The Conserved Lid Tryptophan, W211, Potentiates Thermostability and Thermoactivity in Bacterial Thermoalkalophilic Lipases

Carnosine Inhibits Aβ42Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster

(2013) Francesco Attanasio et al.   CHEMBIOCHEM

Modifying the catalytic preference of tributyrin in Bacillus thermocatenulatus lipase through in-silico modeling of enzyme-substrate complex

(2013) E. Durmaz et al.   PROTEIN ENGINEERING DESIGN & SELECTION

Protein analysis by dynamic light scattering: Methods and techniques for students

(2012) Bernard Lorber et al.   BIOCHEMISTRY AND MOLECULAR BIOLOGY EDUCATION

Extracellular expression and characterization of thermostable lipases, LIP8, LIP14 and LIP18, from Yarrowia lipolytica

(2012) Arti Kumari et al.   BIOTECHNOLOGY LETTERS

Improvement of Thermal Stability via Outer-Loop Ion Pair Interaction of Mutated T1 Lipase from Geobacillus zalihae Strain T1

(2012) Rudzanna Ruslan et al.   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Engineering the third wave of biocatalysis

(2012) U. T. Bornscheuer et al.   NATURE

The role of tryptophan in protein fibrillogenesis: relevance of Trp7 and Trp14 to the amyloidogenic properties of myoglobin

(2012) P. Cecchini et al.   PROTEIN ENGINEERING DESIGN & SELECTION

Conformational stability and aggregation of therapeutic monoclonal antibodies studied with ANS and Thioflavin T binding

(2011) Veysel Kayser et al.   mAbs

Stabilizing Salt-Bridge Enhances Protein Thermostability by Reducing the Heat Capacity Change of Unfolding

(2011) Chi-Ho Chan et al.   PLoS One

CHARMM: The biomolecular simulation program

(2009) B. R. Brooks et al.   JOURNAL OF COMPUTATIONAL CHEMISTRY

Activation of Bacterial Thermoalkalophilic Lipases Is Spurred by Dramatic Structural Rearrangements

(2008) César Carrasco-López et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Characterization of Globular Protein Solutions by Dynamic Light Scattering, Electrophoretic Mobility, and Viscosity Measurements

(2008) Barbara Jachimska et al.   LANGMUIR