, Mark AE, Berger S, Koksch B.
    Org Biomol Chem; 2005 Apr 07; 3(7):1189-94. PubMed ID: 15785806
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