-
1
-
-
0028212643
-
Autonomous subdomains in protein folding
-
L.C. Wu, R. Grandori, and J. Carey Autonomous subdomains in protein folding Protein Sci 3 1994 369 371
-
(1994)
Protein Sci
, vol.3
, pp. 369-371
-
-
Wu, L.C.1
Grandori, R.2
Carey, J.3
-
2
-
-
0022370492
-
Compact state of a protein molecule with pronounced small-scale mobility: Bovine α-lactalbumin
-
D.A. Dolgikh, L.V. Abaturov, I.A. Bolotina, E.V. Brazhnikov, V.E. Bychkova, and R.I. Gilmanshin Compact state of a protein molecule with pronounced small-scale mobility: bovine α-lactalbumin Eur Biophys J 13 1985 109 121
-
(1985)
Eur Biophys J
, vol.13
, pp. 109-121
-
-
Dolgikh, D.A.1
Abaturov, L.V.2
Bolotina, I.A.3
Brazhnikov, E.V.4
Bychkova, V.E.5
Gilmanshin, R.I.6
-
3
-
-
77956912419
-
Acid-induced unfolding of didecameric keyhole limpet hemocyanin: Detection and characterizations of decameric and tetrameric intermediate states
-
A. Varshney, B. Ahmad, G. Rabbani, V. Kumar, S. Yadav, and R.H. Khan Acid-induced unfolding of didecameric keyhole limpet hemocyanin: detection and characterizations of decameric and tetrameric intermediate states Amino Acids 39 2010 899 910
-
(2010)
Amino Acids
, vol.39
, pp. 899-910
-
-
Varshney, A.1
Ahmad, B.2
Rabbani, G.3
Kumar, V.4
Yadav, S.5
Khan, R.H.6
-
4
-
-
0002829561
-
Molten globule-like state of human serum albumin at low pH
-
S. Muzammil, Y. Kumar, and S. Tayyab Molten globule-like state of human serum albumin at low pH Eur J Biochem 266 1999 26 32
-
(1999)
Eur J Biochem
, vol.266
, pp. 26-32
-
-
Muzammil, S.1
Kumar, Y.2
Tayyab, S.3
-
5
-
-
33847179057
-
A molten globule-like intermediate state detected in the thermal transition of cytochrome c under low salt concentration
-
S. Nakamura, T. Baba, and S. Kidokoro A molten globule-like intermediate state detected in the thermal transition of cytochrome c under low salt concentration Biophys Chem 127 2007 103 112
-
(2007)
Biophys Chem
, vol.127
, pp. 103-112
-
-
Nakamura, S.1
Baba, T.2
Kidokoro, S.3
-
6
-
-
35148850244
-
Identification and thermodynamic characterization of molten globule states of periplasmic binding proteins
-
R.S. Prajapati, S. Indu, and R. Varadarajan Identification and thermodynamic characterization of molten globule states of periplasmic binding proteins Biochemistry 46 2007 10339 10352
-
(2007)
Biochemistry
, vol.46
, pp. 10339-10352
-
-
Prajapati, R.S.1
Indu, S.2
Varadarajan, R.3
-
7
-
-
77953543617
-
More stable structure of wheat germ lipase at low pH than its native state
-
E. Ahmad, S. Fatima, M.M. Khan, and R.H. Khan More stable structure of wheat germ lipase at low pH than its native state Biochimie 92 2010 885 893
-
(2010)
Biochimie
, vol.92
, pp. 885-893
-
-
Ahmad, E.1
Fatima, S.2
Khan, M.M.3
Khan, R.H.4
-
8
-
-
0032499651
-
Bovine serum fetuin is unfolded through a molten globule state
-
C. Wang, I. Lascu, and A. Giartosio Bovine serum fetuin is unfolded through a molten globule state Biochemistry 37 1998 8457 8464
-
(1998)
Biochemistry
, vol.37
, pp. 8457-8464
-
-
Wang, C.1
Lascu, I.2
Giartosio, A.3
-
9
-
-
0034851461
-
β-Lactoglobulin molten globule induced by high pressure
-
J. Yang, A.K. Dunker, J.R. Powers, S. Clark, and B.G. Swanson β-Lactoglobulin molten globule induced by high pressure J Agric Food Chem 49 2001 3236 3243
-
(2001)
J Agric Food Chem
, vol.49
, pp. 3236-3243
-
-
Yang, J.1
Dunker, A.K.2
Powers, J.R.3
Clark, S.4
Swanson, B.G.5
-
10
-
-
0242607667
