The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The same, but different, but still the same : structural and dynamical differences of neutrophil elastase and cathepsin G. / Schuhmann, Fabian; Tan, Xiangyin; Gerhards, Luca; Bordallo, Heloisa N.; Solov'yov, Ilia A.

In: European Physical Journal D, Vol. 76, No. 7, 126, 07.2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Schuhmann, F, Tan, X, Gerhards, L, Bordallo, HN & Solov'yov, IA 2022, 'The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G', European Physical Journal D, vol. 76, no. 7, 126. https://doi.org/10.1140/epjd/s10053-022-00452-0

APA

Schuhmann, F., Tan, X., Gerhards, L., Bordallo, H. N., & Solov'yov, I. A. (2022). The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G. European Physical Journal D, 76(7), [126]. https://doi.org/10.1140/epjd/s10053-022-00452-0

Vancouver

Schuhmann F, Tan X, Gerhards L, Bordallo HN, Solov'yov IA. The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G. European Physical Journal D. 2022 Jul;76(7). 126. https://doi.org/10.1140/epjd/s10053-022-00452-0

Author

Schuhmann, Fabian ; Tan, Xiangyin ; Gerhards, Luca ; Bordallo, Heloisa N. ; Solov'yov, Ilia A. / The same, but different, but still the same : structural and dynamical differences of neutrophil elastase and cathepsin G. In: European Physical Journal D. 2022 ; Vol. 76, No. 7.

Bibtex

@article{3ab0ce25f7ec4fefa18f3d558d9d596b,
title = "The same, but different, but still the same: structural and dynamical differences of neutrophil elastase and cathepsin G",
abstract = "Although the general mechanism for serine protease catalysis is well established, some questions still remain. For instance, the two enzymes, neutrophil elastase and cathepsin G, have a lot of structural resemblances. However, elastase degrades virulence factors, while cathepsin G does not. This paper studies both enzymes computationally to probe for their conformational differences. In the process, a methodology is established to not only quantify similarities between the protein trajectories describing proteins' temporal evolution but also account for a varying number of amino acid residues comprising each structure. Our results indicate slight differences in the behavior of the active sites of neutrophil elastase and cathepsin G in the solvent. These subtle changes could indicate differences in the general behavior responsible for the different specificity of the two enzymes.",
keywords = "OPTIMIZATION, ALIGNMENT, MECHANISM, TARGETS",
author = "Fabian Schuhmann and Xiangyin Tan and Luca Gerhards and Bordallo, {Heloisa N.} and Solov'yov, {Ilia A.}",
year = "2022",
month = jul,
doi = "10.1140/epjd/s10053-022-00452-0",
language = "English",
volume = "76",
journal = "European Physical Journal D",
issn = "1434-6060",
publisher = "Springer",
number = "7",

}

RIS

TY - JOUR

T1 - The same, but different, but still the same

T2 - structural and dynamical differences of neutrophil elastase and cathepsin G

AU - Schuhmann, Fabian

AU - Tan, Xiangyin

AU - Gerhards, Luca

AU - Bordallo, Heloisa N.

AU - Solov'yov, Ilia A.

PY - 2022/7

Y1 - 2022/7

N2 - Although the general mechanism for serine protease catalysis is well established, some questions still remain. For instance, the two enzymes, neutrophil elastase and cathepsin G, have a lot of structural resemblances. However, elastase degrades virulence factors, while cathepsin G does not. This paper studies both enzymes computationally to probe for their conformational differences. In the process, a methodology is established to not only quantify similarities between the protein trajectories describing proteins' temporal evolution but also account for a varying number of amino acid residues comprising each structure. Our results indicate slight differences in the behavior of the active sites of neutrophil elastase and cathepsin G in the solvent. These subtle changes could indicate differences in the general behavior responsible for the different specificity of the two enzymes.

AB - Although the general mechanism for serine protease catalysis is well established, some questions still remain. For instance, the two enzymes, neutrophil elastase and cathepsin G, have a lot of structural resemblances. However, elastase degrades virulence factors, while cathepsin G does not. This paper studies both enzymes computationally to probe for their conformational differences. In the process, a methodology is established to not only quantify similarities between the protein trajectories describing proteins' temporal evolution but also account for a varying number of amino acid residues comprising each structure. Our results indicate slight differences in the behavior of the active sites of neutrophil elastase and cathepsin G in the solvent. These subtle changes could indicate differences in the general behavior responsible for the different specificity of the two enzymes.

KW - OPTIMIZATION

KW - ALIGNMENT

KW - MECHANISM

KW - TARGETS

U2 - 10.1140/epjd/s10053-022-00452-0

DO - 10.1140/epjd/s10053-022-00452-0

M3 - Journal article

VL - 76

JO - European Physical Journal D

JF - European Physical Journal D

SN - 1434-6060

IS - 7

M1 - 126

ER -

ID: 315253505