-
1
-
-
0002006297
-
Are there pathways for protein folding?
-
Levinthal, C. Are there pathways for protein folding? J. Chim. Phys 65 44-45 (1968).
-
(1968)
J. Chim. Phys
, vol.65
, pp. 44-45
-
-
Levinthal, C.1
-
2
-
-
0030272670
-
Time-resolved biophysical methods in the study of protein folding
-
Plaxco, K.W. & Dobson, C.M. Time-resolved biophysical methods in the study of protein folding. Curr. Opin. Struct. Biol. 6, 630-636 (1996).
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 630-636
-
-
Plaxco, K.W.1
Dobson, C.M.2
-
3
-
-
0001474715
-
Real-time NMR studies of protein folding
-
Van Nuland, N.A.J., Forge, V. Balbach, J. & Dobson, C.M. Real-time NMR studies of protein folding. Acc. Chem. Res. 31, 773-778 (1998).
-
(1998)
Acc. Chem. Res.
, vol.31
, pp. 773-778
-
-
Van Nuland, N.A.J.1
Forge, V.2
Balbach, J.3
Dobson, C.M.4
-
4
-
-
0026653655
-
Protein folding studied using hydrogen-exchange labeling and two dimensional NMR
-
Englander, S.W. & Mayne, L. Protein folding studied using hydrogen-exchange labeling and two dimensional NMR. Annu. Rev. Biophys. Biomol. Struct. 21, 243-265 (1992).
-
(1992)
Annu. Rev. Biophys. Biomol. Struct.
, vol.21
, pp. 243-265
-
-
Englander, S.W.1
Mayne, L.2
-
5
-
-
0028917296
-
Structures of folding intermediates
-
Ptitsyn, O.B. Structures of folding intermediates. Curr. Opin. Struct. Biol. 5, 74-78 (1995).
-
(1995)
Curr. Opin. Struct. Biol.
, vol.5
, pp. 74-78
-
-
Ptitsyn, O.B.1
-
6
-
-
0029961647
-
Structural analysis of non-native states of proteins by NMR
-
Shortle, D.R. Structural analysis of non-native states of proteins by NMR. Curr. Opin. Struct. Biol. 6, 24-30 (1996).
-
(1996)
Curr. Opin. Struct. Biol.
, vol.6
, pp. 24-30
-
-
Shortle, D.R.1
-
7
-
-
0031851978
-
Equilibrium NMR studies of unfolded and partially folded proteins
-
Dyson, H.J. & Wright, P.E. Equilibrium NMR studies of unfolded and partially folded proteins. Nature Struct. Biol. 5(Suppl), 499-503 (1998).
-
(1998)
Nature Struct. Biol.
, vol.5
, Issue.SUPPL.
, pp. 499-503
-
-
Dyson, H.J.1
Wright, P.E.2
-
8
-
-
1842298212
-
From Levinthal to pathways to funnels
-
Dill, K.A. & Chan, H.S. From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19 (1997).
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 10-19
-
-
Dill, K.A.1
Chan, H.S.2
-
9
-
-
0344301982
-
Protein folding: A perspective from theory and experiment
-
Dobson, C.M., Sali, A. & Karplus, M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. 37, 868-893 (1998).
-
(1998)
Angew. Chem. Int. Ed.
, vol.37
, pp. 868-893
-
-
Dobson, C.M.1
Sali, A.2
Karplus, M.3
-
10
-
-
0028978422
-
Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
-
Shiraki, K., Nishikawa, K. & Goto, Y. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194 (1995).
-
(1995)
J. Mol. Biol.
, vol.245
, pp. 180-194
-
-
Shiraki, K.1
Nishikawa, K.2
Goto, Y.3
-
11
-
-
0030593499
-
Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat
-
Schonbrunner, N., Wey, J., Engels, J., Georg, H. & Kiefhaber, T. Native-like β-structure in a trifluoroethanol-induced partially folded state of the all-β-sheet protein tendamistat. J. Mol. Biol. 260, 432-445 (1996).
-
(1996)
J. Mol. Biol.
, vol.260
, pp. 432-445
-
-
Schonbrunner, N.1
Wey, J.2
Engels, J.3
Georg, H.4
Kiefhaber, T.5
-
12
-
-
0032568860
-
Exploring the folding pathways of annexin I, a multidomain protein. I. Non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I
-
Cordier-Ochsenbein, F. et al. Exploring the folding pathways of annexin I, a multidomain protein. I. Non-native structures stabilize the partially folded state of the isolated domain 2 of annexin I. J. Mol. Biol. 279, 1163-1175 (1998).
