-
1
-
-
0025370815
-
Dominant forces in protein folding
-
DOI 10.1021/bi00483a001
-
Dill, K.A. Dominant forces in protein folding. Biochemistry 1990, 29 (30), 7133-7155. (Pubitemid 20230041)
-
(1990)
Biochemistry
, vol.29
, Issue.31
, pp. 7133-7155
-
-
Dill, K.A.1
-
2
-
-
0024963570
-
Conformational states of beta-lactamase: Molten globule state at acidic and alkaline pH with high salt
-
Goto, A.; Fink, A.L. Conformational states of beta-lactamase: Molten globule state at acidic and alkaline pH with high salt. Biochemistry 1989, 28 (3), 945-952.
-
(1989)
Biochemistry
, vol.28
, Issue.3
, pp. 945-952
-
-
Goto, A.1
Fink, A.L.2
-
3
-
-
0002643399
-
Minimizing protein interactions
-
Creighton, T.E.; Ed.; Information Press: Oxford, UK
-
Volkin, D.B.; Klibanov, A.M. Minimizing protein interactions. In Protein Function: A practical approach; Creighton, T.E.; Ed.; Information Press: Oxford, UK, 1989, 1-24.
-
(1989)
Protein Function: A Practical Approach
, pp. 1-24
-
-
Volkin, D.B.1
Klibanov, A.M.2
-
4
-
-
0028367331
-
Structural characterization of a highly-ordered 'molten globule' at low pH
-
Christina, R.; Smith, R.A.G.; Dobson, C.M. Structural characterization of highly- ordered 'molten globule' at low pH. Nature Structural Biology 1994, 1, 23-29. (Pubitemid 24974776)
-
(1994)
Nature Structural Biology
, vol.1
, Issue.1
, pp. 23-29
-
-
Redfield, C.1
Smith, R.A.G.2
Dobson, C.M.3
-
5
-
-
0032754813
-
Polyol-induced molten globule of cytochrome c: An evidence for stabilization by hydrophobic interaction
-
DOI 10.1016/S0167-4838(99)00159-4, PII S0167483899001594
-
Kamiyama, T.; Sadahide, Y.; Nogusa, Y.; Gekko, K. Polyols-induced molten globule of cytochrome c: An evidence for stabilization by hydrophobic interaction. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology 1999, 1434, 44-57. (Pubitemid 29521331)
-
(1999)
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
, vol.1434
, Issue.1
, pp. 44-57
-
-
Kamiyama, T.1
Sadahide, Y.2
Nogusa, Y.3
Gekko, K.4
-
6
-
-
0027400842
-
Molten globule of cytochrome c studied by small angle X-ray scattering
-
DOI 10.1006/jmbi.1993.1064
-
Kataoka, M.; Hagihara, Y.; Mihara, K.; Goto, Y. Molten globule of cytochrome c studied by small angle X-ray scattering. Journal of Molecular Biology 1993, 229, 591-596. (Pubitemid 23068036)
-
(1993)
Journal of Molecular Biology
, vol.229
, Issue.3
, pp. 591-596
-
-
Kataoka, M.1
Hagihara, Y.2
Mihara, K.3
Got, Y.4
-
7
-
-
0028243107
-
Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
-
DOI 10.1021/bi00182a019
-
Nishii, I.; Kataoka, M.; Tokunaga, F.; Goto, Y. Cold denaturation of molten globule states of apomyoglobin and a profile for protein folding. Biochemistry 1994, 33 (16), 4903-4909. (Pubitemid 24158440)
-
(1994)
Biochemistry
, vol.33
, Issue.16
, pp. 4903-4909
-
-
Nishii, I.1
Kataoka, M.2
Tokunaga, F.3
Goto, Y.4
-
8
-
-
0025982146
-
Molten globule intermediates and protein folding
-
Christensen, H.; Pain, R.H. Molten globule intermediates and protein folding. European Biophysics Journal 1991, 19, 221-229.
