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Keeping the body moving
Check out our tour of the G-protein-coupled receptor Beta Subunit 1GG2B. This particular protein beta, along with its other two partners alpha and gamma play a key part in adrenaline signaling, a process that “keeps you moving”.

Our tour of 1GG2 Beta starts with the surface model, depicting the physical volume and shape of protein colored in blue for aesthetic purposes. The long chain of amino acids comprising protein starts with a straight tail then forms a larger doughnut shape as the main body.

The surface fades away, revealing the inner ball and stick molecular model colored in gold, depicting the atomic locations and bonds comprising 1GG2 B.

We then take you inside 1GG2 B, fading the atomic structure away, to show the secondary structure depicted in light purple. The secondary structure shows hydrogen bonding between components of 1GG2 B, a key part to understanding how a protein functions and how it will react.

Touring the secondary structure of proteins truly reveals the beauty and symmetry we find in nature. We see the main doughnut shaped body of 1GG2B internally subdivided into seven sections, similar to a flower with an odd number of petals. Each section starts from the inside of the doughnut, moving outward folding down then up, forming four parallel beta sheets, eventually returning to start another section. Our tour finishes by bringing us to the section of beta sheets where 1GG2B bonds with alpha and the helix inside the tail serving as an anchor point to gamma through a coiled coil interaction.

We at Rendering Reality are thankful to those whose great research into 1GG2, made this video possible.

http://www.rcsb.org/pdb/explore.do?st...
G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND
The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.
Wall, M.A., Coleman, D.E., Lee, E., Iniguez-Lluhi, J.A., Posner, B.A., Gilman, A.G., Sprang, S.R.
Journal: (1995) Cell(Cambridge,Mass.) 83: 1047-1058
PubMed: 8521505


http://www.rcsb.org/pdb/static.do?p=h...
“The Protein Data Bank (PDB)
Secondary structure
The arrangement a protein arising from hydrogen bonding interactions within contiguous segments of the polypeptide backbone. The two main types of secondary structure are the alpha helix and the beta-pleated sheet

Alpha helix
A secondary structural motif of a protein. It is characterized by hydrogen bonds between the carbonyl group (-C=O) of one amino acid and the amino (N-H) group of the amino acid 4 residues below it along the helix. The helix makes one complete turn every 3.6 amino acids.

Beta sheet
A secondary structural motif of a protein. It is characterized by 2 or more amino acid chains lying side-by-side where hydrogen bonds are formed between carbonyl groups (C=O) of one chain and amino groups (N-H) of the adjacent chain. This arrangement forms a sheet-like structure.”


http://www.ncbi.nlm.nih.gov/pmc/artic...
G protein βγ subunits: Central mediators of G protein-coupled receptor signaling
A. V. Smrcka
Cell Mol Life Sci. 2008 Jul; 65(14): 2191–2214.