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Elsevier BV
Journal of Molecular Biology (78)
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Petukhov, M., Muñoz, V., Yumoto, N., Yoshikawa, S., & Serrano, L. (1998). Position dependence of non-polar amino acid intrinsic helical propensities. Journal of Molecular Biology, 278(1), 279–289.

Authors 5
  1. Michael Petukhov (first)
  2. Victor Muñoz (additional)
  3. Noboru Yumoto (additional)
  4. Susumu Yoshikawa (additional)
  5. Luis Serrano (additional)
References 40 Referenced 61
  1. 10.1006/jmbi.1994.1052 / J. Mol. Biol. / Biased probability Monte-Carlo conformational searches and electrostatic calculations for peptides and proteins by Abagyan (1994)
  2. 10.1126/science.8178170 / Science / Rules for α-helix termination by glycine by Aurora (1994)
  3. 10.1002/prot.340100206 / Proteins: Struct. Funct. Genet. / Side chain backbone hydrogen bonding contributes to helix stability in peptides derived from an α-helical region of carboxypeptidase A by Bruch (1991)
  4. 10.1038/351586a0 / Nature / Large differences in the helix propensities of alanine and glycine by Chakrabartty (1991)
  5. 10.1021/bi00713a027 / Biochemistry / Determination of the helix and β-form of proteins in aqueous solution by circular dichroism by Chen (1974)
  6. 10.1002/prot.340190202 / Proteins: Struct. Funct. Genet. / α-Helix-forming propensities in peptides and proteins by Creamer (1994)
  7. 10.1002/pro.5560040708 / Protein Sci. / N- and C-capping preferences for all 20 amino acids in α-helical peptides by Doig (1995)
  8. 10.1002/jcc.540160303 / J. Comput. Chem. / The double cubic lattice method by Eisenhaber (1995)
  9. 10.1002/prot.340100403 / Proteins: Struct. Funct. Genet. / Physical reasons for secondary structure stability by Finkelstein (1991)
  10. 10.1016/0003-2697(89)90602-7 / Anal. Biochem. / Calculation of protein extinction coefficients from amino acid sequence data by Gill (1989)
  11. 10.1002/pro.5560050204 / Protein Sci. / A program to identify and analyse structural motifs in proteins by Hutchinson (1996)
  12. 10.1002/pro.5560021006 / Protein Sci. / Effect of a single aspartate on helix stability at different positions an a neutral alanine-base peptide by Huyghues-Despointes (1993)
  13. 10.1002/prot.340200108 / Proteins: Struct. Funct. Genet. / Estimation of changes in side chain configurational entropy in binding and folding by Lee (1994)
  14. 10.1080/07391102.1989.10507739 / J. Biomol. Struct. Dynam. / New methodology for computer-aided modelling of biomolecular structure and dynamics. 1. Non-cyclic structures by Mazur (1989)
  15. 10.1016/0022-2836(87)90314-7 / J. Mol. Biol. / Analysis of the relationship between side-chain conformation and secondary structure in globular proteins by McGregor (1987)
  16. 10.1006/jmbi.1997.0923 / J. Mol. Biol. / Estimating the relative populations of 310-helix and alpha-helix in Ala-rich peptides by Millhauser (1997)
  17. 10.1021/j100589a006 / J. Phys. Chem. / Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions and intrinsic torsional potentials for the naturally occurring amino acids by Momany (1975)
  18. 10.1002/prot.340200403 / Proteins: Struct. Funct. Genet. / Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices by Muñoz (1994)
  19. 10.1016/0958-1669(95)80066-2 / Curr. Opin. Biotechnol. / Helix design, prediction and stability by Muñoz (1995)
  20. 10.1006/jmbi.1994.0023 / J. Mol. Biol. / Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rotational modification of the helical content of natural peptides by Muñoz (1995)
  21. 10.1006/jmbi.1994.0024 / J. Mol. Biol. / Elucidating the folding problem of helical peptides using empirical parameters. III. Temperature and pH dependence by Muñoz (1995)
