Coiled-coil structure of group A streptococcal M proteins. Different temperature stability of class A and C proteins by hydrophobic-nonhydrophobic amino acid substitutions at heptad positions a and d

Biochemistry

Volumn 36, Issue 16, 1997, Pages 4987-4994

  Cedervall, Tommy ^c   Johansson, Maria U ^a   Åkerström, Bo ^a,b  

^a LUND UNIVERSITY   (Sweden)

^b Section for Molecular Signaling   (Sweden)

^c NONE

Author keywords

[No Author keywords available]

Indexed keywords

M PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; ELECTRON MICROSCOPY; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; TEMPERATURE MEASUREMENT;

AMINO ACID SEQUENCE; AMINO ACIDS; ANTIGENS, BACTERIAL; ANTIGENS, SURFACE; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; CARRIER PROTEINS; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; FIBRINOGEN; HEAT; HUMANS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STREPTOCOCCUS PYOGENES; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); STREPTOCOCCUS SP. 'GROUP A';

EID: 0030887662     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962971q     Document Type: Article

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