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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.
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
13 distal cells secrete primarily the silk- and polyglycine-collagen diblocks, whereas the proximal cell
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
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
27 omain are also unlikely because insertion of polyglycines into the linker connecting them has no dele
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
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
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
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
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
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