  22. 10.1021/bi00046a039 / Biochemistry / Analysis of i, i+5 and i, i+8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motif by Muñoz (1995)
  23. 10.1002/(SICI)1097-0282(19970415)41:5<495::AID-BIP2>3.0.CO;2-H / Biopolymers / Development of the multiple sequence approximation within the AGADIR model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms by Muñoz (1997)
  24. 10.1038/nsb0595-380 / Nature Struct. Biol. / The “hydrophobic staple” motif. A role for loop-residues in α-helix stability and protein folding by Muñoz (1995)
  25. 10.1073/pnas.94.7.2833 / Proc. Natl Acad. Sci. USA / A direct comparison of helix propensity in proteins and peptides by Myers (1997)
  26. 10.1021/j100234a011 / J. Phys. Chem. / Energy parameters in polypeptides. 9. Updating of geometrical parameters, nonbonded interactions and hydrogen bond interactions for the naturally occurring amino acids by Nemethy (1983)
  27. 10.1073/pnas.84.10.3086 / Proc. Natl Acad. Sci. USA / Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides by Oii (1987)
  28. 10.1006/jmbi.1994.1545 / J. Mol. Biol. / Helix-stabilizing interaction between tyrosine and leucine or valine when spacing if i,i+4 by Padmanbhan (1994)
  29. 10.1126/science.3381086 / Science / Amino acid preferences for specific locations at the ends of α-helices by Richardson (1988)
  30. 10.1002/pro.5560031014 / Protein Sci. / Sequence determinants of the capping box, a stabilizing motif at the N-terminal of α-helices by Seale (1994)
  31. 10.1146/annurev.bb.21.060192.000523 / Annu. Rev. Biophys. Biomol. Struct. / The mechanism of α-helix formation by peptides by Scholtz (1992)
  32. 10.1006/jmbi.1995.0619 / J. Mol. Biol. / Comparison between the φ distribution of the amino acids in the protein database and NMR data indicates that amino acids have various φ propensities in the random coil conformation by Serrano (1995)
  33. 10.1038/342296a0 / Nature / Capping and α-helix stability by Serrano (1989)
  34. 10.1006/jmbi.1996.0041 / J. Mol. Biol. / Analysis of main chain torsion angles in proteins. Prediction of NMR coupling constants for native and random-coil conformations by Smith (1996)
  35. 10.1002/pro.5560041117 / Protein Sci. / Addition of side chain interactions to modified Lifson-Roig helix-coil theory by Stapley (1995)
  36. 10.1038/nsb0795-596 / Nature Struct. Biol. / Intrinsic φ, ψ propensities of amino acids, derived from the coil regions of known structures by Swindells (1995)
  37. 10.1006/jmbi.1995.0422 / J. Mol. Biol. / Experimental analysis of the Schellman motif by Viguera (1995)
  38. 10.1016/0263-7855(90)80070-V / J. Mol. Graph. / WHATIF by Vriend (1990)
  39. 10.1017/S0033583500005333 / Quart. Rev. Biophys. / Calculations of electrostatic interactions in biological systems and in solution by Warshel (1984)
  40. 10.1126/science.8503008 / Science / Structural basis of amino acids alpha-helical propensity by Blaber (1993)
Dates
Type When
Created 22 years, 10 months ago (Oct. 7, 2002, 8:30 a.m.)
Deposited 6 years, 3 months ago (May 7, 2019, 7:54 a.m.)
Indexed 2 months ago (July 2, 2025, 2:30 p.m.)
Issued 27 years, 5 months ago (April 1, 1998)
Published 27 years, 5 months ago (April 1, 1998)
Published Print 27 years, 5 months ago (April 1, 1998)
Funders 0

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@article{Petukhov_1998, title={Position dependence of non-polar amino acid intrinsic helical propensities}, volume={278}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.1998.1682}, DOI={10.1006/jmbi.1998.1682}, number={1}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Petukhov, Michael and Muñoz, Victor and Yumoto, Noboru and Yoshikawa, Susumu and Serrano, Luis}, year={1998}, month=apr, pages={279–289} }