How strong are side chain interactions in the folding intermediate?

Protein Science

Volumn 18, Issue 10, 2009, Pages 2152-2159

  Samatova, Ekaterina N ^a   Katina, Natalia S ^a   Balobanov, Vitaly A ^a   Melnik, Bogdan S ^a   Dolgikh, Dmitry A ^b   Bychkova, Valentina E ^a   Finkelstein, Alexei V ^a  

^a INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^b SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Apomyoglobin mutants; Changes in free energy; Conserved residues; Protein folding; Protein stability; Strength of interactions

Indexed keywords

ALANINE; APOMYOGLOBIN;

ACIDITY; AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY;

AMINO ACID SUBSTITUTION; AMINO ACIDS; ANIMALS; APOPROTEINS; MYOGLOBIN; POINT MUTATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SPERM WHALE; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 70349448685     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.229     Document Type: Article

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