Literature DB >> 10422839

Heat capacity change for ribonuclease A folding.

C N Pace1, G R Grimsley, S T Thomas, G I Makhatadze.   

Abstract

The change in heat capacity deltaCp for the folding of ribonuclease A was determined using differential scanning calorimetry and thermal denaturation curves. The methods gave equivalent results, deltaCp = 1.15+/-0.08 kcal mol(-1) K(-1). Estimates of the conformational stability of ribonuclease A based on these results from thermal unfolding are in good agreement with estimates from urea unfolding analyzed using the linear extrapolation method.

Entities:  

Mesh:

Substances:

Year:  1999        PMID: 10422839      PMCID: PMC2144378          DOI: 10.1110/ps.8.7.1500

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  40 in total

1.  Thermodynamic investigations of proteins. I. Standard functions for proteins with lysozyme as an example.

Authors:  W Pfeil; P L Privalov
Journal:  Biophys Chem       Date:  1976-01       Impact factor: 2.352

Review 2.  Measuring and increasing protein stability.

Authors:  C N Pace
Journal:  Trends Biotechnol       Date:  1990-04       Impact factor: 19.536

3.  Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin.

Authors:  R F Greene; C N Pace
Journal:  J Biol Chem       Date:  1974-09-10       Impact factor: 5.157

4.  Calorimetric investigation of ribonuclease thermal denaturation.

Authors:  P L Privalov; E I Tiktopulo; N N Khechinashvili
Journal:  Int J Pept Protein Res       Date:  1973

5.  Thermodynamics of protein denaturation. A calorimetric study of the reversible denaturation of chymotrypsinogen and conclusions regarding the accuracy of the two-state approximation.

Authors:  W M Jackson; J F Brandts
Journal:  Biochemistry       Date:  1970-05-26       Impact factor: 3.162

6.  Thermodynamics of the denaturation of ribonuclease by guanidine hydrochloride.

Authors:  A Salahuddin; C Tanford
Journal:  Biochemistry       Date:  1970-03-17       Impact factor: 3.162

7.  Thermodynamics of the unfolding of beta-lactoglobulin A in aqueous urea solutions between 5 and 55 degrees.

Authors:  N C Pace; C Tanford
Journal:  Biochemistry       Date:  1968-01       Impact factor: 3.162

8.  Studies of the chymotrypsinogen family of proteins. XI. Heat-capacity changes accompanying reversible thermal unfolding of proteins.

Authors:  D F Shiao; R Lumry; J Fahey
Journal:  J Am Chem Soc       Date:  1971-04-21       Impact factor: 15.419

9.  Reversible pressure--temperature denaturation of chymotrypsinogen.

Authors:  S A Hawley
Journal:  Biochemistry       Date:  1971-06-22       Impact factor: 3.162

10.  The thermodynamics of protein denaturation. 3. The denaturation of ribonuclease in water and in aqueous urea and aqueous ethanol mixtures.

Authors:  J F Brandts; L Hunt
Journal:  J Am Chem Soc       Date:  1967-09-13       Impact factor: 15.419

View more
  17 in total

1.  Pressure versus temperature unfolding of ribonuclease A: an FTIR spectroscopic characterization of 10 variants at the carboxy-terminal site.

Authors:  J Torrent; P Rubens; M Ribó; K Heremans; M Vilanova
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

2.  Contribution of proton linkage to the thermodynamic stability of the major cold-shock protein of Escherichia coli CspA.

Authors:  S A Petrosian; G I Makhatadze
Journal:  Protein Sci       Date:  2000-02       Impact factor: 6.725

3.  Heat capacity changes upon burial of polar and nonpolar groups in proteins.

Authors:  V V Loladze; D N Ermolenko; G I Makhatadze
Journal:  Protein Sci       Date:  2001-07       Impact factor: 6.725

4.  pH dependence thermal stability of a chymotrypsin inhibitor from Schizolobium parahyba seeds.

Authors:  Rozeni C L Teles; Leonardo de A Calderon; Francisco J Medrano; João A R G Barbosa; Beatriz G Guimarães; Marcelo M Santoro; Sonia M de Freitas
Journal:  Biophys J       Date:  2005-03-11       Impact factor: 4.033

5.  Cold instability of aponeocarzinostatin and its stabilization by labile chromophore.

Authors:  Kandaswamy Jayachithra; Thallampuranam Krishnaswamy Suresh Kumar; Ta-Jung Lu; Chin Yu; Der-Hang Chin
Journal:  Biophys J       Date:  2005-04-08       Impact factor: 4.033

6.  Human 60-kDa lysophospholipase contains an N-terminal L-asparaginase domain that is allosterically regulated by L-asparagine.

Authors:  Christos S Karamitros; Manfred Konrad
Journal:  J Biol Chem       Date:  2014-03-22       Impact factor: 5.157

7.  Refinement of noncalorimetric determination of the change in heat capacity, DeltaC(p), of protein unfolding and validation across a wide temperature range.

Authors:  Deepika Talla-Singh; Wesley E Stites
Journal:  Proteins       Date:  2008-06

8.  Nonlinear least-squares data fitting in Excel spreadsheets.

Authors:  Gerdi Kemmer; Sandro Keller
Journal:  Nat Protoc       Date:  2010-01-28       Impact factor: 13.491

9.  Thermodynamic Analysis of Point Mutations Inhibiting High-Temperature Reversible Oligomerization of PDZ3.

Authors:  Tomonori Saotome; Taichi Mezaki; Subbaian Brindha; Satoru Unzai; Jose C Martinez; Shun-Ichi Kidokoro; Yutaka Kuroda
Journal:  Biophys J       Date:  2020-08-28       Impact factor: 4.033

10.  Replacing a single atom accelerates the folding of a protein and increases its thermostability.

Authors:  Ulrich Arnold; Ronald T Raines
Journal:  Org Biomol Chem       Date:  2016-07-12       Impact factor: 3.876

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.