-
1
-
-
0022644158
-
Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy
-
Fox RO, Evans PA & Dobson CA (1986) Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy. Nature 320, 192-194.
-
(1986)
Nature
, vol.320
, pp. 192-194
-
-
Fox, R.O.1
Evans, P.A.2
Dobson, C.A.3
-
2
-
-
0023218558
-
Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis
-
Evans PA, Dobson CM, Kautz RA, Hatfull G & Fox RO (1987) Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis. Nature 329, 266-268.
-
(1987)
Nature
, vol.329
, pp. 266-268
-
-
Evans, P.A.1
Dobson, C.M.2
Kautz, R.A.3
Hatfull, G.4
Fox, R.O.5
-
3
-
-
0025366064
-
Coupling between local structure and global stability of a protein: Mutants of staphylococcal nulcease
-
Alexandrescu TA, Hinck AP & Markley JL (1990) Coupling between local structure and global stability of a protein: mutants of staphylococcal nulcease. Biochemistry 29, 4516-4525.
-
(1990)
Biochemistry
, vol.29
, pp. 4516-4525
-
-
Alexandrescu, T.A.1
Hinck, A.P.2
Markley, J.L.3
-
4
-
-
0000261801
-
Staphylococcal nuclease: Proposed mechanism of action based on structure of enzyme-thymidine 3′,5′-bisphosphate-calcium ion complex at 1.5-Å resolution
-
Cotton FA, Hazen EE & Legg MJ (1979) Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3′,5′-bisphosphate-calcium ion complex at 1.5-Å resolution. Proc Nat Acad Sci USA 76, 2551-2562.
-
(1979)
Proc Nat Acad Sci USA
, vol.76
, pp. 2551-2562
-
-
Cotton, F.A.1
Hazen, E.E.2
Legg, M.J.3
-
5
-
-
0034692902
-
Increasing the thermostability of staphylococcal nuclease: Implications for the origin of protein thermostability
-
Chen J, Lu Z, Sakon J & Stites WE (2000) Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability. J Mol Biol 303, 125-130.
-
(2000)
J Mol Biol
, vol.303
, pp. 125-130
-
-
Chen, J.1
Lu, Z.2
Sakon, J.3
Stites, W.E.4
-
6
-
-
23644462645
-
Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding
-
Chen HM, Chan SC, Leung KW, Wu JM, Fang HJ & Tsong TY (2005) Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding. FEBS Journal 272, 3967-3974.
-
(2005)
FEBS Journal
, vol.272
, pp. 3967-3974
-
-
Chen, H.M.1
Chan, S.C.2
Leung, K.W.3
Wu, J.M.4
Fang, H.J.5
Tsong, T.Y.6
-
7
-
-
0026534194
-
pH induced folding/unfolding of staphylococcal nuclease: Determination of kinetic parameters by the sequential jump method
-
Chen HM, Markin VS & Tsong TY (1992) pH induced folding/unfolding of staphylococcal nuclease: determination of kinetic parameters by the sequential jump method. Biochemistry 31, 1483-1491.
-
(1992)
Biochemistry
, vol.31
, pp. 1483-1491
-
-
Chen, H.M.1
Markin, V.S.2
Tsong, T.Y.3
-
8
-
-
0026975884
-
Kinetic evidence of microscopic states in protein folding
-
Chen HM, Markin VS & Tsong TY (1992) Kinetic evidence of microscopic states in protein folding. Biochemistry 31, 12369-12375.
-
(1992)
Biochemistry
, vol.31
, pp. 12369-12375
-
-
Chen, H.M.1
Markin, V.S.2
Tsong, T.Y.3
-
9
-
-
0029975983
-
Least activation path for protein folding: Investigation of staphylococcal nuclease folding by stopped-flow CD
-
Su ZD, Arooz TM, Chen HM, Gross CJ & Tsong TY (1996) Least activation path for protein folding: investigation of staphylococcal nuclease folding by stopped-flow CD. Proc Natl Acad Sci USA 93, 2539-2544.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 2539-2544
-
-
Su, Z.D.1
Arooz, T.M.2
Chen, H.M.3
Gross, C.J.4
Tsong, T.Y.5
-
10
-
-
0026435470
-
Time-resolved fluorescence studies of the thermal and guanidine induced unfolding of nuclease A and its unstable mutant
-
Eftink M & Wasylewski Z (1992) Time-resolved fluorescence studies of the thermal and guanidine induced unfolding of nuclease A and its unstable mutant. Time-Resolved Laser Spectroscopy Biochemistry III 1640, 579-584.
-
(1992)
Time-Resolved Laser Spectroscopy Biochemistry III
, vol.1640
, pp. 579-584
-
-
Eftink, M.1
Wasylewski, Z.2
-
13
-
-
0027953952
-
Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants
-
Carra JH, Anderson EA & Privalov PL (1994) Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants. Biochemistry 33, 10842-10850.
-
(1994)
Biochemistry
, vol.33
, pp. 10842-10850
-
-
Carra, J.H.1
Anderson, E.A.2
Privalov, P.L.3
-
14
-
-
0031042186
-
Predicting the equilibrium protein folding pathway: Structure-based analysis of staphylococcal nuclease
-
Vincent JH & Freire E (1997) Predicting the equilibrium protein folding pathway: structure-based analysis of staphylococcal nuclease. Proteins: Structure, Function and Genetics 21, 171-183.
-
(1997)
Proteins: Structure, Function and Genetics
, vol.21
, pp. 171-183
-
-
Vincent, J.H.1
Freire, E.2
-
15
-
-
0027495402
-
Mutations can cause large changes in the conformation of a denatured protein
-
Flanagan JM, Kataoka M, Fujisawa T & Engelman DM (1993) Mutations can cause large changes in the conformation of a denatured protein. Biochemistry 32, 10359-10370.
