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1 tein, a catalytically inactive derivative of staphylococcal nuclease.
2 o investigate single molecules of the enzyme staphylococcal nuclease.
3 introduced into the 43-52 (or Omega) loop of staphylococcal nuclease.
4 mutants have been made in the model protein staphylococcal nuclease.
5 ge of unfolding for cooperativity mutants of staphylococcal nuclease.
6 al tandem duplications of random size within Staphylococcal nuclease.
7 study the nature of disorder in crystals of Staphylococcal nuclease.
8 and closed states of an engineered mutant of staphylococcal nuclease.
9 the stability effects of other mutations in staphylococcal nuclease.
10 lysine and some glutamate point mutations in staphylococcal nuclease.
11 (Delta131Delta), a well-studied fragment of staphylococcal nuclease.
12 for ubiquitin, chymotrypsin inhibitor 2, and staphylococcal nuclease.
13 at 25 internal positions in a stable form of staphylococcal nuclease.
14 Lys, Asp, and Glu at internal position 38 in staphylococcal nuclease.
15 polar and ionizable groups on the surface of staphylococcal nuclease.
16 zeta) group in the delta-PHS/V66K variant of staphylococcal nuclease.
17 rface of two globular proteins, lysozyme and staphylococcal nuclease.
18 maller than those produced by deaminases and staphylococcal nuclease.
19 of the effects of pH on the V66D variant of staphylococcal nuclease.
20 expressed as C-terminal fusion proteins with staphylococcal nuclease.
21 y built up previously at these same sites in staphylococcal nuclease.
22 e destabilized overall relative to wild-type staphylococcal nuclease.
23 reviously for Glu34 in ubiquitin and His8 in staphylococcal nuclease.
24 charge were made at 22 ionizable residues in staphylococcal nuclease.
25 uple mutants were constructed in the core of staphylococcal nuclease.
26 apping sets of four positions in the core of staphylococcal nuclease.
27 d in 11 pairings of six sites in the core of staphylococcal nuclease.
28 rine leukemia virus (Mo-MuLV) Gag protein to staphylococcal nuclease.
29 analysis of the pH dependence of m-values of staphylococcal nuclease.
30 on the kinetics of pressure-denaturation of staphylococcal nuclease.
31 s nuclease activity similar to that of other staphylococcal nucleases.
33 ge experiments as a function of urea for SN (staphylococcal nuclease), a protein with an OB-fold moti
35 Peptide design was based on the surface of staphylococcal nuclease, a cationic DNA binding protein
36 omologues were transplanted into the core of staphylococcal nuclease, a protein of modest stability.
37 have determined delta Vu for two mutants of staphylococcal nuclease, A69T + A90S and H121P, whose un
38 side chains in the major hydrophobic core of staphylococcal nuclease and 42 homologous proteins was d
41 Pro22 and Leu25) as a cleavable fusion with staphylococcal nuclease and refolded the protein by an a
42 ivated point mutants of two target proteins (staphylococcal nuclease and ribose binding protein).
43 the solution structure of the V66W mutant of Staphylococcal nuclease and the corresponding 1-136 frag
45 sozyme, bovine pancreatic trypsin inhibitor, staphylococcal nuclease and turkey ovomucoid third domai
46 We have studied the equilibrium unfolding staphylococcal nuclease and two of its variants, V66W an
48 ts of anions on the folding of acid-unfolded staphylococcal nuclease, and urea on the unfolding of th
49 In this report, several denatured forms of staphylococcal nuclease are aligned by using compressed
50 on the structure, stability, and kinetics of staphylococcal nuclease are attributed to the binding of
51 he side chains of Lys66, Asp66, and Glu66 in staphylococcal nuclease are fully buried and surrounded
52 lu-66 in variants of a highly stable form of staphylococcal nuclease are shifted by as many as 5 pK(a
54 he global topology of this denatured form of staphylococcal nuclease, as described by an ensemble of
55 to which side chain interactions within the staphylococcal nuclease beta-barrel affect its global st
56 ructure, a conclusion reached indirectly for staphylococcal nuclease by combining two different types
57 lu-66, buried in the hydrophobic interior of staphylococcal nuclease by mutagenesis, titrate with pK(
59 le multiple mutants have been constructed in staphylococcal nuclease by various combinations of eight
60 ented, and it is shown that phage displaying staphylococcal nuclease can be enriched 100-fold in a si
61 -ray scatter are carried out for crystalline Staphylococcal nuclease; correlations and diffuse x-ray
62 66, and Asp-66 buried in the interior of the staphylococcal nuclease Delta+PHS variant were reported
66 followed by mass spectrometry, we identified staphylococcal nuclease domain containing 1 (SND1), a nu
67 d mass spectrometry-based screen to identify staphylococcal nuclease domain-containing 1 (SND1) as a
71 cids to the stability of the native state of staphylococcal nuclease, each of the 23 lysines, 5 argin
72 permit the creation of fusion proteins with staphylococcal nuclease, EcoRI endonuclease, beta-globin
73 in the Delta 131 Delta denatured fragment of staphylococcal nuclease, even in the presence of 8 M ure
74 sure-jump relaxation kinetics experiments on staphylococcal nuclease folding and unfolding demonstrat
75 dependence of the unfolding free energy for staphylococcal nuclease from what is expected from an id
