Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins-Reference-Cited by-同舟云学术

Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins

Published:2019-03-01 Issue:12 Volume:141 Page:4908-4918
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Beveridge Rebecca¹,Migas Lukasz G.¹,Das Rahul K.²^ORCID,Pappu Rohit V.²^ORCID,Kriwacki Richard W.³,Barran Perdita E.¹^ORCID

Affiliation:

1. The Michael Barber Centre for Collaborative Mass Spectrometry, The School of Chemistry, Manchester Institute for Biotechnology, University of Manchester, Manchester M13 9PL, U.K.

2. Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, Campus Box 1097, One Brookings Drive, St. Louis, Missouri 63130, United States

3. Structural Biology, MS 311, Room D1024F, St. Jude Children’s Research Hospital, 262 Danny Thomas Place, Memphis, Tennessee 38105-3678, United States

Funder

University of Manchester

Biotechnology and Biological Sciences Research Council

Engineering and Physical Sciences Research Council

Austrian Science Fund

University Of Edinburgh

Division of Molecular and Cellular Biosciences

National Cancer Institute

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis