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Fernandez-Lima FA, Blase RC, Russell DH. A Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes. Int J Mass Spectrom. 2010;298(1):111-118doi: 10.1016/j.ijms.2009.10.009.
Fernandez-Lima, F. A., Blase, R. C., & Russell, D. H. (2010). A Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes. International journal of mass spectrometry, 298(1), 111-118. https://doi.org/10.1016/j.ijms.2009.10.009
Fernandez-Lima, Francisco A, et al. "A Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes." International journal of mass spectrometry vol. 298,1 (2010): 111-118. doi: https://doi.org/10.1016/j.ijms.2009.10.009
Fernandez-Lima FA, Blase RC, Russell DH. A Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes. Int J Mass Spectrom. 2010 Dec 01;298(1):111-118. doi: 10.1016/j.ijms.2009.10.009. PMID: 21503273; PMCID: PMC3077763.
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Int J Mass Spectrom. 2010 Dec 01;298(1):111-118. doi: 10.1016/j.ijms.2009.10.009.

A Study of Ion-Neutral Collision Cross Section Values for Low Charge States of Peptides, Proteins, and Peptide/Protein Complexes.

International journal of mass spectrometry

Francisco A Fernandez-Lima, Ryan C Blase, David H Russell

Affiliations

  1. Department of Chemistry, Texas A&M University, College Station, Texas, 77843, USA.

PMID: 21503273 PMCID: PMC3077763 DOI: 10.1016/j.ijms.2009.10.009

Abstract

Here, we report ion-helium collision cross sections (CCS) for a number of peptide, small protein, and peptide/protein ionic complexes. The CCS values reported here are compared to previously reported results.[1, 2] We also compare values for low charge state species, i.e., [M + H](+) and [M + 2H](2+), formed by MALDI with values for high charge state species formed by ESI, and the measured CCSs are compared with predicted CCS for solid-state and solution phase structures and calculated structures obtained by using a protein-protein structure algorithm generator, based on a combined Biomolecular complex Generation with Global Evaluation and Ranking[3] and Multi Dimensional Scaling[4].

References

  1. J Am Soc Mass Spectrom. 2005 Sep;16(9):1493-1497 - PubMed
  2. Biophys J. 2007 Dec 15;93(12):4392-403 - PubMed
  3. Proteins. 2000 Jun 1;39(4):372-84 - PubMed
  4. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1476-82 - PubMed
  5. J Am Soc Mass Spectrom. 2005 Jun;16(6):893-905 - PubMed
  6. J Am Soc Mass Spectrom. 1999 Aug;10(8):719-31 - PubMed
  7. J Am Soc Mass Spectrom. 1999 Aug;10(8):711-8 - PubMed
  8. J Mol Biol. 1994 Nov 25;244(2):183-97 - PubMed
  9. J Biol Chem. 1980 Mar 25;255(6):2578-82 - PubMed
  10. J Am Soc Mass Spectrom. 2007 Jul;18(7):1239-48 - PubMed
  11. J Mol Biol. 2003 Apr 4;327(4):857-65 - PubMed
  12. Chem Biol. 2009 Apr 24;16(4):382-90 - PubMed
  13. J Phys Chem A. 2008 Nov 6;112(44):11061-6 - PubMed
  14. Biochim Biophys Acta. 1997 Aug 15;1341(1):1-13 - PubMed
  15. J Mol Biol. 1987 Apr 5;194(3):531-44 - PubMed
  16. J Am Soc Mass Spectrom. 2007 Jul;18(7):1232-8 - PubMed
  17. Anal Chem. 1985 Mar;57(3):675-9 - PubMed
  18. Proteins. 2006 Apr 1;63(1):113-26 - PubMed
  19. Anal Chem. 2007 Feb 15;79(4):1523-8 - PubMed
  20. J Chem Phys. 2004 Jun 22;120(24):11919-29 - PubMed
  21. Phys Rev Lett. 2006 Mar 10;96(9):090601 - PubMed
  22. J Am Chem Soc. 2005 Oct 12;127(40):13778-9 - PubMed
  23. J Am Soc Mass Spectrom. 1999 Aug;10(8):685-702 - PubMed
  24. J Am Soc Mass Spectrom. 2004 Jun;15(6):870-8 - PubMed
  25. J Biomol NMR. 2000 Feb;16(2):93-108 - PubMed
  26. J Biol Chem. 1982 Jun 10;257(11):6010-5 - PubMed
  27. Proteins. 2003 Nov 1;53(2):182-92 - PubMed
  28. J Am Soc Mass Spectrom. 1999 Aug;10(8):675-84 - PubMed
  29. J Biol Chem. 1982 Jun 10;257(11):6016-22 - PubMed
  30. Curr Protein Pept Sci. 2008 Feb;9(1):1-15 - PubMed
  31. J Am Soc Mass Spectrom. 1994 May;5(5):425-33 - PubMed
  32. J Am Chem Soc. 1996 Jul 31;118(30):7178-89 - PubMed
  33. J Chem Phys. 2008 Apr 7;128(13):134111 - PubMed
  34. Protein Sci. 1995 Jul;4(7):1402-11 - PubMed
  35. J Am Soc Mass Spectrom. 2005 Feb;16(2):158-65 - PubMed
  36. J Biomol NMR. 1996 Dec;8(4):379-90 - PubMed
  37. Proc Natl Acad Sci U S A. 2004 May 11;101(19):7215-22 - PubMed
  38. Anal Chem. 1996 Jun 1;68(11):1895-904 - PubMed
  39. Biochemistry. 1997 Aug 5;36(31):9409-22 - PubMed
  40. Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):709-13 - PubMed
  41. Annu Rev Phys Chem. 2000;51:179-207 - PubMed
  42. Anal Chem. 2000 Sep 1;72(17):3965-71 - PubMed
  43. J Chem Phys. 2006 Sep 21;125(11):114103 - PubMed
  44. Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1227-37 - PubMed
  45. J Mol Biol. 1998 Feb 13;276(1):151-64 - PubMed
  46. J Chem Phys. 2007 Oct 21;127(15):154322 - PubMed
  47. J Am Soc Mass Spectrom. 1999 Nov;10(11):1188-211 - PubMed
  48. J Biomol NMR. 1993 Nov;3(6):639-52 - PubMed
  49. Anal Chem. 2009 Jan 1;81(1):248-54 - PubMed
  50. Science. 1993 Nov 5;262(5135):896-900 - PubMed
  51. Biochemistry. 2000 Oct 31;39(43):13115-26 - PubMed
  52. J Am Soc Mass Spectrom. 2002 May;13(5):506-17 - PubMed
  53. J Phys Chem A. 2009 Jul 23;113(29):8221-34 - PubMed
  54. Anal Chem. 2008 Dec 15;80(24):9689-99 - PubMed
  55. Biochemistry. 1998 Jul 7;37(27):9641-9 - PubMed
  56. J Chem Phys. 2008 Feb 14;128(6):064105 - PubMed
  57. Anal Chem. 2004 Dec 15;76(24):7366-74 - PubMed
  58. Biophys J. 2007 Mar 15;92(6):2041-53 - PubMed
  59. J Mass Spectrom. 2001 Sep;36(9):1038-52 - PubMed
  60. Talanta. 2007 Oct 15;73(4):692-9 - PubMed

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