Combined fitting parameters of heat denaturation curves of GFP-cycle3 and its mutants using a model involving two consecutive irreversible steps of denaturation (eq. 9, 10).

Chemical denaturation profiles of wild-type apoE3 and apoE3 variants.

Dimitra Georgiadou (340654)
Angeliki Chroni (340655)
Alexander Vezeridis (340657)
Vassilis I. Zannis (340659)
Efstratios Stratikos (340662)

February 2013

Each variant is presented in comparison with the wild-type protein (black circles). Solid lines r...

Baseline length and automated fitting of denaturation data

Allen, Devon L.
Pielak, Gary J.

January 1998

To understand relationships between protein sequence and stability, we often compare data from prote...

Simulations on the response of protein denaturation temperature to changes in environmental temperatures under conditions of threshold selection for kinetic stability.

M. Luisa Romero-Romero (347004)
Valeria A. Risso (205127)
Sergio Martinez-Rodriguez (2814223)
Eric A. Gaucher (358033)
Beatriz Ibarra-Molero (158272)
Jose M. Sanchez-Ruiz (118283)

June 2016

The simulations shown are identical to that displayed in <a href="http://www.plosone.org/article/...

GFP-cycle3 melting and choice of irreversible denaturation models.

Tatiana N. Melnik (298781)
Tatiana V. Povarnitsyna (298782)
Anatoly S. Glukhov (112969)
Bogdan S. Melnik (298784)

February 2013

Dependences of excess molar heat capacity versus temperature for GFP-cycle3 measured at three sca...

Thermal denaturation profiles of HPR and its variants.

Md. Tabish Rehman (355007)
Punyatirtha Dey (355008)
Md. Imtaiyaz Hassan (355009)
Faizan Ahmad (54871)
Janendra K. Batra (292666)

February 2013

Heat induced unfolding curves of HPR and its variants are shown as plots of fD ...

Thermal stability of WT and mutants of the c-Src-SH3 domain.

Julio Bacarizo (437897)
Sergio Martinez-Rodriguez (2814223)
Jose Manuel Martin-Garcia (671937)
Montserrat Andujar-Sanchez (671938)
Emilia Ortiz-Salmeron (671939)
Jose Luis Neira (5661655)
Ana Camara-Artigas (5661658)

December 2014

aErrors are fitting errors to the two-state denaturation model.Thermal stability of WT and...

Comparison of parameters of the one-step irreversible thermal denaturation of different proteins.

Megha Goyal (679966)
Tapan K. Chaudhuri (679967)
Kunihiro Kuwajima (416424)

December 2014

*For these proteins, T* values were not reported, but instead, the Tmax,...

The GdmCl chemical-denaturation parameters for the three PsTRXs at pH 7.0 and 25°Ca.

David Aguado-Llera (355692)
Ana Isabel Martínez-Gómez (355694)
Jesús Prieto (22724)
Marco Marenchino (355697)
José Angel Traverso (355699)
Javier Gómez (206268)
Ana Chueca (355702)
José L. Neira (355704)

February 2013

aThe errors are fitting errors to the two-state model. The chemical-denaturations were only fully...

Denaturation temperatures of chimeric proteins.

Kazufumi Takano (154761)
Tomohiro Okamoto (357392)
Jun Okada (23397)
Shun-ichi Tanaka (357393)
Clement Angkawidjaja (154759)
Yuichi Koga (154760)
Shigenori Kanaya (154762)

February 2013

aErrors are ±0.3°C.bData from <a href="http://www.plosone.org/article/info:doi/10.1371/jou...

Thermal denaturation curves of the wild type and mutant ADs.

Yuuki Hayashi (67499)
Fumitaka Yasugi (716954)
Munehito Arai (716955)

April 2015

The denaturation curves were monitored by the CD ellipticity at 222 nm (<a href="http://www.ploso...

Melting Temperature (Tm) extrapolated by the thermal denaturation profiles of human NGF and proNGF Wild Type and mutants.

Francesca Malerba (161148)
Francesca Paoletti (161149)
Bruno Bruni Ercole (795980)
Serena Materazzi (144070)
Romina Nassini (144009)
Elisabetta Coppi (677153)
Riccardo Patacchini (144063)
Simona Capsoni (161132)
Doriano Lamba (179482)
Antonino Cattaneo (161159)

September 2015

The values are averages of the different experiments. The errors represent standard deviations.</...

Thermal denaturation of AGT variants studied by differential scanning calorimetry (DSC).