-
(1991)
European Biophysics Journal
, vol.19
, pp. 221-229
-
-
Christensen, H.1
Pain, R.H.2
-
9
-
-
0024447135
-
Microcalorimetric studies of conformational transitions of ferricytochrome c in acidic solution
-
DOI 10.1016/0301-4622(89)80041-9
-
Potekhin, S.; Pfeil, W. Microcalorimetric studies of conformational transitions of ferrycy- tochrome c in acidic solution. Biophysical Chemistry 1989, 34 (1), 55-62. (Pubitemid 19240371)
-
(1989)
Biophysical Chemistry
, vol.34
, Issue.1
, pp. 55-62
-
-
Potekhin, S.1
Pfeil, W.2
-
10
-
-
0036731234
-
Modulation of globular protein functionality by weakly interacting cosolvents
-
DOI 10.1080/20024091054210
-
McClements, D.J. Modulation of globular protein functionality by weakly interacting cosol- vents. Critical Reviewes in Food Sciences and Nutrition 2002, 42, 417-471. (Pubitemid 39649737)
-
(2002)
Critical Reviews in Food Science and Nutrition
, vol.42
, Issue.5
, pp. 417-471
-
-
McClements, D.J.1
-
11
-
-
0019872612
-
Thermodynamic and kinetic examination of protein stabilization by glycerol
-
Gekko, K.; Timasheff, S.N. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry 1981, 20 (16), 4677-4686.
-
(1981)
Biochemistry
, vol.20
, Issue.16
, pp. 4677-4686
-
-
Gekko, K.1
Timasheff, S.N.2
-
12
-
-
0025268101
-
Competing solvent effects of polyols and guanidine hydrochloride on protein stability
-
Gekko, K.; Ito, H. Competing solvent effects of polyols and guanidine hydrochloride on protein stability. The Journal of Biochemistry 1990, 107, 572-577. (Pubitemid 20120324)
-
(1990)
Journal of Biochemistry
, vol.107
, Issue.4
, pp. 572-577
-
-
Gekko, K.1
Ito, H.2
-
13
-
-
0019741203
-
Mechanism of polyol-induced protein stabilization: Solubility of amino acids and diglycine in aqueous polyol solutions
-
Gekko, K. Mechanism of polyol-induced protein stabilization: Solubility of amino acids and diglycine in aqueous polyol solutions. The Journal of Biochemistry 1981, 90 (6), 1633-1641.
-
(1981)
The Journal of Biochemistry
, vol.90
, Issue.6
, pp. 1633-1641
-
-
Gekko, K.1
-
14
-
-
0031013887
-
Mechanism of stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denatured than for the native protein
-
Xie, G.; Timasheff, S.N. Mechanism of stabilization of ribonuclease A by sorbitol: Preferential hydration is greater for the denatured than for the native protein. Protein Science 1997, 6 (1), 211-222.
-
(1997)
Protein Science
, vol.6
, Issue.1
, pp. 211-222
-
-
Xie, G.1
Timasheff, S.N.2
-
15
-
-
0025101548
-
Acid induced unfolding of proteins
-
Goto, Y.; Calciano, L.J.; Fink, A.L. Acid induced unfolding of proteins. Proceedings of National Academy of Sciences, USA 1990, 87, 573-577.
-
(1990)
Proceedings of National Academy of Sciences, USA
, vol.87
, pp. 573-577
-
-
Goto, Y.1
Calciano, L.J.2
Fink, A.L.3
-
16
-
-
0028931842
-
Mechanism of solvents induced thermal stabilization of a- amylase from Bacillus amyloliquefaciens
-
Rajendran, S.; Radha, C.; Prakash, V. Mechanism of solvents induced thermal stabilization of a- amylase from Bacillus amyloliquefaciens. International Journal of Peptide and Protein Research 1995, 45, 122-128.
-
(1995)
International Journal of Peptide and Protein Research
, vol.45
, pp. 122-128
-
-
Rajendran, S.1
Radha, C.2
Prakash, V.3
-
17
-
-
0027995384
-
Classification of acid denaturation of proteins: Intermediates and unfolded states
-
504-12, 511
-
Fink, A.L.; Calciano, L.J.; Kurotsu, T.; Palleros, D.R. Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry, 1994, 33, 12, 504-12, 511.
