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1 or the repetitive tripeptide backbone of the antifreeze protein.
2 synthetic macromolecular (polymer) mimics of antifreeze proteins.
3 mal hysteresis as a functional effect of the antifreeze proteins.
4 comparable to that of the most active insect antifreeze proteins.
5 ilar to that of freezing point depression by antifreeze proteins.
6  Such repeats are a common feature of animal antifreeze proteins.
7 ch is known as an enhancer of certain insect antifreeze proteins.
8 lvent interaction of an ice-binding type III antifreeze protein (AFP III) and ubiquitin a non-ice-bin
9                Oligopeptides inspired by the antifreeze protein (AFP) and antifreeze glycoprotein (AF
10          We have studied the winter flounder antifreeze protein (AFP) and two of its mutants using mo
11                        The TH activity of an antifreeze protein (AFP) depends on the specific AFP and
12 example, evolved repetitive tandem arrays of antifreeze protein (AFP) genes that facilitate adaptatio
13  stereospecific binding of shorthorn sculpin antifreeze protein (AFP) to (2 -1 0) secondary prism fac
14                                           An antifreeze protein (AFP) with no known homologs has been
15  the cell membrane, while insect hyperactive antifreeze proteins (AFP) are soluble and generally smal
16 enes encoding insect, Dendroides canadensis, antifreeze proteins (AFP) were produced by Agrobacterium
17                                        Since antifreeze proteins (AFPs) act as KHIs, we have used the
18                                              Antifreeze proteins (AFPs) and antifreeze glycoproteins
19                                              Antifreeze proteins (AFPs) are a subset of ice-binding p
20                                              Antifreeze proteins (AFPs) are a unique class of protein
21              The primary sequences of type I antifreeze proteins (AFPs) are Ala rich and contain thre
22                                              Antifreeze proteins (AFPs) are found in fish, insects, p
23                                              Antifreeze proteins (AFPs) are of great importance for a
24                                     Type III antifreeze proteins (AFPs) are present in the body fluid
25                                              Antifreeze proteins (AFPs) are remarkable biomolecules t
26                                              Antifreeze proteins (AFPs) are specific proteins that ar
27                                          The antifreeze proteins (AFPs) bind ice nuclei and depress t
28                                              Antifreeze proteins (AFPs) bind ice to reduce freezing t
29                                              Antifreeze proteins (AFPs) can produce a difference betw
30                                              Antifreeze proteins (AFPs) facilitate the survival of di
31                                              Antifreeze proteins (AFPs) have been identified in certa
32                                              Antifreeze proteins (AFPs) have independently evolved in
33                                              Antifreeze proteins (AFPs) have the ability to modify ic
34                                              Antifreeze proteins (AFPs) help some organisms resist fr
35                                              Antifreeze proteins (AFPs) make up a class of structural
36                                              Antifreeze proteins (AFPs) of polar marine teleost fishe
37  subpolar marine teleost fishes have evolved antifreeze proteins (AFPs) or antifreeze glycoproteins (
38                                              Antifreeze proteins (AFPs) protect certain cold-adapted
39                                              Antifreeze proteins (AFPs) protect certain organisms fro
40                                              Antifreeze proteins (AFPs) protect many plants and organ
41 nisms produce ice-binding proteins (IBPs) or antifreeze proteins (AFPs) to adapt to low temperatures,
42                  It has been argued that for antifreeze proteins (AFPs) to stop ice crystal growth, t
43                                              Antifreeze proteins (AFPs), known to protect organisms f
44  basis of the cytoprotective capabilities of antifreeze proteins (AFPs), we hypothesized that supplem
45 om freezing by the presence of extracellular antifreeze proteins (AFPs), which bind to ice, modify it
46  limit supercooling and induce freezing, and antifreeze proteins (AFPs), which function to prevent fr
47 dy plants, and overwintering insects produce antifreeze proteins (AFPs), which lower the freezing poi
48                              It appears that antifreeze proteins and antifreeze glycoproteins have re
49 both have been implicated in the activity of antifreeze proteins and antifreeze glycoproteins.
50                           Hyperactive insect antifreeze proteins and bacterial ice-nucleating protein
51 f hydrogen bond dynamics for the function of antifreeze proteins and for molecular recognition.
52                                              Antifreeze proteins and glycoproteins [AF(G)Ps] have bee
53 que polysaccharide resemble those present in antifreeze proteins and glycoproteins.