Noel Mesa-Torres (450797)
Israel Fabelo-Rosa (450798)
Debora Riverol (450799)
Cristina Yunta (450800)
Armando Albert (450801)
Eduardo Salido (179852)
Angel L. Pey (355133)

August 2013

A) Representative DSC traces obtained at 3°C/min; Lines are best-fits from a two-state irreversib...

Thermodynamic parameters for denaturation of wild-type, C58/145A and ΔC6 Sto-RNase HI.

Kazufumi Takano (154761)
Tomohiro Okamoto (357392)
Jun Okada (23397)
Shun-ichi Tanaka (357393)
Clement Angkawidjaja (154759)
Yuichi Koga (154760)
Shigenori Kanaya (154762)

February 2013

aData from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0016226#pone.001...

Transition temperatures of HPR and variants.

Md. Tabish Rehman (355007)
Punyatirtha Dey (355008)
Md. Imtaiyaz Hassan (355009)
Faizan Ahmad (54871)
Janendra K. Batra (292666)

February 2013

The transition temperatures were derived from the thermal denaturation curves of HPR and its vari...

Model used to derive equation 3 and describe the experimental thermal inactivation profiles for wild-type phytase and variants (Figures 7A and B).

Inmaculada Sanchez-Romero (439639)
Antonio Ariza (8356)
Keith S. Wilson (416959)
Michael Skjøt (439640)
Jesper Vind (416953)
Leonardo De Maria (416956)
Lars K. Skov (416958)
Jose M. Sanchez-Ruiz (118283)

July 2013

(A) An intermediate state (or ensemble) is assumed to be critical for the irreversible denaturati...

Chemical denaturation profiles of wild-type apoE3 and apoE3 variants.

Dimitra Georgiadou (340654)
Angeliki Chroni (340655)
Alexander Vezeridis (340657)
Vassilis I. Zannis (340659)
Efstratios Stratikos (340662)

February 2013

Each variant is presented in comparison with the wild-type protein (black circles). Solid lines r...

Baseline length and automated fitting of denaturation data

Allen, Devon L.
Pielak, Gary J.

January 1998

To understand relationships between protein sequence and stability, we often compare data from prote...

Simulations on the response of protein denaturation temperature to changes in environmental temperatures under conditions of threshold selection for kinetic stability.

M. Luisa Romero-Romero (347004)
Valeria A. Risso (205127)
Sergio Martinez-Rodriguez (2814223)
Eric A. Gaucher (358033)
Beatriz Ibarra-Molero (158272)
Jose M. Sanchez-Ruiz (118283)

June 2016

The simulations shown are identical to that displayed in <a href="http://www.plosone.org/article/...

GFP-cycle3 melting and choice of irreversible denaturation models.

Tatiana N. Melnik (298781)
Tatiana V. Povarnitsyna (298782)
Anatoly S. Glukhov (112969)
Bogdan S. Melnik (298784)

February 2013

Dependences of excess molar heat capacity versus temperature for GFP-cycle3 measured at three sca...

Thermal denaturation profiles of HPR and its variants.

Md. Tabish Rehman (355007)
Punyatirtha Dey (355008)
Md. Imtaiyaz Hassan (355009)
Faizan Ahmad (54871)
Janendra K. Batra (292666)

February 2013

Heat induced unfolding curves of HPR and its variants are shown as plots of fD ...

Thermal stability of WT and mutants of the c-Src-SH3 domain.

Julio Bacarizo (437897)
Sergio Martinez-Rodriguez (2814223)
Jose Manuel Martin-Garcia (671937)
Montserrat Andujar-Sanchez (671938)
Emilia Ortiz-Salmeron (671939)
Jose Luis Neira (5661655)
Ana Camara-Artigas (5661658)

December 2014

aErrors are fitting errors to the two-state denaturation model.Thermal stability of WT and...

Comparison of parameters of the one-step irreversible thermal denaturation of different proteins.

Megha Goyal (679966)
Tapan K. Chaudhuri (679967)
Kunihiro Kuwajima (416424)

December 2014

*For these proteins, T* values were not reported, but instead, the Tmax,...

The GdmCl chemical-denaturation parameters for the three PsTRXs at pH 7.0 and 25°Ca.

David Aguado-Llera (355692)
Ana Isabel Martínez-Gómez (355694)
Jesús Prieto (22724)
Marco Marenchino (355697)
José Angel Traverso (355699)
Javier Gómez (206268)
Ana Chueca (355702)
José L. Neira (355704)

February 2013

aThe errors are fitting errors to the two-state model. The chemical-denaturations were only fully...