-
(1994)
Biochemistry
, vol.33
, pp. 12
-
-
Fink, A.L.1
Calciano, L.J.2
Kurotsu, T.3
Palleros, D.R.4
-
18
-
-
0029866454
-
Purification and characterization of a truncated Bacillus subtilis a-amylase produced by Escherichia coli
-
DOI 10.1007/s002530050627
-
Marco, J.L.; Bataus, L.A.; Valencia, F.F.; Ulhoa, C.J.; Astolfi-Filho, S.; Felix, C.R. Purification and characterization of a truncated Bacillus subtillis a-amylase produced by Escherichia coli. Applied Microbiology and Biotechnology 1996, 44, 746-752. (Pubitemid 26074252)
-
(1996)
Applied Microbiology and Biotechnology
, vol.44
, Issue.6
, pp. 746-752
-
-
Marco, J.L.1
Bataus, L.A.2
Valencia, F.F.3
Ulhoa, C.J.4
Astolfi-Filho, S.5
Felix, C.R.6
-
19
-
-
0028429952
-
Protein engineering in the alpha-amylase family: Catalytic mechanism, substrate specificity, and stability
-
Svensson, B. Protein engineering in a-amylase family: Catalytic mechanism, substrate specificity, and stability. Plant Molecular Biology 1994, 25, 141-157. (Pubitemid 2103155)
-
(1994)
Plant Molecular Biology
, vol.25
, Issue.2
, pp. 141-157
-
-
Svensson, B.1
-
20
-
-
0035831255
-
Relationship of sequence and structure to specificity in the a-amylase family of enzymes
-
DOI 10.1016/S0167-4838(00)00302-2, PII S0167483800003022
-
MacGregor, E.A.; Janecek, S.; Svensson, B. Relation of sequence and structure to specificity in the alpha amylase family of enzymes. Biochimica et Biophysica Acta 2001, 1546, 1-20. (Pubitemid 32217799)
-
(2001)
Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
, vol.1546
, Issue.1
, pp. 1-20
-
-
MacGregor E.Ann1
Janecek, S.2
Svensson, B.3
-
21
-
-
0033614827
-
X-ray structure of Novamyl, the five domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: Maltose and ascarbose complexes at 1.7 A° resolution
-
Dauter, Z.; Dauter, M.; Brzozowski, A.M.; Christensen, S.; Borchert, T.V.; Beier, L.; Wilson, K.S.; Devies, G.J. X-ray structure of Novamyl, the five domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: Maltose and ascarbose complexes at 1.7 A° resolution. Biochemistry 1999, 38, 8385-8392.
-
(1999)
Biochemistry
, vol.38
, pp. 8385-8392
-
-
Dauter, Z.1
Dauter, M.2
Brzozowski, A.M.3
Christensen, S.4
Borchert, T.V.5
Beier, L.6
Wilson, K.S.7
Devies, G.J.8
-
22
-
-
71849104860
-
Protein measurement with the Folin phenol reagent
-
Lowry, O.H.; Rosenborough, N.J.; Farr, A.L.; Randall, R.J. Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 1951, 193, 265-275.
-
(1951)
Journal of Biological Chemistry
, vol.193
, pp. 265-275
-
-
Lowry, O.H.1
Rosenborough, N.J.2
Farr, A.L.3
Randall, R.J.4
-
24
-
-
0032571789
-
Amylase measurement with 2-chloro-4-nitrophenyl maltotrioside as substrate
-
DOI 10.1016/S0009-8981(98)00009-6, PII S0009898198000096
-
Foo, A.Y.; Bais, R. Amylase measurement with 2-chloro-4-nitrophenyl maltotrioside as substrate. Clinica Chimica Acta 1998, 272, 137-147. (Pubitemid 28279779)
-
(1998)
Clinica Chimica Acta
, vol.272
, Issue.2
, pp. 137-147
-
-
Foo, A.Y.1
Bais, R.2
-
25
-
-
0023271964
-
Rapid determination of a-amylase activity by use of a new chromogenic substrate
-
Dupuy, G.; Hilaire, G.; Aubry, C. Rapid determination of a-amylase activity by use of a new chromogenic substrate. Clinical Chemistry 1987, 3314, 524-528. (Pubitemid 17157868)
-
(1987)
Clinical Chemistry
, vol.33
, Issue.4
, pp. 524-528
-
-
Dupuy, G.1
Hilaire, G.2
Aubry, C.3
-
26
-
-
0034237678
-
Structural characterization of acid-induced intermediates of human glutathione transferase P1-1
-
DOI 10.1016/S1357-2725(00)00018-2, PII S1357272500000182
-
Dragani, B.; Cocco, R.; Principe, D.R.; Cicconetti, M.; Aceto, A. Structural characterization of acid induced intermediates of human glutathione transferase P1.1. The International Journal of Biochemistry and Cell Biology 2000, 32, 725-736. (Pubitemid 30336464)
-
(2000)
International Journal of Biochemistry and Cell Biology
, vol.32
, Issue.7
, pp. 725-736
-
-
Dragani, B.1
Cocco, R.2
Principe, D.R.3
Cicconetti, M.4
Aceto, A.5
-
27
-
-
0019593952
-
Fluorescence quenching studies with proteins
-
Eftink, M.R.; Ghiron, C.A. Fluorescence quenching studies with proteins. Analytical Biochemistry 1982, 114, 199-227.
