Unraveling the differential structural stability and dynamics features of T7 endolysin partially folded conformations

• Published in: Biochimica et biophysica acta Vol. 1862; no. 4; pp. 924 - 935
• Main Authors: Sharma, Meenakshi, Kumar, Dinesh, Poluri, Krishna Mohan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2018
• Subjects: Amidase; anti-infective agents; Bacteriophage; bacteriophages; denaturation; endolysin; fluorescence; Gram-negative bacteria; hydrophobicity; Lysozyme; Molten globule; nuclear magnetic resonance spectroscopy; Partially folded conformation; T7 endolysin; urea; Partially folded conformation; Bacteriophage; T7 endolysin; Lysozyme; Amidase; Molten globule

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-dep...