ライフサイエンスコーパス: simple protein

1 rdinarily cooperative equilibrium folding of simple proteins.

2 ing the factors that govern folding rates of simple proteins.

3 Both metazoan parasites and simple protein allergens induce T helper type 2 (TH2) im

4 owing field of proteomic research, rapid and simple protein analysis is a crucial component of protei

5 rature jumps in the acid-denatured form of a simple protein and monitored by fluorescence resonance e

6 assay (PLA) is one of the most sensitive and simple protein assays developed to date, yet a major lim

7 nhanced fluorescence (MAMEF), we show that a simple protein-based assay system can be optically ampli

8 rly remarkable are those enzymes that act as simple protein catalysts, without the assistance of meta

9 present a drug delivery platform based on a simple protein-containing hydrogel that can be both imag

10 These surprisingly simple proteins define the minimal chemical diversity su

11 developed a DNA aptamer-based TM assay as a simple protein detection system without additional secon

12 atory sites is interpreted primarily through simple protein-DNA and protein-protein interactions, wit

13 often requires additional factors beyond the simple protein-DNA interaction.

14 Simple protein engineering provides highly specific bios

15 ding and unfolding kinetics of mutants for a simple protein folding reaction to characterize the stru

16 The rapid evolution of gene products with simple protein folds and a lack of well-characterized fu

17 t Universal Common Ancestor, suggesting that simple protein folds can evolve from random sequences re

18 multi-reading frame maximum potential ORFs, simple protein folds, and the splicing machinery.

19 A simple protein immobilization procedure was used to func

20 A pentamer of this small, topologically simple protein is resistant to mechanical deformation ov

21 ngly minor sequence differences in the ultra-simple protein itself or in the transmembrane domain of

22 produce disparate results for the relatively simple protein-ligand systems studied in this work.

23 Residue level analysis of the folding of simple proteins may hold the key to understanding foldin

24 ed to modification analyses of proteins in a simple protein mixture, Cdc2p protein complexes isolated

25 icular ion from a set of ions derived from a simple protein mixture.

26 e probe 9 selectively labeled HCA II both in simple protein mixtures and in cellular extracts.

27 f MSAD for interrogating intact proteins and simple protein mixtures in a multiplexed manner, we have

28 On simple protein mixtures, the tagging chemistry yields gr

29 analysis of protein aggregates, as found in simple protein mixtures, to complex aggregates, as found

30 With a simple protein model, it is shown that overall rotation

31 in folding has been studied extensively with simple protein models such as short cubic-lattice chains

32 rk has investigated the energy landscapes of simple protein models, but what do the landscapes of rea

33 cterize the polypeptide molecular weights of simple proteins or glycoproteins or to determine the sto

34 have monitored the folding of a kinetically simple protein, peptostreptococcal protein L (protein L)

35 ard were extracted from human plasma using a simple protein precipitation procedure.

36 yet is attained in nature with a relatively simple protein processed from water.

37 by SNARE expression and localization than by simple protein-protein affinity.

38 n that are predictable based on the rules of simple protein-protein and protein-DNA interactions.

39 CTL-dependent mechanism that extends beyond simple protein recruitment.

40 trast CT allows differentiation of simulated simple, protein-rich, hemorrhagic, and enhancing renal c

41 ro phantom specifically designed to simulate simple, protein-rich, hemorrhagic, and enhancing renal c

42 Even relatively simple protein samples may carry a wide range of modific

43 is no uniformly superior algorithm, and that simple protein similarity measures combined with hierarc

44 In the conventional paradigm, simple protein structures are assumed to fold in an all-

45 el four-stranded coiled coils are relatively simple protein structures that embody a heptad sequence

46 theoretical and experimental advances using simple protein systems as guides.

47 re, we report the development of a small and simple protein tag that complements the therapeutic and

48 Our results suggest that these ultra-simple proteins use a variety of molecular mechanisms to