Effect of an engineered disulfide bond on the folding of T4 lysozyme at low temperatures
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00465a026
Reference37 articles.
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2. Thermal denaturation of bacteriophage T4 lysozyme at neutral pH
3. Bevington, P. R. (1969) Data Reduction and Error Analysis for the Physical Sciences, pp232-242, McGraw-Hill, New York.
4. Methanol-stabilized intermediates in the thermal unfolding of ribonuclease A
5. Observation of intermediates in the folding of ribonuclease A at low temperature using proton nuclear magnetic resonance
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5. Computer-aided modeling of structure stabilizing disulfide bonds in recombinant human interferon-γ;Pharmaceutica Acta Helvetiae;1996-06
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