Crystal structures of chain-folded antiparallel β-sheet assemblies from sequence-designed periodic polypeptides

Macromolecules

Volumn 30, Issue 17, 1997, Pages 5012-5024

  Krejchi, Mark T ^a   Cooper, Sharon J ^b   Deguchi, Yoshikuni ^a   Atkins, Edward D T ^b   Fournier, Maurille J ^a   Mason, Thomas L ^a   Tirrell, David A ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTER SIMULATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; MACROMOLECULES; MOLECULAR SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SYNTHESIS (CHEMICAL); TEXTURES; X RAY CRYSTALLOGRAPHY;

GLUTAMIC ACID;

POLYPEPTIDES;

EID: 0031210734     PISSN: 00249297     EISSN: None     Source Type: Journal    
DOI: 10.1021/ma9614050     Document Type: Article

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45. 6EG is ±12.2%, we will discuss the consequences of the folding periodicity being out-of-phase with the amino acid sequence.
46. In adjacent reentry chain-folded lamellae, the straightforward way to relieve overcrowding at the fold surfaces is to allow contiguous sheets to progressively shear, adjacent chains in a sheet to progressively shear, or both; thus, the chains would run oblique to the lamellar normal. This can only be accomplished in the case of the distinctly puckered ap β-sheets if the shears are multiples of 0.695 nm.
47. 15 do not mention chain-folding in their structural investigation of polyAG, but, in view of the considerations discussed in the Appendix, there is every likelihood it existed in their samples. Because they did not notice any low-angle intensity it is reasonable to assume that if it exists, the peak is hidden behind the beam stop; this implies that the straight stems are long and therefore allow closer inter/sheet stacking. Irrespective of the length of the stems, the chain-folded ap β-sheets of polyAG would stack closer than those of the polypeptides investigated herein since there would be no bulky groups in the folds.
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50. 2 units either side of the -NH-CO- group; this extra flexibility allows the in-coming and out-going stems to remain parallel.
51. Extensively stacked ap β-sheets do not occur in globular protein structures and so a β-turn/twisted β-sheet is perfectly satisfactory. In those structures where a few ap β-sheets are associated together there is no indication of sheet alignment or register.
52. Appendix prepared by E.D.T.A.