Stretching single protein molecules: Titin is a weird spring

Science

Volumn 276, Issue 5315, 1997, Pages 1090-1092

  Erickson, Harold P ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN;

AMINO ACID SEQUENCE; ELASTICITY; ENTROPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; REVIEW;

AMINO ACID SEQUENCE; ELASTICITY; ENTROPY; IMMUNOGLOBULINS; MUSCLE PROTEINS; MUSCLE RELAXATION; MUSCLE, SKELETAL; PROTEIN FOLDING; PROTEIN KINASES; SARCOMERES; STRESS, MECHANICAL;

EID: 0030962748     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.276.5315.1090     Document Type: Review

References (10)

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5. A. Soteriou, A. Clarke, S. Martin, J. Trinick, Proc. R. Soc. London Ser. B254, 83 (1993).
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7. W. A. Linke et al., J. Mol. Biol. 261, 62 (1996); M. Gautel and D. Goulding, FEBS Lett. 385, 11 (1996).
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9. H. Granzier, M. Helmes, K. Trombitás, Biophys. J. 70, 430 (1996).
10. A force of 100 pN operating over 0.5 nm corresponds to a free energy of 7 kcal/mol, which is close to the total folding energy of a domain. The implication is that the entire free energy of folding is dissipated by the strong force needed to pull out the first few atoms. In contrast, for refolding, the domain must gather in its full 25 nm or more of polypeptide and compact it into the folded domain. A force of 4 pN operating over 25 nm corresponds to 14 kcal/ mol, which is more than sufficient to block refolding. Domain refolding probably cannot occur efficiently until the force is reduced to 1 pN or less.