Premium
Characteristics of Human Lysozyme and Its Disease‐Related Mutants in their Unfolded States
Author(s) -
Sziegat Friederike,
WirmerBartoschek Julia,
Schwalbe Harald
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201008040
Subject(s) - lysozyme , protein folding , folding (dsp implementation) , native state , amyloid (mycology) , mutant , point mutation , unfolded protein response , protein structure , protein aggregation , biophysics , chemistry , fibril , crystallography , biology , biochemistry , endoplasmic reticulum , gene , inorganic chemistry , electrical engineering , engineering
A subtle balance : The residual structure and dynamics in nonnative hen lysozyme, human lysozyme, and in two amyloidogenic mutants have been characterized by NMR spectroscopy at atomic resolution. The degree of residual structure correlates with the ability of the protein to form amyloid fibrils. The free‐energy landscape connecting different members of the ensemble of premolten protein states is affected by single‐point mutations (see picture).