-
(1982)
Analytical Biochemistry
, vol.114
, pp. 199-227
-
-
Eftink, M.R.1
Ghiron, C.A.2
-
28
-
-
0022503457
-
Calculation of protein conformation from circular dichroism
-
Yang, J.T.; Wu, C.S.C.; Martinez, H.M. Calculation of protein conformation from circular dichroism. Methods in Enzymology 1986, 130, 208-269.
-
(1986)
Methods in Enzymology
, vol.130
, pp. 208-269
-
-
Yang, J.T.1
Wu, C.S.C.2
Martinez, H.M.3
-
29
-
-
0036295226
-
Stabilization of molten globule state of papain by urea
-
DOI 10.1006/bbrc.2002.6368
-
Edwin, F.; Sharma, Y.V.; Jagannadham, M.V. Stabilization of molten globule state of papain by urea. Biochemical and Biophysical Research Communication 2002, 290, 1441-1446. (Pubitemid 34687419)
-
(2002)
Biochemical and Biophysical Research Communications
, vol.290
, Issue.5
, pp. 1441-1446
-
-
Edwin, F.1
Valkya Sharma, Y.2
Jagannadham, M.V.3
-
30
-
-
0032782071
-
Instability, stabilization, and formulation of liquid protein pharmaceuticals
-
DOI 10.1016/S0378-5173(99)00152-0, PII S0378517399001520
-
Wang, W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. International Journal of Pharmacology 1999, 185, 129-188. (Pubitemid 29392904)
-
(1999)
International Journal of Pharmaceutics
, vol.185
, Issue.2
, pp. 129-188
-
-
Wang, W.1
-
31
-
-
0033756327
-
Characterization of acid induced unfolding intermediates of glucose/xylose isomerase
-
Pawar, S.A.; Deshpande, V.V. Characterization of acid induced unfolding intermediates of glucose/xylose isomerase. European Journal of Biochemistry 2000, 267, 6331-6338.
-
(2000)
European Journal of Biochemistry
, vol.267
, pp. 6331-6338
-
-
Pawar, S.A.1
Deshpande, V.V.2
-
32
-
-
0029115374
-
Kinetics of interaction of partially folded proteins with a hydropho- bic dye: Evidence that molten globule character is maximal in early folding intermediates
-
Engelhard, M.; Evans, P.A. Kinetics of interaction of partially folded proteins with a hydropho- bic dye: Evidence that molten globule character is maximal in early folding intermediates. Protein Science 1995, 4, 1553-1562.
-
(1995)
Protein Science
, vol.4
, pp. 1553-1562
-
-
Engelhard, M.1
Evans, P.A.2
-
33
-
-
33745304954
-
Effect of polyols and salts on the acid-induced state of human placental cystatin
-
DOI 10.1134/S0006297906060058
-
Rashid, F.; Sharma, S.; Baig, M.A.; Bano, A. Effect of polyols and salts on the acid- induced state of human placental cystatin. Biochemistry (Moscow) 2006, 71, 619-626. (Pubitemid 43937037)
-
(2006)
Biochemistry (Moscow)
, vol.71
, Issue.6
, pp. 619-626
-
-
Rashid, F.1
Sharma, S.2
Baig, M.A.3
Bano, B.4
-
34
-
-
0042265528
-
Effect of urea at lower concentration on the structure of papain - Formation of a stable molten globule and its characterization
-
Sathish, H.A.; Kumar, P.R.; Prakash, V. Effect of urea at lower concentration on the structure of papain: Formation of a stable molten globule and its characterization. Indian Journal of Biochemistry and Biophysics 2002, 39, 155-162. (Pubitemid 36928232)
-
(2002)
Indian Journal of Biochemistry and Biophysics
, vol.39
, Issue.3
, pp. 155-162
-
-
Sathish, H.A.1
Kumar, P.R.2
Prakash, V.3
-
35
-
-
0041590998
-
Molten globule intermediates of human serum albumin in low concentration of urea
-
Muralidhara, B.K.; Prakash, V. Molten globule intermediates of human serum albumin in low concentration of urea. Indian Journal of Biochemistry and Biophysics 2002, 39, 318-324. (Pubitemid 36937289)
-
(2002)
Indian Journal of Biochemistry and Biophysics
, vol.39
, Issue.5
, pp. 318-324
-
-
Muralidhara, B.K.1
Prakash, V.2
-
36
-
-
2942549124
-
Acid-induced conformational changes in Bacillus amyloliquefaciens a-amylase: Appearance of a molten globule like state
-
DOI 10.1016/j.enzmictec.2004.03.006, PII S014102290400078X
-
Asghari, S.M.; Khajeh, K.; Moradian, F.; Ranjbar, B.; Naderi-Manesh, H. Acid-induced conformational changes in Bacillus amyloliquefaciens a-amylase: Appearance of molten globule likes state. Enzyme Microbial Technology 2004, 35, 51-57. (Pubitemid 38759794)
-
(2004)
Enzyme and Microbial Technology
, vol.35
, Issue.1
, pp. 51-57
-
-
Asghari, S.M.1
Khajeh, K.2
Moradian, F.3
Ranjbar, B.4
Naderi-Manesh, H.5
-
37
-
-
0028933531
-
Crystal structure of calcium depleted Bacillus licheni- formis alpha-amylase at 2.2A resolution
-
Machius, M.; Wiegand, G.; Huber, R. Crystal structure of calcium depleted Bacillus licheni- formis alpha-amylase at 2.2A resolution. Journal of Molecular Biology 1995, 246, 545-559.
