Correlation between 13Cα chemical shifts and helix content of peptide ensembles

Protein Science

Volumn 17, Issue 5, 2008, Pages 950-954

  Weinstock, Daniel S ^b   Narayanan, Chitra ^b   Baum, Jean ^a   Levy, Ronald M ^a  

^a RUTGERS UNIVERSITY   (United States)

^b NONE

Author keywords

Chemical shift; Peptide ensembles

Indexed keywords

ALANYLGLUTAMYLTHREONYLALANYLALANYLALANYLLYSYLPHENYLALANYL LEUCYLARGINYLGLUTAMYLHISTIDYLMETHIONYLASPARTYLSERINE; PEPTIDE; CARBON;

ARTICLE; CALCULATION; CARBON NUCLEAR MAGNETIC RESONANCE; CORRELATION ANALYSIS; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS; SIMULATION; AMINO ACID SEQUENCE; CHEMISTRY; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CARBON ISOTOPES; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY;

EID: 43049095706     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.073365408     Document Type: Article

References (20)

1. Banks, J.L., Beard, H.S., Cao, Y., Cho, A.E., Damm, W., Farid, R., Felts, A.K., Halgren, T.A., Mainz, D.T., Maple, J.R., et al. 2005. Integrated modeling program, applied chemical theory (IMPACT). J. Comput. Chem. 26: 1752-1780.
2. de Dios, A.C., Pearson, J.G., and Oldfield, E. 1993. Secondary and tertiary structure effects on protein NMR chemical shifts: An ab initio approach. Science 260: 1491-1496.
3. Dyson, H.J. and Wright, P.E. 2001. Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol. 339: 259-270.
4. Eliezer, D., Yao, J., Dyson, H.J., and Wright, P.E. 1998. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. 5: 148-155.
5. Frishman, D. and Argos, P. 1995. Knowledge based protein secondary structure assignment. Proteins 23: 566-579.
6. Gallicchio, E. and Levy, R.M. 2004. AGBNP: An analytic implicit solvent model suitable for molecular dynamics and high-resolution modeling. J. Comput. Chem. 25: 479-499.
7. Klee, W.A. 1968. Studies of the conformation of ribonuclease S-peptide. Biochemistry 7: 2731-2736.
8. Marsh, D., Singh, V.K., Zongchao, J., and Forman-Kay, J.D. 2006. Sensitivity of secondary structure propensities to sequence differences between α- and γ-synulcein: Implications for fibrillation. Protein Sci. 15: 2795-2804.
9. Mitchinson, C. and Baldwin, R.L. 1986. The design and production of semisynthetic ribonucleases with increased thermostability by incorporation of S-peptide analogues with enhanced helical stability. Proteins 1: 23-33.
10. 15N chemical shifts. J. Biomol. NMR 26: 215-240.
11. Schwarzinger, S., Kroom, G.J., Foss, T.R., Chung, J., Wright, P.E., and Dyson, H.J. 2001. Sequence-dependent correction of random coil NMR chemical shifts. J. Am. Chem. Soc. 123: 2970-2978.
12. Smith, L.J., Fiebig, K.M., Schwalbe, H., and Dobson, C.M. 1996. The concept of a random coil: Residual structure in peptides and denatured proteins. Fold. Des. 1: R95-R106. doi: 10.1016/S1359-0278(96)00046-6.
13. 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113: 5490-5492.
14. Sugita, Y. and Okamoto, Y. 1999. Replica-exchange molecular dynamics method for protein folding. Chem. Phys. Lett. 314: 141-151.
15. Szilagyi, L. and Jardetzky, O. 1989. α-Proton chemical shifts and protein secondary structure. J. Magn. Reson. 83: 441-449.
16. Tirado-Rives, J. and Jorgenson, W.L. 1991. Molecular dynamics simulations of the unfolding of an α-helical analogue of ribonuclease A S-peptide in water. Biochemistry 30: 3864-3871.
17. Wang, Y. and Jardetzky, O. 2002. Probability-based protein secondary structure identification using combined NMR chemical-shift data. Protein Sci. 11: 852-861.
18. Wishart, D.S. and Sykes, B.D. 1994a. Chemical shifts as a tool for structure determination. Methods Enzymol. 239: 363-392.
19. 13C chemical-shift data. J. Biomol. NMR 4: 171-180.
20. 15N random coil NMR chemical shifts of the common amino acids I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5: 67-81.