Open Access
Protein Science, volume 23, issue 9, pages 1275-1290
A maximum entropy approach to the study of residue-specific backbone angle distributions in alpha-synuclein, an intrinsically disordered protein
1
Laboratory of Chemical Physics; National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health; Bethesda Maryland 20892
|
2
Max Planck Institute of Biophysics; Max-von-Laue-Straße 3, D-60438 Frankfurt am Main Germany
|
Publication type: Journal Article
Publication date: 2014-07-22
Journal:
Protein Science
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 8
ISSN: 09618368, 1469896X
DOI:
10.1002/PRO.2511
PubMed ID:
24976112
Biochemistry
Molecular Biology
Abstract
α‐Synuclein is an intrinsically disordered protein of 140 residues that switches to an α‐helical conformation upon binding phospholipid membranes. We characterize its residue‐specific backbone structure in free solution with a novel maximum entropy procedure that integrates an extensive set of NMR data. These data include intraresidue and sequential HNHα and HNHN NOEs, values for 3JHNHα, 1JHαCα, 2JCαN, and 1JCαN, as well as chemical shifts of 15N, 13Cα, and 13C′ nuclei, which are sensitive to backbone torsion angles. Distributions of these torsion angles were identified that yield best agreement to the experimental data, while using an entropy term to minimize the deviation from statistical distributions seen in a large protein coil library. Results indicate that although at the individual residue level considerable deviations from the coil library distribution are seen, on average the fitted distributions agree fairly well with this library, yielding a moderate population (20–30%) of the PPII region and a somewhat higher population of the potentially aggregation‐prone β region (20–40%) than seen in the database. A generally lower population of the αR region (10–20%) is found. Analysis of 1H1H NOE data required consideration of the considerable backbone diffusion anisotropy of a disordered protein.
Citations by journals
|
1
2
3
4
5
6
|
|
|
Journal of Biomolecular NMR
|
Journal of Biomolecular NMR
6 publications, 8.33%
|
|
Journal of Chemical Theory and Computation
|
Journal of Chemical Theory and Computation
6 publications, 8.33%
|
|
Journal of Physical Chemistry B
|
Journal of Physical Chemistry B
5 publications, 6.94%
|
|
Biochemistry
|
Biochemistry
4 publications, 5.56%
|
|
Journal of the American Chemical Society
|
Journal of the American Chemical Society
3 publications, 4.17%
|
|
Journal of Physical Chemistry Letters
|
Journal of Physical Chemistry Letters
3 publications, 4.17%
|
|
Biophysical Journal
|
Biophysical Journal
2 publications, 2.78%
|
|
Protein Science
|
Protein Science
2 publications, 2.78%
|
|
ChemPhysChem
|
ChemPhysChem
2 publications, 2.78%
|
|
Chemical Science
|
Chemical Science
2 publications, 2.78%
|
|
Progress in Molecular Biology and Translational Science
|
Progress in Molecular Biology and Translational Science
2 publications, 2.78%
|
|
Methods in Enzymology
|
Methods in Enzymology
2 publications, 2.78%
|
|
Journal of Chemical Physics
|
Journal of Chemical Physics
1 publication, 1.39%
|
|
Physical Review E
|
Physical Review E
1 publication, 1.39%
|
|
Physical Review Research
|
Physical Review Research
1 publication, 1.39%
|
|
Magnetic Resonance
|
Magnetic Resonance
1 publication, 1.39%
|
|
International Journal of Molecular Sciences
|
International Journal of Molecular Sciences
1 publication, 1.39%
|
|
Entropy
|
Entropy
1 publication, 1.39%
|
|
Biomolecules
|
Biomolecules
1 publication, 1.39%
|
|
npj Genomic Medicine
|
npj Genomic Medicine
1 publication, 1.39%
|
|
Scientific Reports
|
Scientific Reports
1 publication, 1.39%
|
|
Nature Methods
|
Nature Methods
1 publication, 1.39%
|
|
Communications Biology
|
Communications Biology
1 publication, 1.39%
|
|
RSC Advances
|