-
Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding
-
H.G. Kristinsson, and H.O. Hultin Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding J Agric Food Chem 51 2003 7187 7196
-
(2003)
J Agric Food Chem
, vol.51
, pp. 7187-7196
-
-
Kristinsson, H.G.1
Hultin, H.O.2
-
11
-
-
79953867209
-
Thermodynamic and structural properties of the acid molten globule state of horse cytochrome c
-
S. Nakamura, Y. Seki, E. Katoh, and S. Kidokoro Thermodynamic and structural properties of the acid molten globule state of horse cytochrome c Biochemistry 50 2011 3116 3126
-
(2011)
Biochemistry
, vol.50
, pp. 3116-3126
-
-
Nakamura, S.1
Seki, Y.2
Katoh, E.3
Kidokoro, S.4
-
12
-
-
0027241814
-
Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
-
A.L. Fink, L.J. Calciano, Y. Goto, M. Nishimura, and S.A. Swedberg Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease Protein Sci 2 1993 1155 1160
-
(1993)
Protein Sci
, vol.2
, pp. 1155-1160
-
-
Fink, A.L.1
Calciano, L.J.2
Goto, Y.3
Nishimura, M.4
Swedberg, S.A.5
-
13
-
-
0029917563
-
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface
-
V.E. Bychkova, A.E. Dujsekina, S.I. Klenin, E.I. Tiktopulo, V.N. Uversky, and O.B. Ptitsyn Molten globule-like state of cytochrome c under conditions simulating those near the membrane surface Biochemistry 35 1996 6058 6063
-
(1996)
Biochemistry
, vol.35
, pp. 6058-6063
-
-
Bychkova, V.E.1
Dujsekina, A.E.2
Klenin, S.I.3
Tiktopulo, E.I.4
Uversky, V.N.5
Ptitsyn, O.B.6
-
14
-
-
70349215199
-
Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes
-
J. Jiang, J. Chen, and Y.L. Xiong Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes J Agric Food Chem 57 2009 7576 7583
-
(2009)
J Agric Food Chem
, vol.57
, pp. 7576-7583
-
-
Jiang, J.1
Chen, J.2
Xiong, Y.L.3
-
15
-
-
0019084280
-
Hydrolysis of α-d-glucans and α-d-gluco-oligosaccharides by Cladosporium resinae glucoamylases
-
B.V. McCleary, and M.A. Anderson Hydrolysis of α-d-glucans and α-d-gluco-oligosaccharides by Cladosporium resinae glucoamylases Carbohydrate Res 86 1980 77 96
-
(1980)
Carbohydrate Res
, vol.86
, pp. 77-96
-
-
McCleary, B.V.1
Anderson, M.A.2
-
16
-
-
0021801286
-
General biochemical characterization of thermostable pullulanase and glucoamylase from Clostridium thermohydrosulfuricum
-
H.H. Hyun, and J.G. Zeikus General biochemical characterization of thermostable pullulanase and glucoamylase from Clostridium thermohydrosulfuricum Appl Environ Microbiol 49 1985 1168 1173
-
(1985)
Appl Environ Microbiol
, vol.49
, pp. 1168-1173
-
-
Hyun, H.H.1
Zeikus, J.G.2
-
17
-
-
4143107093
-
Direct production of ethanol from raw corn starch via fermentation by use of a novel surface-engineered yeast strain codisplaying glucoamylase and α-amylase
-
H. Shigechi, J. Koh, Y. Fujita, T. Matsumoto, Y. Bito, and M. Ueda Direct production of ethanol from raw corn starch via fermentation by use of a novel surface-engineered yeast strain codisplaying glucoamylase and α-amylase Appl Environ Microbiol 8 2004 5037 5040
-
(2004)
Appl Environ Microbiol
, vol.8
, pp. 5037-5040
-
-
Shigechi, H.1
Koh, J.2
Fujita, Y.3
Matsumoto, T.4
Bito, Y.5
Ueda, M.6
-
18
-
-
85004616477
-
Selective submerged productions of three types of glucoamylases by a Black-koji mold
-
S. Hayashida Selective submerged productions of three types of glucoamylases by a Black-koji mold Agric Biol Chem 39 1975 2093 2099
-
(1975)
Agric Biol Chem
, vol.39
