Application of multivariate curve resolution to the temperature-induced unfolding of α-chymotrypsin

[1]  Anna de Juan,et al.  Soft Modeling of Analytical Data , 2006 .

[2]  Romà Tauler,et al.  Local rank exploratory analysis of evolving rank-deficient systems , 2004 .

[3]  Romà Tauler,et al.  Chemometrics applied to unravel multicomponent processes and mixtures: Revisiting latest trends in multivariate resolution , 2003 .

[4]  Romà Tauler,et al.  Modeling temperature-dependent protein structural transitions by combined near-IR and mid-IR spectroscopies and multivariate curve resolution. , 2003, Analytical chemistry.

[5]  Romà Tauler,et al.  Detection and resolution of intermediate species in protein folding processes using fluorescence and circular dichroism spectroscopies and multivariate curve resolution. , 2002, Analytical chemistry.

[6]  Lee Whitmore,et al.  DICHROWEB: an interactive website for the analysis of protein secondary structure from circular dichroism spectra , 2002, Bioinform..

[7]  N. Sreerama,et al.  Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. , 2000, Analytical biochemistry.

[8]  W. C. Johnson,et al.  Analyzing protein circular dichroism spectra for accurate secondary structures , 1999, Proteins.

[9]  Dr. Bengt Nölting.  Protein Folding Kinetics , 1999, Springer Berlin Heidelberg.

[10]  R. Tauler,et al.  Multivariate curve resolution: a possible tool in the detection of intermediate structures in protein folding. , 1998, Biophysical journal.

[11]  Romà Tauler,et al.  Second-order multivariate curve resolution applied to rank-deficient data obtained from acid-base spectrophotometric titrations of mixtures of nucleic bases , 1997 .

[12]  J. Iborra,et al.  Dynamic structure/function relationships in the alpha-chymotrypsin deactivation process by heat and pH. , 1997, European journal of biochemistry.

[13]  Alison Rodger,et al.  Circular Dichroism and Linear Dichroism , 1997 .

[14]  D. Hamada,et al.  Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein , 1996, Nature Structural Biology.

[15]  N. Greenfield.  Methods to estimate the conformation of proteins and polypeptides from circular dichroism data. , 1996, Analytical biochemistry.

[16]  D. Massart,et al.  Orthogonal projection approach applied to peak purity assessment. , 1996, Analytical chemistry.

[17]  G. Fasman.  Circular Dichroism and the Conformational Analysis of Biomolecules , 1996, Springer US.

[18]  R. Tauler.  Multivariate curve resolution applied to second order data , 1995 .

[19]  R. Manne.  On the resolution problem in hyphenated chromatography , 1995 .

[20]  Dominique Bonvin,et al.  On the Rank Deficiency and Rank Augmentation of the Spectral Measurement Matrix , 1996 .

[21]  Age K. Smilde,et al.  Multicomponent Determination of Chlorinated Hydrocarbons Using a Reaction-Based Chemical Sensor. 3. Medium-Rank Second-Order Calibration with Restricted Tucker Models , 1994 .

[22]  N. Berova,et al.  Circular Dichroism: Principles and Applications , 1994 .

[23]  R. H. Pain,et al.  Mechanisms of protein folding , 1994 .

[24]  W. Windig,et al.  Interactive self-modeling mixture analysis , 1991 .

[25]  M. Maeder.  Evolving factor analysis for the resolution of overlapping chromatographic peaks , 1987 .

[26]  T. Creighton.  Proteins: Structures and Molecular Properties , 1986 .

[27]  M. Maeder,et al.  The resolution of overlapping chromatographic peaks by evolving factor analysis , 1986 .

[28]  G. Golub.  Matrix computations , 1983 .

[29]  Johnson Wc,et al.  Information content in the circular dichroism of proteins. , 1981 .

[30]  S. Provencher,et al.  Estimation of globular protein secondary structure from circular dichroism. , 1981, Biochemistry.

[31]  Georg E. Schulz,et al.  Principles of Protein Structure , 1979 .