RSC Advances
1 publication, 1.39%
|
|
Biochimica et Biophysica Acta - Proteins and Proteomics
|
Biochimica et Biophysica Acta - Proteins and Proteomics
1 publication, 1.39%
|
|
Progress in Nuclear Magnetic Resonance Spectroscopy
|
Progress in Nuclear Magnetic Resonance Spectroscopy
1 publication, 1.39%
|
|
Journal of Chemical Information and Modeling
|
Journal of Chemical Information and Modeling
1 publication, 1.39%
|
|
JACS Au
|
JACS Au
1 publication, 1.39%
|
|
Journal of Physical Chemistry A
|
Journal of Physical Chemistry A
1 publication, 1.39%
|
|
1
2
3
4
5
6
|
Citations by publishers
|
5
10
15
20
25
|
|
|
American Chemical Society (ACS)
|
American Chemical Society (ACS)
24 publications, 33.33%
|
|
Springer Nature
|
Springer Nature
11 publications, 15.28%
|
|
Elsevier
|
Elsevier
8 publications, 11.11%
|
|
Wiley
|
Wiley
5 publications, 6.94%
|
|
Royal Society of Chemistry (RSC)
|
Royal Society of Chemistry (RSC)
4 publications, 5.56%
|
|
Multidisciplinary Digital Publishing Institute (MDPI)
|
Multidisciplinary Digital Publishing Institute (MDPI)
3 publications, 4.17%
|
|
American Physical Society (APS)
|
American Physical Society (APS)
2 publications, 2.78%
|
|
Biophysical Society
|
Biophysical Society
2 publications, 2.78%
|
|
American Institute of Physics (AIP)
|
American Institute of Physics (AIP)
1 publication, 1.39%
|
|
Copernicus
|
Copernicus
1 publication, 1.39%
|
|
Korean Society for Brain and Neural Science
|
Korean Society for Brain and Neural Science, 1, 1.39%
Korean Society for Brain and Neural Science
1 publication, 1.39%
|
|
Proceedings of the National Academy of Sciences (PNAS)
|
Proceedings of the National Academy of Sciences (PNAS)
1 publication, 1.39%
|
|
5
10
15
20
25
|
- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
{"yearsCitations":{"type":"bar","data":{"show":true,"labels":[2014,2015,2016,2017,2018,2019,2020,2021,2022,2023,2024],"ids":[0,0,0,0,0,0,0,0,0,0,0],"codes":[0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["","","","","","","","","","",""],"datasets":[{"label":"Citations number","data":[2,7,8,3,6,12,13,6,8,6,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":["2.78","9.72","11.11","4.17","8.33","16.67","18.06","8.33","11.11","8.33","1.39"],"barThickness":null}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"journals":{"type":"bar","data":{"show":true,"labels":["Journal of Biomolecular NMR","Journal of Chemical Theory and Computation","Journal of Physical Chemistry B","Biochemistry","Journal of the American Chemical Society","Journal of Physical Chemistry Letters","Biophysical Journal","Protein Science","ChemPhysChem","Chemical Science","Progress in Molecular Biology and Translational Science","Methods in Enzymology","Journal of Chemical Physics","Physical Review E","Physical Review Research","Magnetic Resonance","International Journal of Molecular Sciences","Entropy","Biomolecules","npj Genomic Medicine","Scientific Reports","Nature Methods","Communications Biology","RSC Advances","Biochimica et Biophysica Acta - Proteins and Proteomics","Progress in Nuclear Magnetic Resonance Spectroscopy","Journal of Chemical Information and Modeling","JACS Au","Journal of Physical Chemistry A"],"ids":[21752,58,14990,9964,4813,21963,4026,2646,16306,9646,22083,24566,544,12743,26813,28502,14627,2366,13780,18368,13767,14446,11778,3100,11289,24071,13608,26622,15255],"codes":[0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/Bmz9XNb2QDptmPTa5N8huM54tShVewUj8fZqKFRy_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/ARM4e6URKRsbRZvIF0vFis9DjxGloBjnBYJXbHmZ_medium.webp","\/storage\/images\/resized\/nrK64iXHTzj43wMrfN1ZoUQ0vanswGzWPN45K3jA_medium.webp","\/storage\/images\/resized\/nrK64iXHTzj43wMrfN1ZoUQ0vanswGzWPN45K3jA_medium.webp","\/storage\/images\/resized\/cxBZptDQQvWgQeXj5GoTXDfgUEoGVvFgpDRctnDr_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp"],"datasets":[{"label":"","data":[6,6,5,4,3,3,2,2,2,2,2,2,1,1,1,1,1,1,1,1,1,1,1,1,1,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[8.33,8.33,6.94,5.56,4.17,4.17,2.78,2.78,2.78,2.78,2.78,2.78,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39,1.39],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Journals","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"publishers":{"type":"bar","data":{"show":true,"labels":["American