---
_id: '8466'
abstract:
- lang: eng
text: Recent advances in NMR spectroscopy and the availability of high magnetic
field strengths now offer the possibility to record real-time 3D NMR spectra of
short-lived protein states, e.g., states that become transiently populated during
protein folding. Here we present a strategy for obtaining sequential NMR assignments
as well as atom-resolved information on structural and dynamic features within
a folding intermediate of the amyloidogenic protein β2-microglobulin that has
a half-lifetime of only 20 min.
article_processing_charge: No
article_type: original
author:
- first_name: Enrico
full_name: Rennella, Enrico
last_name: Rennella
- first_name: Thomas
full_name: Cutuil, Thomas
last_name: Cutuil
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: Isabel
full_name: Ayala, Isabel
last_name: Ayala
- first_name: Vincent
full_name: Forge, Vincent
last_name: Forge
- first_name: Bernhard
full_name: Brutscher, Bernhard
last_name: Brutscher
citation:
ama: Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. Real-time NMR
characterization of structure and dynamics in a transiently populated protein
folding intermediate. Journal of the American Chemical Society. 2012;134(19):8066-8069.
doi:10.1021/ja302598j
apa: Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., & Brutscher,
B. (2012). Real-time NMR characterization of structure and dynamics in a transiently
populated protein folding intermediate. Journal of the American Chemical Society.
American Chemical Society. https://doi.org/10.1021/ja302598j
chicago: Rennella, Enrico, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge,
and Bernhard Brutscher. “Real-Time NMR Characterization of Structure and Dynamics
in a Transiently Populated Protein Folding Intermediate.” Journal of the American
Chemical Society. American Chemical Society, 2012. https://doi.org/10.1021/ja302598j.
ieee: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, and B. Brutscher,
“Real-time NMR characterization of structure and dynamics in a transiently populated
protein folding intermediate,” Journal of the American Chemical Society,
vol. 134, no. 19. American Chemical Society, pp. 8066–8069, 2012.
ista: Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. 2012. Real-time
NMR characterization of structure and dynamics in a transiently populated protein
folding intermediate. Journal of the American Chemical Society. 134(19), 8066–8069.
mla: Rennella, Enrico, et al. “Real-Time NMR Characterization of Structure and Dynamics
in a Transiently Populated Protein Folding Intermediate.” Journal of the American
Chemical Society, vol. 134, no. 19, American Chemical Society, 2012, pp. 8066–69,
doi:10.1021/ja302598j.
short: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, B. Brutscher, Journal
of the American Chemical Society 134 (2012) 8066–8069.
date_created: 2020-09-18T10:10:28Z
date_published: 2012-05-03T00:00:00Z
date_updated: 2021-01-12T08:19:28Z
day: '03'
doi: 10.1021/ja302598j
extern: '1'
intvolume: ' 134'
issue: '19'
language:
- iso: eng
month: '05'
oa_version: None
page: 8066-8069
publication: Journal of the American Chemical Society
publication_identifier:
issn:
- 0002-7863
- 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Real-time NMR characterization of structure and dynamics in a transiently populated
protein folding intermediate
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
year: '2012'
...
---
_id: '8467'
abstract:
- lang: eng
text: Partial deuteration is a powerful tool to increase coherence life times and
spectral resolution in proton solid-state NMR. The J coupling to deuterium needs,
however, to be decoupled to maintain the good resolution in the (usually indirect)
13C dimension(s). We present a simple and reversible way to expand a commercial
1.3 mm HCN MAS probe with a 2H channel with sufficient field strength for J-decoupling
of deuterium, namely 2–3 kHz. The coil is placed at the outside of the stator
and requires no significant modifications to the probe. The performance and the
realizable gains in sensitivity and resolution are demonstrated using perdeuterated
ubiquitin, with selectively CHD2-labeled methyl groups.
article_processing_charge: No
article_type: original
author:
- first_name: Matthias
full_name: Huber, Matthias
last_name: Huber
- first_name: Oliver
full_name: With, Oliver
last_name: With
- first_name: Paul
full_name: Schanda, Paul
id: 7B541462-FAF6-11E9-A490-E8DFE5697425
last_name: Schanda
orcid: 0000-0002-9350-7606
- first_name: René
full_name: Verel, René
last_name: Verel
- first_name: Matthias
full_name: Ernst, Matthias
last_name: Ernst
- first_name: Beat H.
full_name: Meier, Beat H.
last_name: Meier
citation:
ama: Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. A supplementary coil
for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance.
