Conserved noncanonical residue Gly-126 confers instability to the middle part of the tropomyosin molecule

Journal of Biological Chemistry

Volumn 286, Issue 18, 2011, Pages 15766-15772

  Nevzorov, Ilya A ^a,b   Nikolaeva, Olga P ^b   Kainov, Yaroslav A ^c   Redwood, Charles S ^d   Levitsky, Dmitrii I ^a,b  

^a BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c N N BLOKHIN RUSSIAN CANCER RESEARCH CENTER   (Russian Federation)

^d UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN CYTOSKELETON; AMINO ACID RESIDUES; ARG RESIDUES; COILED-COIL STRUCTURE; COOPERATIVITY; F-ACTIN; HELICAL COILED-COIL; LOW TEMPERATURES; MUSCLE CONTRACTIONS; NON-COOPERATIVE; SKELETAL MUSCLE; THERMAL UNFOLDING; TROPOMYOSIN; WILD TYPES;

AMINO ACIDS; DIFFERENTIAL SCANNING CALORIMETRY; MUSCLE; PROTEINS;

MOLECULES;

ALANINE; ARGININE; ASPARTIC ACID; F ACTIN; GLYCINE; TROPOMYOSIN; TRYPSIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; GENE MUTATION; LOW TEMPERATURE; MUTANT; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

AMINO ACID SUBSTITUTION; GLYCINE; HUMANS; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; TROPOMYOSIN;

EID: 79955545375     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.209353     Document Type: Article

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