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1 f amino acid side chains as well as by local solvent exposure.
2 terval = 0.89, 3.73), an indication of daily solvent exposure.
3 le Trp701 displayed an intermediate level of solvent exposure.
4 quencies consistent with a greater degree of solvent exposure.
5 ions in terms of interchain interactions and solvent exposure.
6 ked to autoimmune disorders and occupational solvent exposure.
7 nsity score (OR 2.9, 95% CI 1.2-7.1) for any solvent exposure.
8 al methionines are directly related to their solvent exposure.
9  evaluation of the nervous-system effects of solvent exposure.
10 y and invariant residues tend to exhibit low solvent exposure.
11 es are more likely to be labeled despite low solvent exposure.
12 underlying layer is vulnerable to subsequent solvent exposure.
13 solvent exposure, and a biphasic response to solvent exposure.
14 d across all HLA-DQ proteins and had limited solvent exposure.
15 ibit different RAs in response to changes in solvent exposure.
16 ntration favoring conformations with greater solvent exposure.
17 a6, increasing the S-adenosylmethionine site solvent exposure.
18 c cluster that sequesters these H-bonds from solvent exposure.
19  consistent with P-cluster fragmentation and solvent exposure.
20 is effect revealed no obvious correlation to solvent exposure.
21 g surface is highly charged, consistent with solvent exposure.
22 mine changes of Tyr and Trp environments and solvent exposures.
23 ilter's (1) histidine protonation state, (2) solvent exposure, (3) oligomeric state (the number of pr
24 es that undergo cooperative changes in their solvent exposure, along with the hierarchy of interactio
25 e invasive breast cancer was associated with solvent exposure among clinical laboratory technologists
26 , 4.56) in the highest quartile of nonhexane solvent exposure and 1.62 (95% CI: 0.97, 2.72) in the hi
27 ed bases A1492 and G530 results in increased solvent exposure and an uncompensated loss of hydrogen b
28 elices, characteristic repeating patterns of solvent exposure and burial are observed.
29 plexes is found to depend on both changes in solvent exposure and changes to the residue microenviron
30 er ATP or ADP, phosphorylation increased the solvent exposure and decreased the polarity of the envir
31 id isomerization rates can be predicted from solvent exposure and flexibility as determined by molecu
32  the proteins AncCDT-1 and mRFP despite high solvent exposure and flexibility of the TFA-Lys side cha
33 in which Trp residues had a higher degree of solvent exposure and fluorescence quenching.
34 dual spectral segment centroids, compared to solvent exposure and hydrogen bonding predictions and re
35 K4, K10, E15, E19, N35, N40, and E42, due to solvent exposure and low packing density.
36                                         Both solvent exposure and probe motions of ANSmal are enhance
37 ) which shields the side chain of Trp25 from solvent exposure and produces ring current shifts as lar
38          An arginine gateway opens, allowing solvent exposure and protonation of the chromophore's ph
39  largely unique, these findings suggest that solvent exposure and redox regulation of cryptic cystein
40 r encephalopathy requiring recent industrial solvent exposure and referral bias rather than associati
41 ng thermal stress: no change, an increase in solvent exposure, and a biphasic response to solvent exp
42 ns alter the site-specific microenvironment, solvent exposure, and conformational flexibility of the
43 mal markers, physical activity, occupational solvent exposure, and constipation showed associations w
44  subdomain to probe its secondary structure, solvent exposure, and protein-protein interactions.
45 risingly, NMR chemical shifts, site-resolved solvent exposure, and relaxation studies show that the c
46 explained by the latter's deeper burial from solvent exposure, and stronger interaction with the carb
47 nteraction with NFkappaB, which controls its solvent exposure, and we demonstrate that this regulatio
48 d series of electrical measurements, optical/solvent exposures, and X-ray photoelectron spectroscopy.
49                                  Kinetics of solvent exposure are now known for nearly all backbone N
50            These results are consistent with solvent exposure as a major determinant of hydroxyl radi
51   Residue pairs were classified according to solvent exposure as well as by whether their backbone NH
52 of Arc-L1-Arc and wild-type Arc have similar solvent exposures as measured by the urea dependencies o
53 ombin interface and to screen for changes in solvent exposure at distant sites.
