Crambin

Jorgensen, W.L. Tirado-Rives, J. The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic peptides and crambin. J. Am. Chem. Soc. 110 1657-1666, 1988... 

A related method is the component synthesis method [17], which uses a so-called static condition to model the interactions between parts of a molecule whose corresponding diagonal blocks in the Hessian are first diagonalized. It has been combined with a residue clustering algorithm that provides a hierarchy of parts, which at the lowest level provides small enough matrices for efficient diagonalization [18]. It has been applied to double-helical DNA [17] and the protein crambin [18]. 

LSD Caves, JD Evanseck, M Karplus. Locally accessible conformations of proteins Multiple molecular dynamics simulations of crambin. Protein Sci 7 649-666, 1998. 

The OPLS Potential Function for Proteins. Energy Minimization for Crystals of Cyclic Peptides and Crambin William L. Jorgensen and Julian Tirado-Rives Journal of the American Chemical Society 110 (1988) 1657... 

Briinger A, Karpins M, Petsko GA. Crystallographic refinement by simulated annealing application to crambin. Acta Crystallogr, Sect A 1989 A45 50-61. 

Shimada J, Kussell EL, Shakhnovich El. The folding thermodynamics and kinetics of crambin using an all-atom Monte Carlo simulation. J Mol Biol 2001 308 79-95. 

Ogawa T, Kurita N, Sekino H, Kitao O, Tanaka S (2004) Consistent charge equilibration (CQEq) method application to amino acids and crambin protein. Chem Phys Lett 397(4-6) 382-387... 

Levitt, M. Sander, C. Stem, P.S., Protein normal-mode dynamics - trypsin-inhibitor, crambin, ribonuclease and lysozyme, 7. Mol. Biol. 1985,181, 423 47... 

Figure 3 Comparison of several thionins reveals their structural similarity. The structures are color coded for their secondary structure, cyan a-helix, red /3-strand, magenta random coil/turn. (a) a-Purothionin (2plh) and (b) /3-purothionin (1 bhp) have four disulfide bonds, (c) Crambin (1 ejg) has three disulfide bonds. Despite its thionin fold it lacks antimicrobial or other toxic activity, (d) An overlay of crambin (1ejg, black), a-purothionin (2plh, red), /3-purothionin (1 bhp, orange), viscotoxin A3 (ledO, magenta), and viscotoxin B (Ijmp, cyan) from Viscum album reveals the conserved structure of the peptide backbone.

Crambin, amide exchange rate 149 Creatine kinase 656... 

The 46-residue protein crambin has been solved at 0.83 A resolution at 130 K.6 Some proteins have been crystallized in microgravity in space rockets where the convection-free conditions can produce larger and better crystals. RNase A crystals grown in microgravity diffracted x-rays to 1.06 A resolution, approximately 0.2 A higher resolution than previously observed in terrestrially grown RNase A crystals.7 At these very high resolutions, alternate conformations of some side chains may even be seen. 

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