Position dependence of amino acid intrinsic helical propensities II: Non‐charged polar residues: Ser, Thr, Asn, and Gln
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L Serrano | Luis Serrano | M. Petukhov | N. Yumoto | M Petukhov | K Uegaki | N Yumoto | S Yoshikawa | K. Uegaki | Susumu Yoshikawa
[1] V. Muñoz,et al. Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides. , 1995, Journal of molecular biology.
[2] G. Millhauser,et al. Estimating the relative populations of 3(10)-helix and alpha-helix in Ala-rich peptides: a hydrogen exchange and high field NMR study. , 1997, Journal of molecular biology.
[3] V. Muñoz,et al. Position dependence of non-polar amino acid intrinsic helical propensities. , 1998, Journal of molecular biology.
[4] D. Eisenberg,et al. Atomic solvation parameters applied to molecular dynamics of proteins in solution , 1992, Protein science : a publication of the Protein Society.
[5] P. V. von Hippel,et al. Calculation of protein extinction coefficients from amino acid sequence data. , 1989, Analytical biochemistry.
[6] H. Scheraga,et al. Accessible surface areas as a measure of the thermodynamic parameters of hydration of peptides. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[7] M. Swindells,et al. Intrinsic φ,ψ propensities of amino acids, derived from the coil regions of known structures , 1995, Nature Structural Biology.
[8] Y H Chen,et al. Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. , 1974, Biochemistry.
[9] A. H. Juffer,et al. Comparison of atomic solvation parametric sets: Applicability and limitations in protein folding and binding , 1995, Protein science : a publication of the Protein Society.
[10] G. Rose,et al. α‐Helix‐forming propensities in peptides and proteins , 1994 .
[11] R. L. Baldwin,et al. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. , 1993, Biochemistry.
[12] G Vriend,et al. WHAT IF: a molecular modeling and drug design program. , 1990, Journal of molecular graphics.
[13] C. Deber,et al. Peptides in membranes: Helicity and hydrophobicity , 1995, Biopolymers.
[14] R. L. Baldwin,et al. Helix propagation and N‐cap propensities of the amino acids measured in alanine‐based peptides in 40 volume percent trifluoroethanol , 1996, Protein science : a publication of the Protein Society.
[15] J Moult,et al. Role of electrostatic screening in determining protein main chain conformational preferences. , 1995, Biochemistry.
[16] R. L. Baldwin,et al. Stability of alpha-helices. , 1995, Advances in protein chemistry.
[17] L Serrano,et al. Helix design, prediction and stability. , 1995, Current opinion in biotechnology.
[18] L M Amzel,et al. Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation , 1994, Proteins.
[19] Uwe Sauer,et al. Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59 , 1993 .
[20] B. Matthews,et al. Structural basis of amino acid alpha helix propensity. , 1993, Science.
[21] J. Richardson,et al. Amino acid preferences for specific locations at the ends of alpha helices. , 1988, Science.
[22] Luis Serrano,et al. Elucidating the folding problem of helical peptides using empirical parameters , 1994, Nature Structural Biology.
[23] L Serrano,et al. Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters. , 1998, Journal of molecular biology.
[24] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[25] L Serrano,et al. Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalisms. , 1997, Biopolymers.
[26] H. Scheraga,et al. Conformational analysis of the 20 naturally occurring amino acid residues using ECEPP. , 1977, Macromolecules.
[27] V. Muñoz,et al. Intrinsic secondary structure propensities of the amino acids, using statistical ϕ–ψ matrices: Comparison with experimental scales , 1994 .
[28] A. Doig,et al. Side-chain structures in the first turn of the alpha-helix. , 1999, Journal of molecular biology.
[29] Chris Sander,et al. The double cubic lattice method: Efficient approaches to numerical integration of surface area and volume and to dot surface contouring of molecular assemblies , 1995, J. Comput. Chem..
[30] L. Gierasch,et al. Side chain–backbone hydrogen bonding contributes to helix stability in peptides derived from an α‐helical region of carboxypeptidase A , 1991, Proteins.
[31] R. L. Baldwin,et al. N‐ and C‐capping preferences for all 20 amino acids in α‐helical peptides , 1995, Protein science : a publication of the Protein Society.