54 at proteins by controlling the chemistry and solvent exposure at their terminal interfaces.
55 ed spectroscopic probes of the structure and solvent exposure at these positions.
56 oid antagonists induce red shifts reflecting solvent exposure at this position.
57 le proteins having comparable differences in solvent exposure between their folded and unfolded state
58                                              Solvent exposure can be characterized by several measure
59                          All 7 patients with solvent exposure carried the 2C19EM genotype, compared w
60 V1316M exhibited exceptional instability and solvent exposure compared with all variants.
61 ull range of information on base-pairing and solvent exposure concerning the four more abundant ribon
62 eters such as backbone/Cu-loop dynamics, Cys solvent exposure, Cys-Cys distances, and cross-correlate
63 CA [cANCA] 3.9 [1.6-9.5]), high occupational solvent exposure during working lifetime (with PSV 2.7 [
64 rrounding the heme propionates leads to more solvent exposure for both propionate groups, which may a
65 ontexts were red shifted, indicating reduced solvent exposure for the fluorophore.
66 ha3 helix correlates with a higher degree of solvent exposure for this secondary structure element.
67 orted occupational activities with potential solvent exposure, furniture refinishing (OR = 9.73, 95 p
68 factors, where its side-chain is buried from solvent exposure in a hydrophobic cavity located beneath
69 ined the TQ mutant possesses greater overall solvent exposure in comparison to wild-type but with red
70 ions of van der Waals clashes and acyl chain solvent exposure in dictating FABP affinity and specific
71      In addition, a feature of intramembrane solvent exposure in LysO is inferred with the identifica
72 ntiated connective tissue disease (UCTD) and solvent exposure in Michigan and Ohio.
73 with ANCA 4.9 [1.3-18.6]), high occupational solvent exposure in the index year (with PSV 3.4 [0.9-12
74 ing sites were chosen on the basis of a high solvent exposure in the native state and a small change
75 cular self-cleavage at Asp-193 evoked higher solvent exposure in the regions of the substrate-binding
76                         Activities involving solvent exposure, including painting and use of solvents
77 nformations with altered thermostability and solvent exposure, indicating that the WXG/GXW motifs are
78                             Thus, insofar as solvent exposure is concerned, both the base- and the ac
79 r peptide (the tag) into a protein where its solvent exposure is controlled by protein conformation.
80 redicts the effects on pKa values of various solvent exposures, large ionic strength variations, stro
81 ure, whereas the larger antagonists restrict solvent exposure largely through occlusion of solvent.
82 e results provide evidence that occupational solvent exposure may be associated with an increased ris
83 est accessible surface area, suggesting that solvent exposure may be relevant to the ability of the i
84 ta = 1.0) folate suggest that differences in solvent exposure may contribute to the fluorescence effi
85                                 Occupational solvent exposure may increase the risk of connective tis
86 arged residues, it was sometimes argued that solvent exposure meant that the high dielectric of the s
87 xt, depending on the CT route efficiency and solvent exposure of (th)G.
88 onal changes were also found to increase the solvent exposure of a predicted APR, suggesting a likely
89 to examine the influence of bound ligands on solvent exposure of AChBP.
90                                              Solvent exposure of amino acid residues of proteins play
91 pattern correlates strongly with the average solvent exposure of amino acids in globular proteins, as
92 of Ca-ATPase-bound PLB, a decreased level of solvent exposure of ANSmal is observed, suggesting that
93                                The increased solvent exposure of apolar surface area in the Ca(2+)-fr
94 egrees C) is reversible and characterized by solvent exposure of aromatic residues with concomitant d
95 rimental observations, notably the increased solvent exposure of buried residues in the breach region
96 lexibility, and correlations, as well as the solvent exposure of catalytic residues.
