Unraveling the differential structural stability and dynamics features of T7 endolysin partially folded conformations.
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| Abstract | :
Characterization of partially collapsed protein conformations at atomic level is a daunting task due to their inherent flexibility and conformational heterogeneity. T7 bacteriophage endolysin (T7L) is a single-domain amidase that facilitates the lysis of Gram-negative bacteria. T7L exhibits a pH-dependent structural transition from native state to partially folded (PF) conformation. In the pH range 5-3, T7L PF states display differential ANS binding characteristics. |
| Year of Publication | :
2018
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| Journal | :
Biochimica et biophysica acta
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| Date Published | :
2018
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| ISSN Number | :
0006-3002
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| URL | :
http://linkinghub.elsevier.com/retrieve/pii/S0304-4165(18)30004-7
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| DOI | :
10.1016/j.bbagen.2018.01.004
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| Short Title | :
Biochim Biophys Acta
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