-
(1998)
J. Mol. Biol.
, vol.279
, pp. 1163-1175
-
-
Cordier-Ochsenbein, F.1
-
13
-
-
0028964333
-
Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures
-
Guijarro, J.I., Jackson, M., Chaffotte, A.F., Delepierre, M., Mantsch, H.H. & Goldberg, M.E. Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures. Biochemistry 34, 2998-3008 (1995).
-
(1995)
Biochemistry
, vol.34
, pp. 2998-3008
-
-
Guijarro, J.I.1
Jackson, M.2
Chaffotte, A.F.3
Delepierre, M.4
Mantsch, H.H.5
Goldberg, M.E.6
-
14
-
-
0029740071
-
Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
-
Hamada, D., Segawa, S. & Goto, Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct. Biol. 3, 868-873 (1996).
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 868-873
-
-
Hamada, D.1
Segawa, S.2
Goto, Y.3
-
15
-
-
0032498226
-
Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
-
Arai, M., Ikura, T., Semisotnov, G.V., Kihara, H., Amemiya, Y. & Kuwajima, K. Kinetic Refolding of β-Lactoglobulin. Studies by Synchrotron X-ray Scattering, and Circular Dichroism, Absorption and Fluorescence Spectroscopy. J. Mol. Biol. 275, 149-62 (1998).
-
(1998)
J. Mol. Biol.
, vol.275
, pp. 149-162
-
-
Arai, M.1
Ikura, T.2
Semisotnov, G.V.3
Kihara, H.4
Amemiya, Y.5
Kuwajima, K.6
-
16
-
-
0027492164
-
Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
-
Surewicz, W.E., Mantsch, H.H. & Chapman, D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment Biochemistry 32, 389-394 (1993)
-
(1993)
Biochemistry
, vol.32
, pp. 389-394
-
-
Surewicz, W.E.1
Mantsch, H.H.2
Chapman, D.3
-
17
-
-
0028949797
-
Temperature-jump-induced refolding of ribonuclease A: A time-resolved FTIR spectroscopic study
-
Backmann, J., Fabian, H. & Naumann, D. Temperature-jump-induced refolding of ribonuclease A: a time-resolved FTIR spectroscopic study. FEBS. Lett. 364, 175-178 (1995).
-
(1995)
FEBS. Lett.
, vol.364
, pp. 175-178
-
-
Backmann, J.1
Fabian, H.2
Naumann, D.3
-
18
-
-
0029769926
-
A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca(2+)-ATPase: Kinetics of the high-affinity calcium binding at low temperature
-
Troullier, A., Gerwert, K., & Dupont, Y. A time-resolved Fourier transformed infrared difference spectroscopy study of the sarcoplasmic reticulum Ca(2+)-ATPase: kinetics of the high-affinity calcium binding at low temperature. Biophys. J. 71, 2970-2983 (1996).
-
(1996)
Biophys. J.
, vol.71
, pp. 2970-2983
-
-
Troullier, A.1
Gerwert, K.2
Dupont, Y.3
-
19
-
-
0032536156
-
Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy
-
Panick, G., Malessa, R., Winter, R., Rapp, G., Frye, K.J. & Royer, C.A. Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy. J. Mol. Biol. 275, 389-402 (1998).
-
(1998)
J. Mol. Biol.
, vol.275
, pp. 389-402
-
-
Panick, G.1
Malessa, R.2
Winter, R.3
Rapp, G.4
Frye, K.J.5
Royer, C.A.6
-
20
-
-
0142037152
-
New structural insights into the refolding of ribonuclease T, as seen by time-resolved Fourier-transform infrared spectroscopy
-
Reinstadler, D., Fabian, H. & Naumann, D. New structural insights into the refolding of ribonuclease T, as seen by time-resolved Fourier-transform infrared spectroscopy. Proteins 34, 303-316 (1999).
-
(1999)
Proteins
, vol.34
, pp. 303-316
-
-
Reinstadler, D.1
Fabian, H.2
Naumann, D.3
-
21
-
-
0027515417
-
Molecular reaction mechanisms of proteins as monitored by time-resolved FTIR spectroscopy
-
Gerwert, K. Molecular reaction mechanisms of proteins as monitored by time-resolved FTIR spectroscopy. Curr. Opin. Struct. Biol. 3, 769-773 (1993).
