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Compound 1b3d

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Suspiciously Absent

Joined: 22 Jun 2007
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PostPosted: Sat Jun 30, 2007 11:41 am    Post subject: Compound 1b3d Reply with quote

In spencers latest video his points are listed as 1) b) 3) d)

I checked online and there is a compound called 1B3D.

Beast, is this relevant do you think?
Stay tuned...
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PostPosted: Sat Jun 30, 2007 4:02 pm    Post subject: ?-Glutamic acid Reply with quote

It appears to be ?-Glutamic acid which is similar to the amino acid Glutamic acid, BUT DIFFERENT:)
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PostPosted: Sat Jun 30, 2007 4:39 pm    Post subject: Reply with quote

I dont know if this'll help you guys but here's more on 1b3d:

1B3D Hydrolase Hydrolase Inhibitor date Dec 09, 1998
title Stromelysin-1
authors L.Chen, T.J.Rydel, C.M.Dunaway, S.Pikul, K.M.Dunham, F.Gu, B.L.Barnett
compound source
Molecule: Stromelysin-1
Chain: A, B
Synonym: Mmp-3
Engineered: Yes
Other_details: Stromelysin-1 Complex With Hydroxamate- Phosphinamide Inhibitor
Organism_scientific: Homo Sapiens
Organism_common: Human
Expression_system: Escherichia Coli
symmetry Space Group: P 21 21 21
R_factor 0.256
length a length b length c angle alpha angle beta angle gamma
37.900 78.800 105.400 90.00 90.00 90.00
method X-Ray Diffraction resolution 2.30
ligand ZN, CA, S27 enzyme . Hydrolase E.C.
related structures by homologous chain: 1BQO, 1D8F
similarity Contains 1 hemopexin-like domain. Belongs to the Peptidase_M10a family.
catalytic activ. Preferential cleavage where p1', p2' and p3' are hydrophobic residues.
genes Name=MMP3;, Synonyms=STMY1; (H. sapiens)
function Activates procollagenase. Can degrade fibronectin, laminin, gelatins of type i, iii, iv, and v; collagens iii, iv, x, and ix, and cartilage proteoglycans.
Chain Function Process Component
# A, B metalloendopeptidase activity
# stromelysin 1 activity
# calcium ion binding
# metallopeptidase activity
# zinc ion binding
# hydrolase activity
# proteolysis and peptidolysis
# collagen catabolism
# extracellular matrix (sensu Metazoa)
# extracellular space
Primary reference Crystal structure of the stromelysin catalytic domain at 2.0 A resolution: inhibitor-induced conformational changes., Chen L, Rydel TJ, Gu F, Dunaway CM, Pikul S, Dunham KM, Barnett BL, J Mol Biol 1999 Oct 29;293(3):545-57. PMID:10543949

ETA: I'm gonna dig through my books and if I come up with any connections Ill post them here.

Edit 2: It is an Alpha and Beta protein. It also aids in zinc ion bonding in the body and affects proteolysis. Which is the directed degradation (digestion) of proteins by cellular enzymes called proteases or by intramolecular digestion. It diffracts in a single wavelength, but I cannot yet understand if it is relevant to us...

Ill dig more, it gives me something to do that I love, science. Very Happy

EDIT 3: I just saw alot of this in another thread, I guess I'm too slow. oh well I got to do research!!!
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