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  • Alex L. Lai, Eugenia M. Clérico, +5 authors Lila M. Gierasch
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 2017 (First Published: 20 April 2017)
  • Proteins are dynamic entities that populate conformational ensembles, and most functions of proteins depend on their dynamic character. Allostery, in particular, relies on ligand-modulated shifts inContinue Reading
  • Ignacio J. General, Ying Liu, Mandy E. Blackburn, Wenzhi Mao, Lila M. Gierasch, Ivet Bahar
  • Biology, Medicine, Computer Science
  • PLoS Computational Biology
  • 2014 (First Published: 15 May 2014)
  • The versatile functions of the heat shock protein 70 (Hsp70) family of molecular chaperones rely on allosteric interactions between their nucleotide-binding and substrate-binding domains, NBD andContinue Reading
  • Ian Mitchelle, Sergio D. Vera, +4 authors Gail E. Fanucci
  • Chemistry
  • 2011 (First Published: 1 February 2011)
  • In this study, site-directed spin labeling coupled with electron paramagnetic resonance (SDSL-EPR) was used to probe changes in the conformational sampling of subtype B human immunodeficiency virusContinue Reading
    The common human genetic disorder Phenylketonuria (PKU) is primarily caused by defects in the enzyme phenylalanine hydroxylase (PAH). An animal model for PKU, the BTBR Pahenu2 mouse, has a missenseContinue Reading