, pp. 2093-2099
-
-
Hayashida, S.1
-
19
-
-
84987245995
-
Multiplicity of glucoamylase of Aspergillus oryzae. Part 1. Separation and purification of three forms of glucoamylase
-
M.N.N. Miah, and S. Ueda Multiplicity of glucoamylase of Aspergillus oryzae. Part 1. Separation and purification of three forms of glucoamylase Starch 29 1977 191 196
-
(1977)
Starch
, vol.29
, pp. 191-196
-
-
Miah, M.N.N.1
Ueda, S.2
-
20
-
-
0001040146
-
Engineering specificity and stability in glucoamylase from Aspergillus niger
-
L. Alberghin, Harwood Academic Press Amsterdam
-
T.P. Frandsen, H.P. Fierobe, and B. Svensson Engineering specificity and stability in glucoamylase from Aspergillus niger L. Alberghin, Protein engineering in industrial biotechnology 1999 Harwood Academic Press Amsterdam 189 206
-
(1999)
Protein Engineering in Industrial Biotechnology
, pp. 189-206
-
-
Frandsen, T.P.1
Fierobe, H.P.2
Svensson, B.3
-
21
-
-
0001421133
-
The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger
-
B. Svensson, K. Larsen, I. Svendsen, and E. Boel The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger Carlsberg Res Commun 48 1983 529 544
-
(1983)
Carlsberg Res Commun
, vol.48
, pp. 529-544
-
-
Svensson, B.1
Larsen, K.2
Svendsen, I.3
Boel, E.4
-
22
-
-
0023040629
-
Characterization of a glucoamylase G2 from Aspergillus niger
-
B. Svensson, K. Larsen, and A. Gunnarsson Characterization of a glucoamylase G2 from Aspergillus niger Eur J Biochem 154 1986 497 502
-
(1986)
Eur J Biochem
, vol.154
, pp. 497-502
-
-
Svensson, B.1
Larsen, K.2
Gunnarsson, A.3
-
23
-
-
0024430052
-
Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes
-
B. Svensson, H. Jespersen, M.R. Sierks, and E.A. Mac-Gregor Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes Biochem J 264 1989 309 311
-
(1989)
Biochem J
, vol.264
, pp. 309-311
-
-
Svensson, B.1
Jespersen, H.2
Sierks, M.R.3
Mac-Gregor, E.A.4
-
24
-
-
0035834494
-
Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose
-
T. Giardina, A.P. Gunning, N. Juge, C.B. Faulds, C.S.M. Furniss, and B. Svensson Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose J Mol Biol 313 2001 1149 1159
-
(2001)
J Mol Biol
, vol.313
, pp. 1149-1159
-
-
Giardina, T.1
Gunning, A.P.2
Juge, N.3
Faulds, C.B.4
Furniss, C.S.M.5
Svensson, B.6
-
25
-
-
0026663907
-
O-Glycosylation and stability. Unfolding of glucoamylase induced by heat and guanidine hydrochloride
-
G. Williamson, N.J. Belshaw, T.R. Noel, S.G. Ring, and M.P. Williamson O-Glycosylation and stability. Unfolding of glucoamylase induced by heat and guanidine hydrochloride Eur J Biochem 207 1992 661 670
-
(1992)
Eur J Biochem
, vol.207
, pp. 661-670
-
-
Williamson, G.1
Belshaw, N.J.2
Noel, T.R.3
Ring, S.G.4
Williamson, M.P.5
-
26
-
-
79951483232
-
Structure of the catalytic domain of glucoamylase from Aspergillus niger
-
J. Lee, and M. Paetzel Structure of the catalytic domain of glucoamylase from Aspergillus niger Acta Crystallogr F67 2011 188 192
-
(2011)
Acta Crystallogr
, vol.F67
, pp. 188-192
-
-
Lee, J.1
Paetzel, M.2
-
27
-
-
0030604713
-
Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy
-
K. Sorimachi, A.J. Jacks, M.-F.L. Le Gal-Coeffet, G. Williamson, D.B. Archer, and M.P. Williamson Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy J Mol Biol 259 1996 970 987
-
(1996)
J Mol Biol
, vol.259
, pp. 970-987
-
-
Sorimachi, K.1
Jacks, A.J.2
Le Gal-Coeffet, M.-F.L.3
Williamson, G.4
