Observation of conserved solution-phase secondary structure in gas-phase tryptic peptides. Academic Article

abstract

• Results from ion mobility studies of tryptic peptides suggest that, in some cases, the gas-phase structures can be related to the solution-phase structure of the parent protein. The interpretation of ion mobility measurements is supported by results from molecular modeling and H/D exchange experiments on the same peptides. This study clearly illustrates the utility of IM-MS for screening complex mixtures for peptides having intrinsically stable secondary/tertiary structures, and/or posttranslational modification.

authors

• Russell, David

published proceedings

• J Am Chem Soc

altmetric score

• 3

author list (cited authors)

• Ruotolo, B. T., Verbeck, G. F., Thomson, L. M., Gillig, K. J., & Russell, D. H.

citation count

• 54

complete list of authors

• Ruotolo, Brandon T||Verbeck, Guido F||Thomson, Lisa M||Gillig, Kent J||Russell, David H

publication date

• April 2002

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Amino Acid Sequence
• Animals
• Cattle
• Gases
• Hemoglobins
• Horses
• Mass Spectrometry
• Molecular Sequence Data
• Myoglobin
• Oligopeptides
• Peptide Fragments
• Protein Structure, Secondary
• Solutions

PubMed Central ID

• 11960442

Digital Object Identifier (DOI)

• 10.1021/ja0178113

start page

• 4214

end page

• 4215

volume

• 124

issue

• 16

URL

• http://dx.doi.org/10.1021/ja0178113