-
(1993)
Biochemistry
, vol.32
, pp. 10359-10370
-
-
Flanagan, J.M.1
Kataoka, M.2
Fujisawa, T.3
Engelman, D.M.4
-
16
-
-
0033914528
-
Tryptophan 140 is important, but serine 141 is essential for the formation of the integrated conformation of staphylococcal nuclease
-
Yin J & Jing G (2000) Tryptophan 140 is important, but serine 141 is essential for the formation of the integrated conformation of staphylococcal nuclease. J Biochem (Tokyo) 128, 113-119.
-
(2000)
J Biochem (Tokyo)
, vol.128
, pp. 113-119
-
-
Yin, J.1
Jing, G.2
-
17
-
-
0033667255
-
Double point mutant F34WW140F of staphylococcal nuclease is in the molten globule state but highly competent to fold into a functional conformation
-
Li Y & Jing G (2000) Double point mutant F34WW140F of staphylococcal nuclease is in the molten globule state but highly competent to fold into a functional conformation. J Biochem (Tokyo) 128, 739-744.
-
(2000)
J Biochem (Tokyo)
, vol.128
, pp. 739-744
-
-
Li, Y.1
Jing, G.2
-
18
-
-
0019876883
-
Further study of the conformation of nuclease-(1-126) in relation to intrinsic enzymatic activity
-
Parker DS, Davis A & Taniuchi H (1981) Further study of the conformation of nuclease-(1-126) in relation to intrinsic enzymatic activity. J Biol Chem 256, 4557-4569.
-
(1981)
J Biol Chem
, vol.256
, pp. 4557-4569
-
-
Parker, D.S.1
Davis, A.2
Taniuchi, H.3
-
19
-
-
0028143230
-
Residual structure in a staphylococcal nuclease fragment: Is it a molten globule and is its unfolding a first-order phase transition?
-
Griko YV, Gittis A, Lattman EE & Privalov PL (1994) Residual structure in a staphylococcal nuclease fragment: is it a molten globule and is its unfolding a first-order phase transition? J Mol Biol 243, 93-99.
-
(1994)
J Mol Biol
, vol.243
, pp. 93-99
-
-
Griko, Y.V.1
Gittis, A.2
Lattman, E.E.3
Privalov, P.L.4
-
20
-
-
0015361994
-
Formation and stabilization of protein structure
-
Anfinsen CB (1972) Formation and stabilization of protein structure. Biochem J 128, 737-749.
-
(1972)
Biochem J
, vol.128
, pp. 737-749
-
-
Anfinsen, C.B.1
-
21
-
-
0015219176
-
Semisynthetic analogues of an enzymically active complex formed between two overlapping fragments of staphylococcal nuclease
-
Parikh I, Corley L & Anfinsen CB (1971) Semisynthetic analogues of an enzymically active complex formed between two overlapping fragments of staphylococcal nuclease. J Biol Chem 246, 7392-7397.
-
(1971)
J Biol Chem
, vol.246
, pp. 7392-7397
-
-
Parikh, I.1
Corley, L.2
Anfinsen, C.B.3
-
22
-
-
0141843568
-
Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: An application to Δ131Δ
-
Choy W-Y & Kay LE (2003) Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to Δ131Δ. J Am Chem Soc 125, 11988-11992.
-
(2003)
J Am Chem Soc
, vol.125
, pp. 11988-11992
-
-
Choy, W.-Y.1
Kay, L.E.2
-
23
-
-
0017618598
-
Study of equilibration of the system involving two alternative, enzymically active complementing structures simultaneously formed from two overlapping fragments of staphylococcal nuclease
-
Taniuchi H, Parker DS & Bohnert JL (1977) Study of equilibration of the system involving two alternative, enzymically active complementing structures simultaneously formed from two overlapping fragments of staphylococcal nuclease. J Biol Chem 252, 125-140.
-
(1977)
J Biol Chem
, vol.252
, pp. 125-140
-
-
Taniuchi, H.1
Parker, D.S.2
Bohnert, J.L.3
-
24
-
-
0041743075
-
Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: A study by NMR spectroscopy
-
Feng Y, Liu D & Wang J (2003) Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy. J Mol Bol 330, 821-837.
-
(2003)
J Mol Bol
, vol.330
, pp. 821-837
-
-
Feng, Y.1
Liu, D.2
Wang, J.3
-
25
-
-
7044261946
-
Searching for folding initiation sites of staphylococcal nuclease: A study of N-terminal short fragments
-
Dai J, Wang X, Feng Y, Fan G & Wang J (2004) Searching for folding initiation sites of staphylococcal nuclease: a study of N-terminal short fragments. Biopolymers 75, 229-241.
-
(2004)
Biopolymers
, vol.75
, pp. 229-241
-
-
Dai, J.1
Wang, X.2
Feng, Y.3
Fan, G.4
Wang, J.5
-
26
-
-
11344258621
-
Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease
-
Hirano S, Kamikubo H, Yamazaki Y & Kataoka M (2005) Elucidation of information encoded in tryptophan 140 of staphylococcal nuclease. Proteins: Structure, Function and Bioinformatics 56, 271-277.
-
(2005)
Proteins: Structure, Function and Bioinformatics
, vol.56
, pp. 271-277
-
-
Hirano, S.1
Kamikubo, H.2
Yamazaki, Y.3
Kataoka, M.4
-
27
-
-
0024448151
-
Calculation of protein extinction coefficients from amino acid sequence data
-
Gill SC & von Hippel H (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 181, 319-326.
-
(1989)
Anal Biochem
, vol.181
, pp. 319-326
-
-
Gill, S.C.1
Von Hippel, H.2
|