Archer, D.B.5
Williamson, M.P.6
-
28
-
-
0033545898
-
Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry
-
T. Christensen, B. Svensson, and B.W. Sigurskjold Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry Biochemistry 38 1999 6300 6310
-
(1999)
Biochemistry
, vol.38
, pp. 6300-6310
-
-
Christensen, T.1
Svensson, B.2
Sigurskjold, B.W.3
-
29
-
-
85011143323
-
Kinetic and circular dichroism spectroscopic comparison among three forms of glucoamylase from a Rhizopus sp
-
T. Takahashi, M. Iwama, Y. Tsuchida, and M. Irie Kinetic and circular dichroism spectroscopic comparison among three forms of glucoamylase from a Rhizopus sp. Chem Pharm Bull 33 1985 276 281
-
(1985)
Chem Pharm Bull
, vol.33
, pp. 276-281
-
-
Takahashi, T.1
Iwama, M.2
Tsuchida, Y.3
Irie, M.4
-
30
-
-
0030903699
-
Characterisation of a xylanolytic amyloglucosidase of Termitomyces clypeatus
-
A.K. Ghosh, A.K. Naskar, and S. Sengupta Characterisation of a xylanolytic amyloglucosidase of Termitomyces clypeatus Biochim Biophys Acta 1339 1997 289 296
-
(1997)
Biochim Biophys Acta
, vol.1339
, pp. 289-296
-
-
Ghosh, A.K.1
Naskar, A.K.2
Sengupta, S.3
-
31
-
-
77957747579
-
Study of conformational changes in glucoamylase of Aspergillus awamori nakazawa in presence of denaturants through CD-spectroscopy
-
S. Negi, and R. Banerjee Study of conformational changes in glucoamylase of Aspergillus awamori nakazawa in presence of denaturants through CD-spectroscopy Bioresource Technol 101 2010 7577 7580
-
(2010)
Bioresource Technol
, vol.101
, pp. 7577-7580
-
-
Negi, S.1
Banerjee, R.2
-
32
-
-
0001477783
-
The role of tryptophanyl residues in the function of Aspergillus niger glucoamylase G1 and G2
-
A.J. Clarke, and B. Svensson The role of tryptophanyl residues in the function of Aspergillus niger glucoamylase G1 and G2 Carlsberg Res Commun 49 1984 111 122
-
(1984)
Carlsberg Res Commun
, vol.49
, pp. 111-122
-
-
Clarke, A.J.1
Svensson, B.2
-
34
-
-
44049102957
-
Peptide sequence and conformation strongly influence tryptophan fluorescence
-
R.W. Alston, M. Lasagna, G.R. Grimsley, J.M. Scholtz, G.D. Reinhart, and C.N. Pace Peptide sequence and conformation strongly influence tryptophan fluorescence Biophys J 94 2008 2280 2287
-
(2008)
Biophys J
, vol.94
, pp. 2280-2287
-
-
Alston, R.W.1
Lasagna, M.2
Grimsley, G.R.3
Scholtz, J.M.4
Reinhart, G.D.5
Pace, C.N.6
-
35
-
-
0002343673
-
Measuring the conformational stability of a protein
-
T.E. Greighton, Oxford University Press New York
-
C.N. Pace, B.A. Shirley, and J.A. Thomson Measuring the conformational stability of a protein T.E. Greighton, Protein structure: a practical approach 1989 Oxford University Press New York 311 330
-
(1989)
Protein Structure: A Practical Approach
, pp. 311-330
-
-
Pace, C.N.1
Shirley, B.A.2
Thomson, J.A.3
-
36
-
-
0034237709
-
Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation
-
S. Muzammil, Y. Kumar, and S. Tayyab Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation Proteins: Struct Funct Genet 40 2000 29 38
-
(2000)
Proteins: Struct Funct Genet
, vol.40
, pp. 29-38
-
-
Muzammil, S.1
Kumar, Y.2
Tayyab, S.3
-
37
-
-
0015522150
-
Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
-
Y.-H. Chen, J.T. Yang, and H.M. Martinez Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion Biochemistry 11 1972 4120 4131
-
(1972)
Biochemistry
, vol.11
, pp. 4120-4131
-
-
Chen, Y.-H.1
Yang, J.T.2
Martinez, H.M.3
