User:Jaime.Prilusky/Test/Sortable

IB Tomasic, MC Metcalf, AI Guce, NE Clark, SC Garman. J. Biol. Chem. 2010 doi: 10.1074/jbc.M110.118588
The human lysosomal enzymes α-galactosidase and α-N-acetylgalactosaminidase share 46% amino acid sequence identity and have similar folds. Using a rational protein engineering approach, we interconverted the enzymatic specificity of α-GAL and α-NAGAL. The engineered α-GAL retains the antigenicity but has acquired the enzymatic specificity of α-NAGAL. Conversely, the engineered α-NAGAL retains the antigenicity but has acquired the enzymatic specificity of the α-GAL enzyme. Comparison of the crystal structures of the designed enzyme to the wild-type enzymes shows that active sites superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

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by Eric Martz
A historical review on sculptures and physical models of macromolecules.

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by Eran Hodis
Green fluorescent protein (GFP) is a bioluminescent polypeptide isolated from the jellyfish Aequorea victoria. GFP converts the blue chemiluminescence of aequorin into green fluorescent light. In the laboratory, GFP can be incorporated into a variety of biological systems in order to function as a marker protein. Since its discovery in 1962, GFP has become a significant contributor to the research of monitoring gene expression, localization, mobility, traffic, or interactions between various membrane and cytoplasmic proteins.

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This tutorial illustrates some basic properties of protein structure:

• Levels of protein structure.
• Ways of representing protein structure.
• Secondary structures.
• Motifs in proteins.
• Domains.
• Tertiary structure.
• Quaternary structure.

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