Chemical Society (ACS)","Springer Nature","Elsevier","Wiley","Royal Society of Chemistry (RSC)","Multidisciplinary Digital Publishing Institute (MDPI)","American Physical Society (APS)","Biophysical Society","American Institute of Physics (AIP)","Copernicus","Korean Society for Brain and Neural Science","Proceedings of the National Academy of Sciences (PNAS)"],"ids":[40,8,17,11,123,202,1539,1454,250,3207,5390,162],"codes":[0,0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/voXLqlsvTwv5p3iMQ8Dhs95nqB4AXOG7Taj7G4ra_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/bRyGpdm98BkAUYiK1YFNpl5Z7hPu6Gd87gbIeuG3_medium.webp","\/storage\/images\/resized\/leiAYcRDGTSl5B1eCnwpSGqmDEUEfDPPoYisFGhT_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/nrK64iXHTzj43wMrfN1ZoUQ0vanswGzWPN45K3jA_medium.webp","\/storage\/images\/resized\/Bmz9XNb2QDptmPTa5N8huM54tShVewUj8fZqKFRy_medium.webp","\/storage\/images\/resized\/ARM4e6URKRsbRZvIF0vFis9DjxGloBjnBYJXbHmZ_medium.webp","\/storage\/images\/resized\/cxBZptDQQvWgQeXj5GoTXDfgUEoGVvFgpDRctnDr_medium.webp","","\/storage\/images\/resized\/mxFdPe9qujsfvfYfcN0QOclAiYORFb0xrRlwV8gs_medium.webp"],"datasets":[{"label":"","data":[24,11,8,5,4,3,2,2,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[33.33,15.28,11.11,6.94,5.56,4.17,2.78,2.78,1.39,1.39,1.39,1.39],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Publishers","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}}}
Metrics
Cite this
GOST |
RIS |
BibTex |
MLA
Cite this
GOST
Copy
Mantsyzov A. B. et al. A maximum entropy approach to the study of residue-specific backbone angle distributions in alpha-synuclein, an intrinsically disordered protein // Protein Science. 2014. Vol. 23. No. 9. pp. 1275-1290.
GOST all authors (up to 50)
Copy
Mantsyzov A. B., Maltsev A. S., Ying J., Shen Y., Hummer G., Bax A. A maximum entropy approach to the study of residue-specific backbone angle distributions in alpha-synuclein, an intrinsically disordered protein // Protein Science. 2014. Vol. 23. No. 9. pp. 1275-1290.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1002/PRO.2511
UR - https://doi.org/10.1002%2FPRO.2511
TI - A maximum entropy approach to the study of residue-specific backbone angle distributions in alpha-synuclein, an intrinsically disordered protein
T2 - Protein Science
AU - Mantsyzov, Alexey B.
AU - Maltsev, Alexander S
AU - Ying, Jinfa
AU - Shen, Yang
AU - Hummer, Gerhard
AU - Bax, Adriaan
PY - 2014
DA - 2014/07/22 00:00:00
PB - Wiley
SP - 1275-1290
IS - 9
VL - 23
PMID - 24976112
SN - 0961-8368
SN - 1469-896X
ER -
Cite this
BibTex
Copy
@article{2014_Mantsyzov,
author = {Alexey B. Mantsyzov and Alexander S Maltsev and Jinfa Ying and Yang Shen and Gerhard Hummer and Adriaan Bax},
title = {A maximum entropy approach to the study of residue-specific backbone angle distributions in alpha-synuclein, an intrinsically disordered protein},
journal = {Protein Science},
year = {2014},
volume = {23},
publisher = {Wiley},
month = {jul},
url = {https://doi.org/10.1002%2FPRO.2511},
number = {9},
pages = {1275--1290},
doi = {10.1002/PRO.2511}
}
Cite this
MLA
Copy
Mantsyzov, Alexey B., et al. “A maximum entropy approach to the study of residue-specific backbone angle distributions in alpha-synuclein, an intrinsically disordered protein.” Protein Science, vol. 23, no. 9, Jul. 2014, pp. 1275-1290. https://doi.org/10.1002%2FPRO.2511.
Profiles