-
38
-
-
37849031520
-
Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase
-
T. Iida, S. Nishimura, M. Mochizuki, S. Uchiyama, T. Ohkubo, and Y. Urade Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase FEBS J 275 2008 233 241
-
(2008)
FEBS J
, vol.275
, pp. 233-241
-
-
Iida, T.1
Nishimura, S.2
Mochizuki, M.3
Uchiyama, S.4
Ohkubo, T.5
Urade, Y.6
-
39
-
-
0344012492
-
Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group
-
M. Yagi, K. Sakurai, C. Kalidas, C.A. Batt, and Y. Goto Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group J Biol Chem 278 2003 47009 47015
-
(2003)
J Biol Chem
, vol.278
, pp. 47009-47015
-
-
Yagi, M.1
Sakurai, K.2
Kalidas, C.3
Batt, C.A.4
Goto, Y.5
-
40
-
-
0019593952
-
Fluorescence quenching studies with proteins
-
M.R. Eftink, and C.A. Ghiron Fluorescence quenching studies with proteins Anal Biochem 114 1981 199 227
-
(1981)
Anal Biochem
, vol.114
, pp. 199-227
-
-
Eftink, M.R.1
Ghiron, C.A.2
-
41
-
-
0032516445
-
Proline isomerization-independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed α/β protein, Escherichia coli thioredoxin
-
R.E. Georgescu, J.-H. Li, M.E. Goldberg, M.L. Tasayco, and A.F. Chaffotte Proline isomerization-independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed α/β protein, Escherichia coli thioredoxin Biochemistry 37 1998 10286 10297
-
(1998)
Biochemistry
, vol.37
, pp. 10286-10297
-
-
Georgescu, R.E.1
Li, J.-H.2
Goldberg, M.E.3
Tasayco, M.L.4
Chaffotte, A.F.5
-
42
-
-
51649164504
-
Structure and stability of glucoamylase II from Aspergillus niger: A circular dichroism study
-
B.C. Shenoy, A.G.A. Rao, and M.R.R. Rao Structure and stability of glucoamylase II from Aspergillus niger: a circular dichroism study J Biosci 6 1984 601 611
-
(1984)
J Biosci
, vol.6
, pp. 601-611
-
-
Shenoy, B.C.1
Rao, A.G.A.2
Rao, M.R.R.3
-
43
-
-
0029115374
-
Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
-
M. Engelhard, and P.A. Evans Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates Protein Sci 4 1995 1553 1562
-
(1995)
Protein Sci
, vol.4
, pp. 1553-1562
-
-
Engelhard, M.1
Evans, P.A.2
-
44
-
-
0025195499
-
Mechanism of acid-induced folding of proteins
-
Y. Goto, N. Takahashi, and A.L. Fink Mechanism of acid-induced folding of proteins Biochemistry 29 1990 3480 3488
-
(1990)
Biochemistry
, vol.29
, pp. 3480-3488
-
-
Goto, Y.1
Takahashi, N.2
Fink, A.L.3
-
45
-
-
0023037907
-
Conformational changes induced by binding of divalent cations to calregulin
-
N.C. Khanna, M. Tokuda, and D.M. Waisman Conformational changes induced by binding of divalent cations to calregulin J Biol Chem 261 1986 8883 8887
-
(1986)
J Biol Chem
, vol.261
, pp. 8883-8887
-
-
Khanna, N.C.1
Tokuda, M.2
Waisman, D.M.3
-
46
-
-
0016721630
-
Purification and characterization of Aspergillus niger exo-1,4-glucosidase
-
I.M. Freedberg, Y. Levin, C.M. Kay, W.D. McCubbin, and E. Katchalski-Katzir Purification and characterization of Aspergillus niger exo-1,4-glucosidase Biochim Biophys Acta 391 1975 361 381
-
(1975)
Biochim Biophys Acta
, vol.391
, pp. 361-381
-
-
Freedberg, I.M.1
Levin, Y.2
Kay, C.M.3
McCubbin, W.D.4
Katchalski-Katzir, E.5
-
47
-
-
0026726797
-
Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2- resolution
-
A. Aleshin, A. Golubev, L.M. Firsov, and R.B. Honzatko Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2- resolution J Biol Chem 267 1992 19291 19298
-
(1992)
J Biol Chem
, vol.267
