Mutation of conserved histidines alters tertiary structure and nanomechanics of consensus ankyrin repeats

Journal of Biological Chemistry

Volumn 287, Issue 23, 2012, Pages 19115-19121

  Lee, Whasil ^a   Strümpfer, Johan ^c   Bennett, Vann ^b   Schulten, Klaus ^c   Marszalek, Piotr E ^a,d  

^a Duke University   (United States)

^b DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^d DUKE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; ATOMIC FORCE; MECHANICAL EFFECTS; MECHANICAL ENERGIES; MECHANICAL FAILURES; MECHANICAL FATIGUE; MECHANICALLY STABLE; MOLECULAR DYNAMICS SIMULATIONS; MUTANT PROTEINS; REFOLDING; SINGLE MOLECULE FORCE SPECTROSCOPY; TERTIARY STRUCTURES; TETRAPEPTIDE;

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; MECHANICAL PROPERTIES; MOLECULAR DYNAMICS;

PROTEINS;

ANKYRIN; ARGININE; HISTIDINE; MUTANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; ATOMIC FORCE MICROSCOPY; CONSENSUS SEQUENCE; CONTROLLED STUDY; ENERGY; MEASUREMENT; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN REFOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; SIMULATION; SINGLE MOLECULE FORCE SPECTROSCOPY; SPECTROSCOPY;

AMINO ACID SUBSTITUTION; ANKYRIN REPEAT; HUMANS; MODELS, MOLECULAR; MUTATION, MISSENSE; PROTEIN STRUCTURE, TERTIARY; SPHEROCYTOSIS, HEREDITARY;

EID: 84861748866     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.365569     Document Type: Article

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