-
(1995)
Journal of Molecular Biology
, vol.246
, pp. 545-559
-
-
MacHius, M.1
Wiegand, G.2
Huber, R.3
-
38
-
-
0025284694
-
Involvement of denaturation-like changes in Pseudomonas exotoxin a hydrophobicity and membrane penetration determined by characterization of pH and thermal transitions: Roles of two distinct conformationally altered states
-
Jiang, J.X.; Landon, E. Involvement of denaturation-like changes in Pseudomonas exotoxin A, hydrophobicity, and membrane penetration determined by characterization of pH and thermal transitions: Roles of two distinct conformationally altered states. Journal of Biological Chemistry 1990, 265, 8636-8641. (Pubitemid 120000824)
-
(1990)
Journal of Biological Chemistry
, vol.265
, Issue.15
, pp. 8636-8641
-
-
Jiang, J.X.1
London, E.2
-
39
-
-
73449104308
-
Thermal stability of amylase in aqueous cosolvent system
-
Yadav, J.K.; Prakash, V. Thermal stability of amylase in aqueous cosolvent system. Journal of Biosciences 2009, 43 (3).
-
(2009)
Journal of Biosciences
, vol.43
, Issue.3
-
-
Yadav, J.K.1
Prakash, V.2
-
40
-
-
0030725266
-
Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state
-
Kendrick, B.S.; Chang, B.S.; Arakawa, T.; Peterson, B.; Randolph, T.W.; Manning, M.C.; Carpenter, J.F. Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: Role in restricted conformational mobility and compaction of native state. Proceedings of National Academy of Sciences, USA 1997, 94, 1917-1922.
-
(1997)
Proceedings of National Academy of Sciences, USA
, vol.94
, pp. 1917-1922
-
-
Kendrick, B.S.1
Chang, B.S.2
Arakawa, T.3
Peterson, B.4
Randolph, T.W.5
Manning, M.C.6
Carpenter, J.F.7
-
41
-
-
0028862864
-
The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
-
Liu, Y.; Bolen, D.W. The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 1995, 34, 12884-12891.
-
(1995)
Biochemistry
, vol.34
, pp. 12884-12891
-
-
Liu, Y.1
Bolen, D.W.2
-
42
-
-
67651033247
-
Characterization of acid-induced molten globule like state of ficin
-
Devaraj, K.B.; Kumar, P.R.; Prakash, V. Characterization of acid-induced molten globule like state of ficin. International Journal of Biological Macromolecules 2009, 45 (3), 248-254.
-
(2009)
International Journal of Biological Macromolecules
, vol.45
, Issue.3
, pp. 248-254
-
-
Devaraj, K.B.1
Kumar, P.R.2
Prakash, V.3
-
43
-
-
52949105129
-
PH induced structural alterations in an aspartic protease from Vigna radiate indicating an alkali induced molten globule state
-
Kulkarni, A.; Gaikwad, S.; Rao, M. pH induced structural alterations in an aspartic protease from Vigna radiate indicating an alkali induced molten globule state. International Journal of Biological Macromolecules 2008, 43 (4), 375-376.
-
(2008)
International Journal of Biological Macromolecules
, vol.43
, Issue.4
, pp. 375-376
-
-
Kulkarni, A.1
Gaikwad, S.2
Rao, M.3
|