54  This distinguishes AFGPs and PVA from rigid antifreeze proteins and, we argue, is responsible for th
55                                     Type III antifreeze proteins are found in Arctic and Antarctic ee
56 vation of donor cells and tissue, but native antifreeze proteins are often not suitable, nor easily a
57                                              Antifreeze proteins are produced by extremophile species
58                                For instance, antifreeze proteins, bovine serum albumin, and ovomucoid
59 ers which have no structural similarities to antifreeze proteins but reproduce the same macroscopic p
60                                    Thus, the antifreeze protein can bind to the molecularly rough ice
61 s (antifreeze activity) produced by purified antifreeze proteins (DAFPs) from the larvae of the beetl
62 Dendroides canadensis produce a family of 13 antifreeze proteins (DAFPs), four of which are in the he
63 fibrils formed from engineered R. inquisitor antifreeze protein, depending upon geometry, we estimate
64 tures (spruce budworm and Rhagium inquisitor antifreeze proteins) derived from sonication-based measu
65                          We hypothesize that antifreeze protein diversity is an important contributor
66 dentification of a phenotype associated with antifreeze protein expression in plant tissue.
67 ave used site-selective strategies to attach antifreeze proteins found in Arctic fish and insects to
68 ed to investigate the mechanism by which the antifreeze protein from the spruce budworm, Choristoneur
69                                              Antifreeze proteins from polar fish species are remarkab
70                                  A synthetic antifreeze protein gene was expressed in plants and redu
71                                          The antifreeze protein genes, both with and without the sign
72 e of large-molecular-mass antifreezes (e.g., antifreeze proteins), has been described in animals, pla
73 olecular evolution and diversity of Type III antifreeze proteins in a single individual Antarctic fis
74 ng avoidance conferred by different types of antifreeze proteins in various polar and subpolar fishes
75           Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress
76 ng that increased activity of the two-domain antifreeze protein is not dependent on structure of the
77                       The sequence of carrot antifreeze protein is similar to that of polygalacturona
78 yoprotection by a dehydrin is not due to any antifreeze protein-like activity, as has been reported p
79                                              Antifreeze proteins lower the noncolligative freezing po
80 This opens up a new field of metallo-organic antifreeze protein mimetics and provides insight into th
81 carrot shares these functional features with antifreeze proteins of fish.
82 th a clear life-saving function, the diverse antifreeze proteins of polar fishes are exemplary adapti
83                                              Antifreeze proteins prevent ice crystal growth in extrac
84 ish growth hormone (ccGH) cDNA driven by the antifreeze protein promoter from an ocean pout Zoarces a
85                                              Antifreeze proteins restrict the growth of ice crystals
86 rimary sequence of the mature spruce budworm antifreeze protein (sbwAFP) was constructed by primer ov
87 e recently discovered glycine-rich snow flea antifreeze protein (sfAFP) has no sequence homology with
88        Here, we show that, for the snow flea antifreeze protein (sfAFP), stability and cooperativity
89 termine the X-ray structure of the snow flea antifreeze protein (sfAFP).
90  initiate the crystallization process of the antifreeze protein solution.
91           The gene for a thermal hysteresis (antifreeze) protein (sthp-64) from the bittersweet night
92 s C, in part by synthesizing the most potent antifreeze protein studied thus far (RiAFP).
93 ure of RD3, a naturally occurring two-domain antifreeze protein, suggests that the two nearly identic
94 pted to live at subzero temperatures express antifreeze proteins that improve their tolerance to free
95 proline as a minimum (bio)synthetic mimic of antifreeze proteins that is accessible by solution, soli
96 ore, we identify three properties of Type I "antifreeze" proteins that discriminate among these two o
97 he simulations indicate that the 2.5 nm long antifreeze protein TmAFP nucleates ice at 2 +/- 1 degree
98 phobic groups at the ice-binding site of the antifreeze protein TmAFP of Tenebrio molitor and extende
99 n the initial recognition and binding of the antifreeze protein to ice by lowering the barrier for bi
100 that the model alpha-helical winter flounder antifreeze protein uses an unusual undertwisting of its
101   Ice-binding proteins (IBPs), also known as antifreeze proteins, were added to ice cream to investig
102 the properties of water at the surface of an antifreeze protein with femtosecond surface sum frequenc

 
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