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Journal Abstract Search

367 related items for PubMed ID: 10452612

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  • 3. Three-dimensional solution structure and stability of phage 434 Cro protein.
    Padmanabhan S, Jiménez MA, Gonzalez C, Sanz JM, Giménez-Gallego G, Rico M.
    Biochemistry; 1997 May 27; 36(21):6424-36. PubMed ID: 9174359
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  • 4. Folding propensities of peptide fragments of myoglobin.
    Reymond MT, Merutka G, Dyson HJ, Wright PE.
    Protein Sci; 1997 Mar 27; 6(3):706-16. PubMed ID: 9070453
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  • 7. Secondary structure switching in Cro protein evolution.
    Newlove T, Konieczka JH, Cordes MH.
    Structure; 2004 Apr 27; 12(4):569-81. PubMed ID: 15062080
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  • 9. Equilibrium unfolding of dimeric and engineered monomeric forms of lambda Cro (F58W) repressor and the effect of added salts: evidence for the formation of folded monomer induced by sodium perchlorate.
    Maity H, Mossing MC, Eftink MR.
    Arch Biochem Biophys; 2005 Feb 01; 434(1):93-107. PubMed ID: 15629113
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  • 10. Secondary structure and oligomerization behavior of equilibrium unfolding intermediates of the lambda cro repressor.
    Fabian H, Fälber K, Gast K, Reinstädler D, Rogov VV, Naumann D, Zamyatkin DF, Filimonov VV.
    Biochemistry; 1999 Apr 27; 38(17):5633-42. PubMed ID: 10220352
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  • 11. Contribution of a buried hydrogen bond to lambda repressor folding kinetics.
    Myers JK, Oas TG.
    Biochemistry; 1999 May 25; 38(21):6761-8. PubMed ID: 10346896
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  • 12. Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.
    Dyson HJ, Merutka G, Waltho JP, Lerner RA, Wright PE.
    J Mol Biol; 1992 Aug 05; 226(3):795-817. PubMed ID: 1507227
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  • 13. A comparative study of dynamic structures between phage 434 Cro and repressor proteins by normal mode analysis.
    Wako H, Tachikawa M, Ogawa A.
    Proteins; 1996 Sep 05; 26(1):72-80. PubMed ID: 8880931
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  • 14. Folding kinetics of a fluorescent variant of monomeric lambda repressor.
    Ghaemmaghami S, Word JM, Burton RE, Richardson JS, Oas TG.
    Biochemistry; 1998 Jun 23; 37(25):9179-85. PubMed ID: 9636065
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  • 15. Differences in the structural stability and cooperativity between monomeric variants of natural and de novo Cro proteins revealed by high-pressure Fourier transform infrared spectroscopy.
    Imamura H, Isogai Y, Kato M.
    Biochemistry; 2012 May 01; 51(17):3539-46. PubMed ID: 22482462
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  • 16. Kinetic role of helix caps in protein folding is context-dependent.
    Kapp GT, Richardson JS, Oas TG.
    Biochemistry; 2004 Apr 06; 43(13):3814-23. PubMed ID: 15049688
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  • 17. Contribution of increased length and intact capping sequences to the conformational preference for helix in a 31-residue peptide from the C terminus of myohemerythrin.
    Reymond MT, Huo S, Duggan B, Wright PE, Dyson HJ.
    Biochemistry; 1997 Apr 29; 36(17):5234-44. PubMed ID: 9136885
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  • 18. Design and synthesis of sequence-specific DNA-binding peptides.
    Grokhovsky SL, Surovaya AN, Brussov RV, Chernov BK, Sidorova NYu, Gursky GV.
    J Biomol Struct Dyn; 1991 Apr 29; 8(5):989-1025. PubMed ID: 1878171
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  • 19. Relationship between sequence determinants of stability for two natural homologous proteins with different folds.
    Van Dorn LO, Newlove T, Chang S, Ingram WM, Cordes MH.
    Biochemistry; 2006 Sep 05; 45(35):10542-53. PubMed ID: 16939206
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  • 20. Two peptide fragments G55-I72 and K97-A109 from staphylococcal nuclease exhibit different behaviors in conformational preferences for helix formation.
    Wang M, Shan L, Wang J.
    Biopolymers; 2006 Oct 15; 83(3):268-79. PubMed ID: 16767771
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