-
(1993)
Curr. Opin. Struct. Biol.
, vol.3
, pp. 769-773
-
-
Gerwert, K.1
-
22
-
-
0028925395
-
A stopped-flow apparatus for infrared spectroscopy of aqueous solutions
-
White, A.J., Drabble, K. & Wharton, C.W. A stopped-flow apparatus for infrared spectroscopy of aqueous solutions. Biochem. J. 306, 843-849 (1995).
-
(1995)
Biochem. J.
, vol.306
, pp. 843-849
-
-
White, A.J.1
Drabble, K.2
Wharton, C.W.3
-
23
-
-
0029731419
-
Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy
-
Reinstadler, D., Fabian, H., Backmann, J. & Naumann, D. Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. Biochemistry 35, 15822-15830 (1996).
-
(1996)
Biochemistry
, vol.35
, pp. 15822-15830
-
-
Reinstadler, D.1
Fabian, H.2
Backmann, J.3
Naumann, D.4
-
24
-
-
0027536094
-
Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study
-
Alexandrescu, A.T., Evans, P.A., Pitkeathly, M., Baum, J. & Dobson, C.M. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: a two-dimensional NMR study. Biochemistry 32, 1707-1718 (1993).
-
(1993)
Biochemistry
, vol.32
, pp. 1707-1718
-
-
Alexandrescu, A.T.1
Evans, P.A.2
Pitkeathly, M.3
Baum, J.4
Dobson, C.M.5
-
25
-
-
0028866620
-
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin
-
Schulman, B.A., Redfield, C., Peng, Z.Y., Dobson, C.M. & Kim, P.S. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin. J. Mol. Biol. 253, 651-657 (1995)
-
(1995)
J. Mol. Biol.
, vol.253
, pp. 651-657
-
-
Schulman, B.A.1
Redfield, C.2
Peng, Z.Y.3
Dobson, C.M.4
Kim, P.S.5
-
26
-
-
0030059690
-
The molten globule state of α-lactalbumin
-
Kuwajima, K. The molten globule state of α-lactalbumin. FASEB J. 10, 102-109 (1996).
-
(1996)
FASEB J.
, vol.10
, pp. 102-109
-
-
Kuwajima, K.1
-
27
-
-
0031050429
-
Structural characterization of the molten globule α-lactalbumin by solution X-ray scattering
-
Kataoka, M., Kuwajima, K., Tokunaga, F. & Goto, Y. Structural characterization of the molten globule α-lactalbumin by solution X-ray scattering. Protein Sci. 6, 422-430 (1997).
-
(1997)
Protein Sci.
, vol.6
, pp. 422-430
-
-
Kataoka, M.1
Kuwajima, K.2
Tokunaga, F.3
Goto, Y.4
-
28
-
-
0030768045
-
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
-
Schulman, B.A., Kim, P.S., Dobson, C.M. & Redfield, C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Struct. Biol. 4, 630-634 (1997).
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 630-634
-
-
Schulman, B.A.1
Kim, P.S.2
Dobson, C.M.3
Redfield, C.4
-
29
-
-
0030737873
-
Detection of residue contacts in a protein folding intermediate
-
Balbach, J., Forge, V., Lau, W.S., Jones, J.A., van Nuland, N.A.J. & Dobson, C.M. Detection of residue contacts in a protein folding intermediate. Proc. Natl. Acad. Sci. USA 94, 7182-7185 (1997).
-
(1997)
Proc. Natl. Acad. Sci. USA
, vol.94
, pp. 7182-7185
-
-
Balbach, J.1
Forge, V.2
Lau, W.S.3
Jones, J.A.4
Van Nuland, N.A.J.5
Dobson, C.M.6
-
30
-
-
0028952169
-
Bipartite structure of the α-lactalbumin molten globule
-
Wu, L.C., Peng, Z.Y. & Kim, P.S. Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2, 281-286 (1995).
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 281-286
-
-
Wu, L.C.1
Peng, Z.Y.2
Kim, P.S.3
-
31
-
-
0031008577
-
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR
-
Chung, E.W. et al. Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR. Protein Sci. 6, 1316-1324 (1997).
