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Crambin is a small seed storage protein from the Abyssinian cabbage. It belongs to thionins. It has 46 residues (amino acids). It has been extensively
Crambin
Type of secondary structure of proteins
Three-dimensional structure of an alpha helix in the protein crambin
Alpha_helix
Electron microscopy technique
Weckert E, Lamzin VS (April 2011). "Crystal structure of small protein crambin at 0.48 Å resolution". Acta Crystallographica. Section F, Structural Biology
Cryo-electron_microscopy
Computational chemistry simulated force field
for Proteins. Energy Minimizations for Crystals of Cyclic Peptides and Crambin". J. Am. Chem. Soc. 110 (6): 1657–1666. doi:10.1021/ja00214a001. PMID 27557051
OPLS
Acetylcholine receptors named for their selective binding of nicotine
PS (February 1985). "Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme". Journal of Molecular Biology. 181 (3): 423–47
Nicotinic acetylcholine receptor
Nicotinic_acetylcholine_receptor
folding motif and overall topology of phoratoxins are identical to that of crambin. Phoratoxin proteins fold into two anti-parallel amphipathic helices that
Phoratoxin_and_viscotoxin
Protein family
microbial infections has also been identified. The hydrophobic protein crambin from the Abyssinian kale (Crambe abyssinica) is also a member of the thionin
Thionin
Group of neurotoxic peptides from snake venom
PS (February 1985). "Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme". Journal of Molecular Biology. 181 (3): 423–47
Α-Neurotoxin
1978 – Icosahedral virus 1981 – Dickerson B-form DNA dodecamer 1981 – Crambin 1985 – Calmodulin 1985 – DNA polymerase 1985 – Photosynthetic reaction
List of biophysically important macromolecular crystal structures
List_of_biophysically_important_macromolecular_crystal_structures
Chemical compound
PS (February 1985). "Protein normal-mode dynamics: trypsin inhibitor, crambin, ribonuclease and lysozyme". Journal of Molecular Biology. 181 (3): 423–447
Α-Bungarotoxin
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