97 e changes cause a rotation of the B loop and solvent exposure of conserved phenylalanines, which are
98 on are highly correlated with the degrees of solvent exposure of corresponding positions in the arche
99 ve to Fe-EDTA-mediated cleavage, whereas the solvent exposure of D and E alpha-helices was decreased
100 of the core polymerase resulted in increased solvent exposure of DNA binding domains of sigma70 and i
101                                          The solvent exposure of each cysteine is ascertained by chem
102  distinguished from the "closed" form by the solvent exposure of F302, a direct T209-Mn2+ bond, and t
103           Bacterial MK proteins exhibit more solvent exposure of feedback inhibitor binding sites and
104 mide quenching is widely used to monitor the solvent exposure of fluorescent probes in vitro.
105 ce (helix H6) as well as the flexibility and solvent exposure of helix H11.
106 branes, the PPII helix may function to force solvent exposure of hydrophobic amino acid side chains i
107  is small and is indicative of a substantial solvent exposure of hydrophobic groups.
108 4 of the C-terminal domain experience strong solvent exposure of hydrophobic residues as well as part
109                    This interaction prevents solvent exposure of hydrophobic residues on the surface
110 ied as hydrophobic or polar according to the solvent exposure of its generic side-chain.
111  with mass spectrometry reveals the relative solvent exposure of labeled residues within a protein, t
112                                              Solvent exposure of loop C and its protection by ligand
113 rystallography revealed major differences in solvent exposure of MHC-bound peptide epitopes, suggesti
114            On synthetic liposomes, increased solvent exposure of MPER tryptophan residues and stable
115 gnificant structural changes that affect the solvent exposure of N-terminal region, and hence the red
116                                The predicted solvent exposure of O6 at several subsites provides an e
117 e quenching experiments detected the partial solvent exposure of Pet aromatic amino acid residues at
118 ctural changes allow the protein to maintain solvent exposure of polar side chains and optimal burial
119 ive site, could result in an increase in the solvent exposure of Pro-1, raising its upper limit pK(a)
120 the larger methionine residue led to greater solvent exposure of residue 108 and heightened packing i
121  was associated with a selective increase in solvent exposure of residues 34 and 40, suggesting that
122 e accessibility method was used to probe the solvent exposure of single cysteine residues engineered
123                                  The reduced solvent exposure of TcTS catalytic cleft might be partia
124 is occupied by a ligand, the flexibility and solvent exposure of TcTS is significantly reduced.
125 t with decreased base stacking and increased solvent exposure of the 3-MI fluorescence probe.
126 opurine and FRET derivatives suggest greater solvent exposure of the 5'-AGGGTTA- segment in the inter
127  the reduced state possibly due to increased solvent exposure of the [3Fe-4S]0 cluster.
128 o map sites of ligand binding and changes in solvent exposure of the acetylcholine-binding protein fr
129 d substrates studied in this work, increased solvent exposure of the active site upon binding of thes
130 inucleotides display a systematically higher solvent exposure of the aminoacylester bond and a weaker
131 at 3'-modified trinucleotides exhibit higher solvent exposure of the aminoacylester bond and may be m
132                                  Conversely, solvent exposure of the aminoacylester bond depends on t
133 re of the EnXyn11A-FAX(3) complex shows that solvent exposure of the backbone xylose O2 and O3 groups
134 he sheet unfolds, increased fluctuations and solvent exposure of the beta-sheet amide groups are also
135  mature virions, consistent with the limited solvent exposure of the epitope.
136 tensively, and in a manner that will enhance solvent exposure of the FAD.
137 atic stacking interactions or to the greater solvent exposure of the flavin ring was not known.
138 MN hydroquinone rather than to the increased solvent exposure of the flavin.
139 , which deactivates catalysis, increased the solvent exposure of the globin domain-dimerization inter
140  two structures suggests that differences in solvent exposure of the heme and the electrostatic envir
141 R106L (DeltaE(m) = 158 mV vs NHE), increased solvent exposure of the heme as a result of the R106L su
142 the N- and C-terminal helices and subsequent solvent exposure of the hydrophobic, heme-containing cav
143 y of beta 2 compared to alpha beta is due to solvent exposure of the isoalloxazine ring in the beta 2
144 conformational flexibility and the extent of solvent exposure of the labile Asp residue.