-
(1997)
Protein Sci.
, vol.6
, pp. 1316-1324
-
-
Chung, E.W.1
-
32
-
-
0030025082
-
Disulfide determinants of calcium-induced packing in α-lactalbumin
-
Wu, L.C., Schulman, B.A., Peng, Z.Y. & Kim, P.S. Disulfide determinants of calcium-induced packing in α-lactalbumin. Biochemistry 35, 859-863 (1996).
-
(1996)
Biochemistry
, vol.35
, pp. 859-863
-
-
Wu, L.C.1
Schulman, B.A.2
Peng, Z.Y.3
Kim, P.S.4
-
34
-
-
0033004311
-
Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin
-
Forge, V. et al. Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin. J. Mol. Biol. 288, 673-688 (1999).
-
(1999)
J. Mol. Biol.
, vol.288
, pp. 673-688
-
-
Forge, V.1
-
35
-
-
0030348041
-
Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
-
Arai, M. & Kuwajima, K. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. Des. 1, 275-87 (1996).
-
(1996)
Fold. Des.
, vol.1
, pp. 275-287
-
-
Arai, M.1
Kuwajima, K.2
-
36
-
-
0029123975
-
Following protein folding in real time using NMR spectroscopy
-
Balbach, J., Forge, V., van Nuland, N.A.J., Winder, S.L., Hore, P.J. & Dobson, C.M. Following protein folding in real time using NMR spectroscopy. Nature Struct. Biol. 2, 865-870 (1995).
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 865-870
-
-
Balbach, J.1
Forge, V.2
Van Nuland, N.A.J.3
Winder, S.L.4
Hore, P.J.5
Dobson, C.M.6
-
37
-
-
0029860435
-
Protein folding monitored at individual residues during a two-dimensional NMR experiment
-
Balbach, J., Forge, V., Lau, W.S., van Nuland, N.A.J., Brew, K. & Dobson, C.M. Protein folding monitored at individual residues during a two-dimensional NMR experiment. Science 274, 1161-1163 (1996).
-
(1996)
Science
, vol.274
, pp. 1161-1163
-
-
Balbach, J.1
Forge, V.2
Lau, W.S.3
Van Nuland, N.A.J.4
Brew, K.5
Dobson, C.M.6
-
38
-
-
0030585408
-
Crystal structures of guinea-pig, goat and bovine α-lactatbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase
-
Pike, A.C., Brew, K. & Acharya, K.R. Crystal structures of guinea-pig, goat and bovine α-lactatbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure 4, 691-703 (1996).
-
(1996)
Structure
, vol.4
, pp. 691-703
-
-
Pike, A.C.1
Brew, K.2
Acharya, K.R.3
-
39
-
-
0000337013
-
Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
-
Kauppinen, J.K., Moffatt, D.J., Manisch, H.H., & Cameron, D.G. Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Applied Spectroscopy 35, 271-276 (1981).
-
(1981)
Applied Spectroscopy
, vol.35
, pp. 271-276
-
-
Kauppinen, J.K.1
Moffatt, D.J.2
Manisch, H.H.3
Cameron, D.G.4
-
40
-
-
0019571021
-
Noise in Fourier self-deconvolution
-
Kauppinen, J.K., Moffatt, D.J., Cameron, D.G. & Mantsch, H.H. Noise in Fourier self-deconvolution. Applied Optics 20, 1866-1879 (1981).
-
(1981)
Applied Optics
, vol.20
, pp. 1866-1879
-
-
Kauppinen, J.K.1
Moffatt, D.J.2
Cameron, D.G.3
Mantsch, H.H.4
-
41
-
-
0023348944
-
A generalized approach to derivative spectroscopy
-
Cameron, D.G. & Moffatt, D.J. A generalized approach to derivative spectroscopy. Applied Spectroscopy 41, 539-544 (1987).
-
(1987)
Applied Spectroscopy
, vol.41
, pp. 539-544
-
-
Cameron, D.G.1
Moffatt, D.J.2
-
42
-
-
0025883964
-
Effect of metal ion binding on the secondary structure of bovine α-lactalbumin as examined by infrared spectroscopy
-
Prestrelski, S.J., Byler, D.M. & Thompson, M.P. Effect of metal ion binding on the secondary structure of bovine α-lactalbumin as examined by infrared spectroscopy. Biochemistry 30, 8797-8804 (1991).