, pp. 19291-19298
-
-
Aleshin, A.1
Golubev, A.2
Firsov, L.M.3
Honzatko, R.B.4
-
48
-
-
0014201795
-
Proteins as random coils. III. Optical rotatory dispersion in 6 M guanidine hydrochloride
-
C. Tanford, K. Kawahara, S. Lapanje, T.M. Hooker Jr., M.H. Zarlengo, and A. Salahuddin Proteins as random coils. III. Optical rotatory dispersion in 6 M guanidine hydrochloride J Am Chem Soc 89 1967 5023 5029
-
(1967)
J Am Chem Soc
, vol.89
, pp. 5023-5029
-
-
Tanford, C.1
Kawahara, K.2
Lapanje, S.3
Hooker, Jr.T.M.4
Zarlengo, M.H.5
Salahuddin, A.6
-
49
-
-
0034719144
-
The stability, structural organization, and denaturation of pectate lyase C, a parallel β-helix protein
-
D.E. Kamen, Y. Griko, and R.W. Woody The stability, structural organization, and denaturation of pectate lyase C, a parallel β-helix protein Biochemistry 39 2000 15932 15943
-
(2000)
Biochemistry
, vol.39
, pp. 15932-15943
-
-
Kamen, D.E.1
Griko, Y.2
Woody, R.W.3
-
50
-
-
0030803337
-
Highly ordered molten globule-like state of ovalbumin at acidic pH: Native-like fragmentation by protease and selective modification of Cys367 with dithiodipyridine
-
E. Tatsumi, and M. Hirose Highly ordered molten globule-like state of ovalbumin at acidic pH: native-like fragmentation by protease and selective modification of Cys367 with dithiodipyridine J Biochem 122 1997 300 308
-
(1997)
J Biochem
, vol.122
, pp. 300-308
-
-
Tatsumi, E.1
Hirose, M.2
-
51
-
-
34248573609
-
Native-like tertiary structure in the Mucor miehei lipase molten globule state obtained at low pH
-
S. Fatima, B. Ahmad, and R.H. Khan Native-like tertiary structure in the Mucor miehei lipase molten globule state obtained at low pH IUBMB Life 59 2007 179 186
-
(2007)
IUBMB Life
, vol.59
, pp. 179-186
-
-
Fatima, S.1
Ahmad, B.2
Khan, R.H.3
-
53
-
-
0040532391
-
Formation of disulfide-bridged dimers during thermoinactivation of glucoamylase from Aspergillus niger
-
Z. Sasvari, and B. Asboth Formation of disulfide-bridged dimers during thermoinactivation of glucoamylase from Aspergillus niger Enzyme Microb Technol 22 1998 466 470
-
(1998)
Enzyme Microb Technol
, vol.22
, pp. 466-470
-
-
Sasvari, Z.1
Asboth, B.2
-
54
-
-
0029904281
-
Influence of the carbohydrate moiety on the stability of glycoproteins
-
C. Wang, M. Eufemi, C. Turano, and A. Giartosio Influence of the carbohydrate moiety on the stability of glycoproteins Biochemistry 35 1996 7299 7307
-
(1996)
Biochemistry
, vol.35
, pp. 7299-7307
-
-
Wang, C.1
Eufemi, M.2
Turano, C.3
Giartosio, A.4
-
56
-
-
77949278164
-
Characterization of a neutral and thermostable glucoamylase from the thermophilic mold Thermomucor indicae-seudaticae: Activity, stability, and structural correlation
-
P. Kumar, A. Islam, F. Ahmad, and T. Satyanarayana Characterization of a neutral and thermostable glucoamylase from the thermophilic mold Thermomucor indicae-seudaticae: activity, stability, and structural correlation Appl Biochem Biotechnol 160 2010 879 890
-
(2010)
Appl Biochem Biotechnol
, vol.160
, pp. 879-890
-
-
Kumar, P.1
Islam, A.2
Ahmad, F.3
Satyanarayana, T.4
-
57
-
-
0028346251
-
Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine hydrochloride
-
Y. Hagihara, Y. Tan, and Y. Goto Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine hydrochloride J Mol Biol 237 1994 336 348
-
(1994)
J Mol Biol
, vol.237
, pp. 336-348
-
-
Hagihara, Y.1
Tan, Y.2
Goto, Y.3
-
58
-
-
17444391310
-
