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Volumn 21, Issue 7, 2005, Pages 3002-3007

Solid-state NMR structural studies of peptides immobilized on gold nanoparticles

Author keywords

[No Author keywords available]

Indexed keywords

ALKANETHIOLATES; BIOMOLECULES; HYDROPHOBIC SURFACES; PEPTIDES;

EID: 16244385641     PISSN: 07437463     EISSN: None     Source Type: Journal    
DOI: 10.1021/la040092w     Document Type: Article
Times cited : (28)

References (38)
  • 19
    • 16244370888 scopus 로고    scopus 로고
    • Gladden, J.; Drobny, G. P. Unpublished result
    • Gladden, J.; Drobny, G. P. Unpublished result.
  • 20
    • 16244376052 scopus 로고    scopus 로고
    • Ph.D. Thesis, Department of Chemistry, University of Washington, Seattle, WA
    • Stringer, J. S. Ph.D. Thesis, Department of Chemistry, University of Washington, Seattle, WA, 1998.
    • (1998)
    • Stringer, J.S.1
  • 25
    • 0038450278 scopus 로고    scopus 로고
    • A study of homonuclear dipolar recoupling pulse sequences in solid-state nuclear magnetic resonance
    • Karlsson, T.; Popham, J. M.; Long, J. R.; Drobny, G. P. A study of homonuclear dipolar recoupling pulse sequences in solid-state nuclear magnetic resonance. J. Am. Chem. Soc. 2003, 125 (24), 7394-7407.
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.24 , pp. 7394-7407
    • Karlsson, T.1    Popham, J.M.2    Long, J.R.3    Drobny, G.P.4
  • 34
    • 0037024166 scopus 로고    scopus 로고
    • Assembly of alpha-helical peptide coatings on hydrophobic surfaces
    • Long, J. R.; Oyler, N.; Drobny, G. P.; Stayton, P. S. Assembly of alpha-helical peptide coatings on hydrophobic surfaces. J. Am. Chem. Soc. 2002, 124 (22), 6297-6303.
    • (2002) J. Am. Chem. Soc. , vol.124 , Issue.22 , pp. 6297-6303
    • Long, J.R.1    Oyler, N.2    Drobny, G.P.3    Stayton, P.S.4
  • 36
    • 16244368982 scopus 로고    scopus 로고
    • NMR studies of the structure and dynamics of proteins adsorbed to biomaterial interfaces
    • Shaw, W. J.; Long, J. R.; Drobny, G. P.; Stayton, P. S. NMR Studies of the Structure and Dynamics of Proteins Adsorbed to Biomaterial Interfaces. Crit. Rev. Oral Biol. Med. 2003, 14 (5), 370-376.
    • (2003) Crit. Rev. Oral Biol. Med. , vol.14 , Issue.5 , pp. 370-376
    • Shaw, W.J.1    Long, J.R.2    Drobny, G.P.3    Stayton, P.S.4
  • 37
    • 16244383375 scopus 로고    scopus 로고
    • NMR studies of the structure and dynamics of proteins adsorbed to biomaterial interfaces
    • Drobny, G. P.; Cotten, M.; Long, J. R.; Stayton, P. S. NMR Studies of the Structure and Dynamics of Proteins Adsorbed to Biomaterial Interfaces. Annu. Rev. Phys. Chem. 2003, 54, 531-573.
    • (2003) Annu. Rev. Phys. Chem. , vol.54 , pp. 531-573
    • Drobny, G.P.1    Cotten, M.2    Long, J.R.3    Stayton, P.S.4
  • 38
    • 84860105825 scopus 로고    scopus 로고
    • accessed
    • Source: Statistics Calculated for All Chemical Shifts from Atoms in the 20 Common Amino Acids. http://www.bmrb.wisc.edu/ref_info/statful.htm (accessed 2004). For the side-chain amine of lysine the minimum shift reported is 7.77 ppm (relative to liquid ammonia), and the maximum shift is 131.04 ppm, with an average shift of 48.17 ppm and a standard deviation of 36.38 ppm.
    • (2004) Source: Statistics Calculated for All Chemical Shifts from Atoms in the 20 Common Amino Acids


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