Denaturation temperatures of chimeric proteins.

Kazufumi Takano (154761)
Tomohiro Okamoto (357392)
Jun Okada (23397)
Shun-ichi Tanaka (357393)
Clement Angkawidjaja (154759)
Yuichi Koga (154760)
Shigenori Kanaya (154762)

February 2013

aErrors are ±0.3°C.bData from <a href="http://www.plosone.org/article/info:doi/10.1371/jou...

Thermal denaturation curves of the wild type and mutant ADs.

Yuuki Hayashi (67499)
Fumitaka Yasugi (716954)
Munehito Arai (716955)

April 2015

The denaturation curves were monitored by the CD ellipticity at 222 nm (<a href="http://www.ploso...

Melting Temperature (Tm) extrapolated by the thermal denaturation profiles of human NGF and proNGF Wild Type and mutants.

Francesca Malerba (161148)
Francesca Paoletti (161149)
Bruno Bruni Ercole (795980)
Serena Materazzi (144070)
Romina Nassini (144009)
Elisabetta Coppi (677153)
Riccardo Patacchini (144063)
Simona Capsoni (161132)
Doriano Lamba (179482)
Antonino Cattaneo (161159)

September 2015

The values are averages of the different experiments. The errors represent standard deviations.</...

Thermal denaturation of AGT variants studied by differential scanning calorimetry (DSC).

Noel Mesa-Torres (450797)
Israel Fabelo-Rosa (450798)
Debora Riverol (450799)
Cristina Yunta (450800)
Armando Albert (450801)
Eduardo Salido (179852)
Angel L. Pey (355133)

August 2013

A) Representative DSC traces obtained at 3°C/min; Lines are best-fits from a two-state irreversib...

Thermodynamic parameters for denaturation of wild-type, C58/145A and ΔC6 Sto-RNase HI.

Kazufumi Takano (154761)
Tomohiro Okamoto (357392)
Jun Okada (23397)
Shun-ichi Tanaka (357393)
Clement Angkawidjaja (154759)
Yuichi Koga (154760)
Shigenori Kanaya (154762)

February 2013

aData from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0016226#pone.001...

Transition temperatures of HPR and variants.

Md. Tabish Rehman (355007)
Punyatirtha Dey (355008)
Md. Imtaiyaz Hassan (355009)
Faizan Ahmad (54871)
Janendra K. Batra (292666)

February 2013

The transition temperatures were derived from the thermal denaturation curves of HPR and its vari...

Model used to derive equation 3 and describe the experimental thermal inactivation profiles for wild-type phytase and variants (Figures 7A and B).

Inmaculada Sanchez-Romero (439639)
Antonio Ariza (8356)
Keith S. Wilson (416959)
Michael Skjøt (439640)
Jesper Vind (416953)
Leonardo De Maria (416956)
Lars K. Skov (416958)
Jose M. Sanchez-Ruiz (118283)

July 2013

(A) An intermediate state (or ensemble) is assumed to be critical for the irreversible denaturati...

Chemical denaturation profiles of wild-type apoE3 and apoE3 variants.

Dimitra Georgiadou (340654)
Angeliki Chroni (340655)
Alexander Vezeridis (340657)
Vassilis I. Zannis (340659)
Efstratios Stratikos (340662)

February 2013

Each variant is presented in comparison with the wild-type protein (black circles). Solid lines r...

Baseline length and automated fitting of denaturation data

Allen, Devon L.
Pielak, Gary J.

January 1998

To understand relationships between protein sequence and stability, we often compare data from prote...

Simulations on the response of protein denaturation temperature to changes in environmental temperatures under conditions of threshold selection for kinetic stability.

M. Luisa Romero-Romero (347004)
Valeria A. Risso (205127)
Sergio Martinez-Rodriguez (2814223)
Eric A. Gaucher (358033)
Beatriz Ibarra-Molero (158272)
Jose M. Sanchez-Ruiz (118283)

June 2016

The simulations shown are identical to that displayed in <a href="http://www.plosone.org/article/...

Combined fitting parameters of heat denaturation curves of GFP<i>-</i>cycle3 and its mutants using a model involving two consecutive irreversible steps of denaturation (eq. 9, 10).

Abstract

Extracted data

Combined fitting parameters of heat denaturation curves of GFP<i>-</i>cycle3 and its mutants using a model involving two consecutive irreversible steps of denaturation (eq. 9, 10).

Abstract

Extracted data

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