Find

Interdisciplinary Nanoscience Center

Daniel Otzen

A thermodynamic analysis of fibrillar polymorphism

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Standard

A thermodynamic analysis of fibrillar polymorphism. / Jeppesen, Martin D; Hein, Kim; Nissen, Poul et al.
In: Advances in Biophysical Chemistry, Vol. 149, No. 1-2, 01.06.2010, p. 40-6.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Vancouver

Jeppesen MD, Hein K, Nissen P, Westh P, Otzen DE. A thermodynamic analysis of fibrillar polymorphism. Advances in Biophysical Chemistry. 2010 Jun 1;149(1-2):40-6. doi: 10.1016/j.bpc.2010.03.016

Author

Jeppesen, Martin D ; Hein, Kim ; Nissen, Poul et al. / A thermodynamic analysis of fibrillar polymorphism. In: Advances in Biophysical Chemistry. 2010 ; Vol. 149, No. 1-2. pp. 40-6.

Bibtex

@article{719a72901fde477384d8998b8741403b,

title = "A thermodynamic analysis of fibrillar polymorphism",

abstract = "We explore the thermodynamic properties of three different fibrils of the peptide hormone glucagon, formed under different salt conditions (glycine, sulfate and NaCl, respectively), and differing considerably in compactness. The three fibrils display a large variation in the specific heat capacity DeltaC(p) determined by isothermal titration calorimetry. Sulfate fibrils show a negative DeltaC(p) expected from a folding reaction, while the DeltaC(p) for glycine fibrils is essentially zero. NaCl fibrils, which are less stable than the other fibrils, have a large and positive C(p). The predicted change in solvent accessible area is not a useful predictor of fibrillar DeltaC(p) unlike the case for globular proteins. We speculate that strong backbone interactions may lead to the unfavorable burial of polar side residues, water and/or charged groups which all can have major influence on the change in C(p). These results highlight differences in the driving forces of native folding and fibril formation.",

keywords = "Amino Acid Sequence, Calorimetry, Circular Dichroism, Glucagon, Glycine, Molecular Sequence Data, Pancreatic Elastase, Protein Folding, Protein Structure, Tertiary, Sodium Chloride, Sulfates, Thermodynamics",

author = "Jeppesen, {Martin D} and Kim Hein and Poul Nissen and Peter Westh and Otzen, {Daniel E}",

year = "2010",

month = jun,

day = "1",

doi = "10.1016/j.bpc.2010.03.016",

language = "English",

volume = "149",

pages = "40--6",

journal = "Advances in Biophysical Chemistry",

issn = "1057-8943",

publisher = "J A I Press Inc.",

number = "1-2",

}

RIS

TY - JOUR

T1 - A thermodynamic analysis of fibrillar polymorphism

AU - Jeppesen, Martin D

AU - Hein, Kim

AU - Nissen, Poul

AU - Westh, Peter

AU - Otzen, Daniel E

PY - 2010/6/1

Y1 - 2010/6/1

N2 - We explore the thermodynamic properties of three different fibrils of the peptide hormone glucagon, formed under different salt conditions (glycine, sulfate and NaCl, respectively), and differing considerably in compactness. The three fibrils display a large variation in the specific heat capacity DeltaC(p) determined by isothermal titration calorimetry. Sulfate fibrils show a negative DeltaC(p) expected from a folding reaction, while the DeltaC(p) for glycine fibrils is essentially zero. NaCl fibrils, which are less stable than the other fibrils, have a large and positive C(p). The predicted change in solvent accessible area is not a useful predictor of fibrillar DeltaC(p) unlike the case for globular proteins. We speculate that strong backbone interactions may lead to the unfavorable burial of polar side residues, water and/or charged groups which all can have major influence on the change in C(p). These results highlight differences in the driving forces of native folding and fibril formation.

AB - We explore the thermodynamic properties of three different fibrils of the peptide hormone glucagon, formed under different salt conditions (glycine, sulfate and NaCl, respectively), and differing considerably in compactness. The three fibrils display a large variation in the specific heat capacity DeltaC(p) determined by isothermal titration calorimetry. Sulfate fibrils show a negative DeltaC(p) expected from a folding reaction, while the DeltaC(p) for glycine fibrils is essentially zero. NaCl fibrils, which are less stable than the other fibrils, have a large and positive C(p). The predicted change in solvent accessible area is not a useful predictor of fibrillar DeltaC(p) unlike the case for globular proteins. We speculate that strong backbone interactions may lead to the unfavorable burial of polar side residues, water and/or charged groups which all can have major influence on the change in C(p). These results highlight differences in the driving forces of native folding and fibril formation.

KW - Amino Acid Sequence

KW - Calorimetry

KW - Circular Dichroism

KW - Glucagon

KW - Glycine

KW - Molecular Sequence Data

KW - Pancreatic Elastase

KW - Protein Folding

KW - Protein Structure, Tertiary

KW - Sodium Chloride

KW - Sulfates

KW - Thermodynamics

U2 - 10.1016/j.bpc.2010.03.016

DO - 10.1016/j.bpc.2010.03.016

M3 - Journal article

C2 - 20435401

VL - 149

SP - 40

EP - 46

JO - Advances in Biophysical Chemistry

JF - Advances in Biophysical Chemistry

SN - 1057-8943

IS - 1-2

ER -