ライフサイエンスコーパス: polyglycine

1 lution when polymerized in short segments of polyglycine.

2 mers in which two Epo monomers are linked by polyglycine.

3 ng regions (CDRs) of Abs by replacement with polyglycine.

4 Polyglycine, a poly secondary-amide, has no sidechains a

5 Lengthening of the polyglycine acceptor nucleophile beyond diglycine does n

6 e and dynamics of proton diffusion through a polyglycine analog of the gA ion channel has been invest

7 e by analyzing conformational equilibria for polyglycine and a glycine-serine block copolypeptide in

8 sed to probe the conformations of protonated polyglycine and polyalanine (Gly(n)H and Ala(n)H+, n = 3

9 he measured collision integrals for both the polyglycine and the polyalanine peptides are consistent

10 a-sheet conformations of poly-L-alanine, and polyglycine, are presented.

11 e attempted to define a minimal peptide on a polyglycine backbone that binds Qa-1b.

12 e chains of similar lengths emanating from a polyglycine backbone).

13 distal cells secrete primarily the silk- and polyglycine-collagen diblocks, whereas the proximal cell

14 the proximal cells secrete the elastin- and polyglycine-collagen diblocks.

15 The resulting polyglycine-containing protein, but not repeat RNA, is p

16 teins, and translation of CGG repeats into a polyglycine-containing protein, FMRpolyG.

17 AUG-initiated (RAN) translation of a cryptic polyglycine-containing protein, FMRpolyG.

18 ith extended structures whose replacement by polyglycine does not affect the structure of other parts

19 ale molecular dynamics simulations show that polyglycine forms compact, albeit disordered, globules i

20 This T1-S1 linker was modeled as two polyglycine helices to accommodate the residues between

21 d tripeptides with alpha-helix, beta-strand, polyglycine II (3(1)-helix), and extended structures.

22 ipeptides adopting alpha-helix, beta-strand, polyglycine II, and fully extended 2 degrees structures.

23 ilk II (beta-sheet), and silk III (threefold polyglycine II-like helix) crystal structures were ident

24 d to distinct conformational preferences for polyglycine in two different environments is presented.

25 ar behavior of loops with polyalanine versus polyglycine inserts is discussed in terms of the current

26 can be either elastin-like (soft), amorphous polyglycine (intermediate), or silk-like (stiff).

27 omain are also unlikely because insertion of polyglycines into the linker connecting them has no dele

28 onnecting loop was replaced with a series of polyglycine linkers of increasing length.

29 ction reaches equilibrium, a large excess of polyglycine nucleophile is often employed to drive the r

30 p-azophenylarsonate (Ars) were replaced with polyglycine, one CDR at a time and in combinations, by o

31 water to obtain friction forces as a single polyglycine peptide chain is pulled out of a bundle of k

32 ulled out of a bundle of k adhering parallel polyglycine peptide chains.

33 otron radiation provide direct evidence that polyglycine peptides adopt elongated conformations.

34 ng RAN translation and enhanced by increased polyglycine protein production.

35 he repeat also elicits production of a toxic polyglycine protein, FMRpolyG, via repeat-associated non

36 n III was shown to be essential, whereas the polyglycine region separating domains I and II could be

37 to evaluate the relationship of CAG and GGN (polyglycine) repeat length in the AR gene.

38 ction of the contacting residue (Asn) on the polyglycine-replaced H1 background restored the ability

39 s suggest that, except for the longest CDRs, polyglycine replacement does not alter the general struc

40 is of functional contributions of a CDR, the polyglycine replacement method appears to be most useful

41 The results suggest that polyglycine replacement of CDRs can provide structural i

42 Polyglycine replacement of H1 abolished Ars binding as e

43 The polyglycine replacement of L2, which does not contain an

44 Polyglycine segments longer than nine residues form inso

45 e site was either deleted or replaced with a polyglycine spacer or a comparable region of E-selectin

46 with 8 to 16 extra amino acids, including a polyglycine stretch and His or FLAG tags, inserted in th

47 cquisition system, while the presence of the polyglycine stretch near the amino terminus of TbpB cont

48 Among the conserved domains, a polyglycine stretch was found to be necessary for envelo

49 the PGI/PGII conformations characteristic of polyglycine structures in solution and in the crystallin

50 rst to show that although GGC regions in the polyglycine tract are highly variable, there are no muta