Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry

Proceedings of the National Academy of Sciences of the United States of America

Volumn 111, Issue 5, 2014, Pages 1801-1806

  Sriswasdi, Sira ^a,b   Harper, Sandra L ^a   Tang, Hsin Yao ^a   Gallagher, Patrick G ^c   Speicher, David W ^a,b  

^a WISTAR INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Hereditary hemolytic anemia; Protein conformations

Indexed keywords

DIMER; MUTANT PROTEIN; SPECTRIN; TETRAMER;

ANALYTIC METHOD; ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; ELLIPTOCYTOSIS; ERYTHROCYTE MEMBRANE; ERYTHROCYTE SHAPE; MACROMOLECULE; MASS SPECTROMETRY; MEMBRANE STABILIZATION; MOLECULAR MODEL; MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STABILITY; WILD TYPE;

HEREDITARY HEMOLYTIC ANEMIA; PROTEIN CONFORMATIONS;

BIOPHYSICAL PHENOMENA; MASS SPECTROMETRY; MUTANT PROTEINS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SPECTRIN;

EID: 84893485432     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1317620111     Document Type: Article

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