76 rkwood-Frohlich equation and discovered that staphylococcal nuclease has a naturally high dielectric
77 , a fragment model of the denatured state of staphylococcal nuclease, has been extended by obtaining
78 , a fragment model of the denatured state of staphylococcal nuclease, has been extended by obtaining
79 ing this approach for mutants of the protein staphylococcal nuclease have contradicted expectations f
80 ively low intrinsic hydrophobicity, leads to staphylococcal nuclease having only marginal stability a
81 tophan of melittin, Ca-free parvalbumin, and staphylococcal nuclease in dry trehalose/sucrose films r
83 anation that the high dielectric constant of staphylococcal nuclease is a property resulting from the
85 have been biosynthetically incorporated into Staphylococcal nuclease, its V66W mutant, and the Delta
87 om light-scattering measurements of B(2) for staphylococcal nuclease, lysozyme, and chymotrypsinogen
88 otropy measurements of fluorescently labeled staphylococcal nuclease molecules reveal distinct patter
90 Comparison of the kinetics of refolding of staphylococcal nuclease, monitored by FRET, and for a pr
91 residue, Asp-66, in the interior of the V66E staphylococcal nuclease mutant, and (ii) it allows us to
92 ings in denatured forms of the small protein staphylococcal nuclease oriented in strained polyacrylam
93 folding for an interesting set of mutants of staphylococcal nuclease: P42G, P47G, P117G, and the doub
95 erogeneous folding kinetics observed for the staphylococcal nuclease protein (SNase) does not require
96 ormed a 1.1-mus MD simulation of crystalline staphylococcal nuclease, providing 100-fold more samplin
97 and Glu residues at 25 internal positions in staphylococcal nuclease showed that their pK(a) values c
98 mal requirements for activity were selected, staphylococcal nuclease (SN) and green fluorescent prote
99 ed to monitor urea denaturation of wild-type staphylococcal nuclease (SN) as well as the m+ and m- mu
100 nes the ratio of DeltaH(vH) /DeltaH(cal) for staphylococcal nuclease (SN) denaturation in guanidine h
102 sure-induced folding/unfolding transition of staphylococcal nuclease (SN) over a pressure range of ap
103 of purified chimeric proteins containing the Staphylococcal nuclease (SN) protein linked to the TM se
104 icelles by utilizing a previously successful Staphylococcal nuclease (SN-EpoR TM) fusion protein.
105 fused to the carboxyl terminus of monomeric staphylococcal nuclease (SN/GpA) as a model system for s
106 to examine in detail the folding reaction of staphylococcal nuclease (SNase) and of some of its cavit
107 between proteases and their substrates using staphylococcal nuclease (SNase) and SNase variants as mo
108 d folding kinetics of wild-type and a mutant staphylococcal nuclease (SNase) at neutral pH are signif
109 mperature fluorescence-detected refolding of staphylococcal nuclease (SNase) can be described by thre
112 (CPHMD(MSlambdaD)) framework to a series of staphylococcal nuclease (SNase) mutants with buried ioni
113 he pressure-induced equilibrium unfolding of staphylococcal nuclease (Snase) was determined by fluore
114 riggered by ionization of internal groups in staphylococcal nuclease (SNase) were studied through mul
115 aised against a peptide (SNpep) derived from staphylococcal nuclease (SNase) with both eliciting pept
116 the HX behavior from a stabilized mutant of Staphylococcal nuclease (SNase) with that predicted for
117 ic volumetric properties of various forms of staphylococcal nuclease (SNase), including three variant
119 nergetic details of the folding landscape of staphylococcal nuclease that are usually inaccessible wi
120 polar couplings (RDCs) in denatured forms of staphylococcal nuclease to changes in denaturant concent
121 ral tryptophan analogues into three forms of Staphylococcal nuclease to investigate the spectroscopic
122 th nine different single-cysteine mutants of staphylococcal nuclease to make covalently linked dimers
123 e spectroscopic data for the denaturation of staphylococcal nuclease to yield well-defined values of
125 aneous reversible unfolding and refolding of staphylococcal nuclease under native conditions was stud
126 ter effect, we have studied four variants of staphylococcal nuclease (V8 strain) each containing one
127 stribution in the ensemble of microstates of staphylococcal nuclease was affected by proton binding.
128 harge pair buried in the hydrophobic core of staphylococcal nuclease was engineered by making the V23
129 monomeric, partially folded intermediate of staphylococcal nuclease was found to double on formation
131 dependence of pK(a) values of histidines in staphylococcal nuclease was measured by (1)H NMR spectro
133 rotein stability, each of the 11 leucines in staphylococcal nuclease was substituted with isoleucine
134 d by P-O cleaving phosphodiesterases such as staphylococcal nuclease, we decided to establish the act
135 Here, using 10 cavity-containing variants of staphylococcal nuclease, we demonstrate that pressure un
136 gle and five multiple stabilizing mutants of staphylococcal nuclease were solved to high resolution.
138 olving the crystal structures of variants of staphylococcal nuclease with Gln-66, Asn-66, and Tyr-66
139 ant properties, we engineered 25 variants of staphylococcal nuclease with lysine residues at internal
140 nformation about the dynamic interactions of staphylococcal nuclease with single substrate molecules.
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