Conformational study of spectrin in presence of submolar concentrations of denaturants
-
S. Ray, M. Bhattacharyya, and A. Chakrabarti Conformational study of spectrin in presence of submolar concentrations of denaturants J Fluoresc 15 2005 61 70
-
(2005)
J Fluoresc
, vol.15
, pp. 61-70
-
-
Ray, S.1
Bhattacharyya, M.2
Chakrabarti, A.3
-
59
-
-
0035912911
-
Structure and dynamics of the α-lactalbumin molten globule: Fluorescence studies using proteins containing a single tryptophan residue
-
S. Chakraborty, V. Ittah, P. Bai, L. Luo, E. Haas, and Z. Peng Structure and dynamics of the α-lactalbumin molten globule: fluorescence studies using proteins containing a single tryptophan residue Biochemistry 40 2001 7228 7238
-
(2001)
Biochemistry
, vol.40
, pp. 7228-7238
-
-
Chakraborty, S.1
Ittah, V.2
Bai, P.3
Luo, L.4
Haas, E.5
Peng, Z.6
-
60
-
-
11244315482
-
PH-dependent quenching of the fluorescence of tryptophan residues in class A β-lactamase from E. coli (TEM-1)
-
C. Christov, D. Ianev, A. Shosheva, and B. Atanasov pH-dependent quenching of the fluorescence of tryptophan residues in class A β-lactamase from E. coli (TEM-1) Z Naturforsch 59 2004 824 827
-
(2004)
Z Naturforsch
, vol.59
, pp. 824-827
-
-
Christov, C.1
Ianev, D.2
Shosheva, A.3
Atanasov, B.4
-
61
-
-
79960189580
-
Effect of pH on the interaction of baicalein with lysozyme by spectroscopic approaches
-
D. Li, T. Zhang, C. Xu, and B. Ji Effect of pH on the interaction of baicalein with lysozyme by spectroscopic approaches J Photochem Photobiol B 104 2011 414 424
-
(2011)
J Photochem Photobiol B
, vol.104
, pp. 414-424
-
-
Li, D.1
Zhang, T.2
Xu, C.3
Ji, B.4
-
62
-
-
7044231247
-
Interactions of human serum albumin with chlorogenic acid and ferulic acid
-
J. Kang, Y. Liu, M.X. Xie, S. Li, M. Jiang, and Y.D. Wang Interactions of human serum albumin with chlorogenic acid and ferulic acid Biochim Biophys Acta 1674 2004 205 214
-
(2004)
Biochim Biophys Acta
, vol.1674
, pp. 205-214
-
-
Kang, J.1
Liu, Y.2
Xie, M.X.3
Li, S.4
Jiang, M.5
Wang, Y.D.6
-
63
-
-
0000200876
-
Studies on the ultraviolet difference spectra of proteins and polypeptides
-
A.N. Glazer, and E.L. Smith Studies on the ultraviolet difference spectra of proteins and polypeptides J Biol Chem 236 1961 2942 2947
-
(1961)
J Biol Chem
, vol.236
, pp. 2942-2947
-
-
Glazer, A.N.1
Smith, E.L.2
-
64
-
-
0027423090
-
Acid-induced unfolding and refolding transitions of cytochrome c: A three-state mechanism in water and deuterium oxide
-
Y. Goto, Y. Hagihara, D. Hamada, M. Hoshino, and I. Nishii Acid-induced unfolding and refolding transitions of cytochrome c: a three-state mechanism in water and deuterium oxide Biochemistry 32 1993 11878 11885
-
(1993)
Biochemistry
, vol.32
, pp. 11878-11885
-
-
Goto, Y.1
Hagihara, Y.2
Hamada, D.3
Hoshino, M.4
Nishii, I.5
-
65
-
-
0028243107
-
Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
-
I. Nishii, M. Kataoka, F. Tokunaga, and Y. Goto Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding Biochemistry 33 1994 4903 4909
-
(1994)
Biochemistry
, vol.33
, pp. 4903-4909
-
-
Nishii, I.1
Kataoka, M.2
Tokunaga, F.3
Goto, Y.4
-
66
-
-
0024417964
-
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
K. Kuwajima The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure Proteins: Struct Funct Bioinform 6 1989 87 103
-
(1989)
Proteins: Struct Funct Bioinform
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
|