145  twisting the 21-24 helix and increasing the solvent exposure of the Lys22 sidechain, as indicated by
146                                              Solvent exposure of the N-terminus of aSyn occurs upon r
147                  This points to an increased solvent exposure of the NorC(sol) heme compared to in th
148 oss by the phenylalanine F12 band, signaling solvent exposure of the phenyl rings.
149 ng residues (P68, L69, Y166), increasing the solvent exposure of the polymorphic site.
150 g apoE3 NT mutant (L155W) revealed increased solvent exposure of the protein interior at pH values be
151  of the construct is consistent with partial solvent exposure of the tryptophan residues.
152 e chain vibrations, shows an increase in the solvent exposure of the tryptophan side chains as the te
153 und form and, in the apo form, determine the solvent exposure of the two Cys residues.
154 revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteri
155 an wild-type (wt) p53beta, and the increased solvent exposure of their aggregation-triggering segment
156 ellular membranes is linked to the degree of solvent exposure of their central and C-terminal hydroph
157 ain, complexed with mAb 64-3-7, demonstrates solvent exposure of these residues in the PR conformatio
158 g of sigma 70 to core polymerase reduced the solvent exposure of these residues.
159 ominance of this isomer is attributed to the solvent exposure of this portion of the hemin which stab
160 rylamide quenching suggest a higher level of solvent exposure of Trp-343 in the connector region of T
161                              Reversal of the solvent exposure of Trp356 is also involved in cleft clo
162 e alpha domain leading to an increase in the solvent exposure of Trp48.
163 d dissociation was correlated with increased solvent exposure of tyrosine residues and subtle changes
164 lar dynamics simulations display alternating solvent exposure of Y671 in the closed and open states.
165                                   The higher solvent-exposure of hydrophobic residues in Abeta42 olig
166 beta2-alpha2 loop to beta turn increases the solvent-exposure of the hydrophobic stretch 169-YSNQNNF-
167 protein undergoes 93% of its total change in solvent exposure on going from the unfolded state to the
168  The nature of the preceding amino acid, the solvent exposure, or the participation in specific eleme
169  structures was found to better describe the solvent exposure over ASA, CN and RD in many application
170  a tyrosine residue(s) undergoes a change in solvent exposure over the pH range 6.55 to 8.19.
171 acrylamide quenching are consistent with the solvent exposure predicted for Trp28, which is shielded
172  local density term for each atom, mimicking solvent exposure preferences.
173 , indicating increased side-chain motion and solvent exposure relative to the spectra of the other Al
174 n correlation intensity corresponding to the solvent exposure/shielding alternation of the side chain
175  versus 71 patients with scleroderma without solvent exposure ("sporadic" disease) and 106 population
176  resin produced no spectral background while solvent exposure tests demonstrated compatibility with a
177 eased inter-beta-sheet distance and a higher solvent exposure than WT-alphaS fibrils, which is also i
178 tate on the reaction pathway, as measured by solvent exposure (the Tanford beta value) also moved wit
179                             Because of their solvent exposure, the metal can be accessed and oxidized
180 ence quantum yield that varies strongly with solvent exposure, thereby distinguishing particular DNA
181                      Bound agonists restrict solvent exposure through loop closure, whereas the large
182 tophan oxidation correlates with the average solvent exposure time of tryptophan residues.
183 d the effects of local RNA structure on 2-AP solvent exposure to be distinguished from nearest neighb
184             Several case reports have linked solvent exposure to Parkinson disease (PD), but few stud
185 changing sites is consistent with a model of solvent exposure via a subglobal cooperative conformatio
186                      Detailed information on solvent exposure was ascertained from 205 cases, diagnos
187                                 Occupational solvent exposure was categorized using self-reported job
188  "open" native-like conformer with increased solvent exposure which fibrilises more readily than the
189                      Rather than emphasising solvent exposure with relatively extended sidechains, ro
190 d prevalence ratios were found for nonhexane solvent exposure, with a maximum of 1.31 (95% confidence
191 complementary information about mobility and solvent exposure yields a picture of the overall topolog

 
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