-
(1991)
Biochemistry
, vol.30
, pp. 8797-8804
-
-
Prestrelski, S.J.1
Byler, D.M.2
Thompson, M.P.3
-
45
-
-
0023693897
-
Structural and conformational changes of beta-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature
-
Casal, H.L., Kohler, U. & Mantsch, H.H. Structural and conformational changes of beta-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 957, 11-20 (1988).
-
(1988)
Biochim. Biophys. Acta
, vol.957
, pp. 11-20
-
-
Casal, H.L.1
Kohler, U.2
Mantsch, H.H.3
-
46
-
-
0003589802
-
Fourier transform infrared spectroscopy
-
(ed Rousseau, D.L.) Academic Press Inc. New York
-
Alben, J.O. & Fiamingo, F.G. Fourier transform infrared spectroscopy. In Optical techniques in biological research (ed Rousseau, D.L.) 133-179 (Academic Press Inc. New York; 1984).
-
(1984)
Optical Techniques in Biological Research
, pp. 133-179
-
-
Alben, J.O.1
Fiamingo, F.G.2
-
47
-
-
0031043161
-
Nucleation mechanisms in protein folding
-
Fersht, A.R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7, 3-9 (1997).
-
(1997)
Curr. Opin. Struct. Biol.
, vol.7
, pp. 3-9
-
-
Fersht, A.R.1
-
48
-
-
0033580657
-
Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants
-
Canet, D. et al. Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants. Biochemistry 38, 6419-6427 (1999).
-
(1999)
Biochemistry
, vol.38
, pp. 6419-6427
-
-
Canet, D.1
-
49
-
-
0026244229
-
Molscript: A program to produce both detailed and schematic plots of protein structures
-
Kraulis, P.J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
-
(1991)
J. Appl. Crystallogr.
, vol.24
, pp. 946-950
-
-
Kraulis, P.J.1
-
50
-
-
0028709475
-
Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy
-
Goormaghtigh, E., Cabiaux, V. & Ruysschaert, J.M. Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. Subcellular Biochemistry 23, 405-450 (1994).
-
(1994)
Subcellular Biochemistry
, vol.23
, pp. 405-450
-
-
Goormaghtigh, E.1
Cabiaux, V.2
Ruysschaert, J.M.3
-
52
-
-
0016797947
-
Estimation of amino-acid residue side-chain absorption in the infrared spectra of protein solution in heavy water
-
Chirgadze, Y.N., Fedorov, O.V. & Trushina, N.P. Estimation of amino-acid residue side-chain absorption in the infrared spectra of protein solution in heavy water. Biopolymers 14, 679-694 (1975).
-
(1975)
Biopolymers
, vol.14
, pp. 679-694
-
-
Chirgadze, Y.N.1
Fedorov, O.V.2
Trushina, N.P.3
-
53
-
-
0000311509
-
Turns in small cyclic peptides -can infrared spectroscopy detect and discriminate amongst them?
-
Shaw, R.A., Perczel, A., Mantsch, H.H. & Fasman, G.D. Turns in small cyclic peptides -can infrared spectroscopy detect and discriminate amongst them? J. Mol. Struct. 324, 143-150 (1994).
-
(1994)
J. Mol. Struct.
, vol.324
, pp. 143-150
-
-
Shaw, R.A.1
Perczel, A.2
Mantsch, H.H.3
Fasman, G.D.4
-
54
-
-
0024283054
-
The solution structure of concanavalin A probed by FT-IR spectroscopy
-
Arrondo, J.L.R., Young, N.M. & Mantsch, H.H. The solution structure of concanavalin A probed by FT-IR spectroscopy. Biochim. Biophys. Acta 952, 261-268 (1988).
-
(1988)
Biochim. Biophys. Acta
, vol.952
, pp. 261-268
-
-
Arrondo, J.L.R.1
Young, N.M.2
Mantsch, H.H.3
-
55
-
-
0026642332
-
Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy
-
Smail, A.A., Mantsch, H.H. & Wong, P.T. Aggregation of chymotrypsinogen: portrait by infrared spectroscopy. Biochim. Biophys. Acta 1121, 183-188 (1992).
-
(1992)
Biochim. Biophys. Acta
, vol.1121
, pp. 183-188
-
-
Smail, A.A.1
Mantsch, H.H.2
Wong, P.T.3
|