Analyzing Protein Structure: Understanding Molecular Interactions at Creative Biostructure, Slides of Biology

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protein structure analysis

Our understanding of life at the molecular level is

highly dependent on the ability to map the

molecular details of individual proteins and

nucleic acids as well as their interactions with

each other and with small molecules (inhibitors,

cofactors, substrates, etc .). The determination of

3D structures of proteins is crucial for the

understanding of these interactions as well as

their structure-function relationships, which also

has many practical applications in drug design

and protein engineering.

Currently, more than 115,000 protein structures have been

deposited into the Protein Data Bank (PDB) and this number

keeps growing at an unprecedented speed due to

technological advances over the years. Several methods are

used to determine the structure of a biomacromolecule,

including X-ray crystallography, NMR spectroscopy, and EM.

X-ray crystallography has made the largest contribution to

the number of protein structures deposited in PDB. NMR

excels at the determination of protein conformations and the

study of protein dynamics in aqueous solutions. EM, and

particularly Cryo-EM can be used to study relatively large

objects such as macromolecular assemblies and complexes.

Learn more about the comparison of crystallography, NMR, a

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protein-crystallization-services-from-gene-to-structure-86.htm