The cross-β configuration in supercontracted proteins

Astbury, W. T.; Beighton, E.; Parker, Kate

doi:10.1016/0006-3002(59)90330-0

Cited by 31 publications

(25 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fibers of longer segments, Aβ 11-25 (30) and Aβ [34][35][36][37][38][39][40][41][42] (61), also display an antiparallel β-strand orientation. The antiparallel orientation might be associated with pathology seeing that it was observed for a subset of fibers of the "Iowa" Aβ mutant that is related to a familial, early onset, Alzheimer's disease (6,7).…”

Section: Resultsmentioning

confidence: 99%

“…Previously described structures of Aβ [35][36][37][38][39][40] and Aβ 37-42 segments (45) are shown in Figure 2 I-K. Aβ 35-40 crystallized in two forms, both displaying antiparallel β-sheets with a face ¼ back orientation, symmetry class 8 ( Fig. 2 I-J).…”

Section: Resultsmentioning

confidence: 99%

“…The Aβ [35][36][37][38][39][40][41][42] segment crystallized in two crystal forms displaying both parallel (face-to-back orientation, symmetry class 2) (Fig. 2G) and antiparallel (face ¼ back orientation, symmetry class 7) (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Generally, the strands are allowed to translate in respect to each other, but the orientation of the strands (parallel vs. antiparallel) remains fixed (41,59). Several segments within the regions of Aβ [11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] and Aβ [27][28][29][30][31][32][33][34][35][36][37][38][39][40][41][42] were predicted either to self-associate into homotypic steric zippers (Fig. 1A) or to form heterotypic steric zippers in which one of the two β-sheets is composed of one segment and the complementary β-sheet is composed of a second segment (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Different amyloid fibers display similar biophysical characteristics (36), most notably their common "cross-β structure" indicated by their X-ray fiber-diffraction patterns, displaying orthogonal reflections at about 4.8-and 10-Å spacings (37)(38)(39). The atomic features of the cross-β structure have been clarified by X-ray-derived atomic models of amyloid-like structures, revealing a motif consisting of a pair of tightly mated β-sheets, called a "steric zipper" (20).…”

mentioning

confidence: 99%

See 4 more Smart Citations

Molecular basis for amyloid-β polymorphism

Colletier

Laganowsky

Landau

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

395

500

View full text Add to dashboard Cite

Amyloid-beta (Aβ) aggregates are the main constituent of senile plaques, the histological hallmark of Alzheimer's disease. Aβ molecules form β-sheet containing structures that assemble into a variety of polymorphic oligomers, protofibers, and fibers that exhibit a range of lifetimes and cellular toxicities. This polymorphic nature of Aβ has frustrated its biophysical characterization, its structural determination, and our understanding of its pathological mechanism. To elucidate Aβ polymorphism in atomic detail, we determined eight new microcrystal structures of fiber-forming segments of Aβ. These structures, all of short, self-complementing pairs of β-sheets termed steric zippers, reveal a variety of modes of self-association of Aβ. Combining these atomic structures with previous NMR studies allows us to propose several fiber models, offering molecular models for some of the repertoire of polydisperse structures accessible to Aβ. These structures and molecular models contribute fundamental information for understanding Aβ polymorphic nature and pathogenesis.amyloid aggregation | 3D profile | protofilaments | heterotypic zipper

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Molecular basis for amyloid-β polymorphism

Colletier

Laganowsky

Landau

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

395

500

View full text Add to dashboard Cite

show abstract

Conformations and optical rotatory properties of poly‐O‐acetylthreonine and poly‐O‐acetylallothreonine

1968

View full text Add to dashboard Cite

SynposisOptically active poly-0-acetylthreonine and poly-0-acetyl-allothreonine exist in the B form in pyridine, in 2-chloroethanol-dichloromethane mixed solvent, and in the solid state. The optical rotatory dispersion of the 6 form of poly-0-acetyl-L-threonine in a 2-chloroethanol-dichloromethane mixture showed ft Cotton effect in the 230 mp region. The ORD data in the visible spectral region fit the MofFitt equation. The absolute values of bo, as measured in pyridine for polypeptides with a molecular weight above 17000, varied in the range 100-200", the sign depending on the absolute configuration of the side chain.

show abstract

Single crystals of poly(L‐glutamic acid)

Keith¹,

Giannoni²,

Padden³

1969

Biopolymers

View full text Add to dashboard Cite

SynopsisLamellar single crystals of alkaline earth salts of poly(Lg1utsmic acid) have been grown by precipitation from dilute aqueous solution and studied by optical and electron microscopy and by x-ray and electron diffraction. The calcium, strontium and barium salts were crystallized in the , ¶ form above room temperature and could be converted to crystals of p-poly(L-glutamic acid) by washing in dilute hydrochloric acid. The magnesium salt, on the other hand, was crystallized in the a form at or below room temperature but could not be converted into crystals of a-poly(Lg1utamic acid) by washing in hydrochloric acid. The crystalline lamellae are very thin (thicknesses range from 25 to 60 d in , ¶ crystals and are about 100 A in a crystals) and the polypeptide chains are oriented normal to the planes of the lamellae. It is clear from the disparity between crystal thickness and molecular length that the molecules crystallize by folding at the upper and lower surfaces of the crystals. Conformations of the molecules a t these folds are discussed briefly.

show abstract

The cross-β configuration in supercontracted proteins

Cited by 31 publications

References 20 publications

Molecular basis for amyloid-β polymorphism

Molecular basis for amyloid-β polymorphism

Conformations and optical rotatory properties of poly‐O‐acetylthreonine and poly‐O‐acetylallothreonine

Single crystals of poly(L‐glutamic acid)

Contact Info

Product

Resources

About