2012;214:76-80. doi:10.1016/j.jmr.2011.10.010
apa: Huber, M., With, O., Schanda, P., Verel, R., Ernst, M., & Meier, B. H.
(2012). A supplementary coil for 2H decoupling with commercial HCN MAS probes.
Journal of Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.jmr.2011.10.010
chicago: Huber, Matthias, Oliver With, Paul Schanda, René Verel, Matthias Ernst,
and Beat H. Meier. “A Supplementary Coil for 2H Decoupling with Commercial HCN
MAS Probes.” Journal of Magnetic Resonance. Elsevier, 2012. https://doi.org/10.1016/j.jmr.2011.10.010.
ieee: M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, and B. H. Meier, “A supplementary
coil for 2H decoupling with commercial HCN MAS probes,” Journal of Magnetic
Resonance, vol. 214. Elsevier, pp. 76–80, 2012.
ista: Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. 2012. A supplementary
coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance.
214, 76–80.
mla: Huber, Matthias, et al. “A Supplementary Coil for 2H Decoupling with Commercial
HCN MAS Probes.” Journal of Magnetic Resonance, vol. 214, Elsevier, 2012,
pp. 76–80, doi:10.1016/j.jmr.2011.10.010.
short: M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, B.H. Meier, Journal of
Magnetic Resonance 214 (2012) 76–80.
date_created: 2020-09-18T10:10:36Z
date_published: 2012-01-01T00:00:00Z
date_updated: 2021-01-12T08:19:28Z
day: '01'
doi: 10.1016/j.jmr.2011.10.010
extern: '1'
intvolume: ' 214'
language:
- iso: eng
month: '01'
oa_version: None
page: 76-80
publication: Journal of Magnetic Resonance
publication_identifier:
issn:
- 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: A supplementary coil for 2H decoupling with commercial HCN MAS probes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 214
year: '2012'
...
---
_id: '8502'
abstract:
- lang: eng
text: 'The famous ergodic hypothesis suggests that for a typical Hamiltonian on
a typical energy surface nearly all trajectories are dense. KAM theory disproves
it. Ehrenfest (The Conceptual Foundations of the Statistical Approach in Mechanics.
Ithaca, NY: Cornell University Press, 1959) and Birkhoff (Collected Math Papers.
Vol 2, New York: Dover, pp 462–465, 1968) stated the quasi-ergodic hypothesis
claiming that a typical Hamiltonian on a typical energy surface has a dense orbit.
This question is wide open. Herman (Proceedings of the International Congress
of Mathematicians, Vol II (Berlin, 1998). Doc Math 1998, Extra Vol II, Berlin:
Int Math Union, pp 797–808, 1998) proposed to look for an example of a Hamiltonian
near H0(I)=⟨I,I⟩2 with a dense orbit on the unit energy surface. In this paper
we construct a Hamiltonian H0(I)+εH1(θ,I,ε) which has an orbit dense in a set
of maximal Hausdorff dimension equal to 5 on the unit energy surface.'
article_processing_charge: No
article_type: original
author:
- first_name: Vadim
full_name: Kaloshin, Vadim
id: FE553552-CDE8-11E9-B324-C0EBE5697425
last_name: Kaloshin
orcid: 0000-0002-6051-2628
- first_name: Maria
full_name: Saprykina, Maria
last_name: Saprykina
citation:
ama: Kaloshin V, Saprykina M. An example of a nearly integrable Hamiltonian system
with a trajectory dense in a set of maximal Hausdorff dimension. Communications
in Mathematical Physics. 2012;315(3):643-697. doi:10.1007/s00220-012-1532-x
apa: Kaloshin, V., & Saprykina, M. (2012). An example of a nearly integrable
Hamiltonian system with a trajectory dense in a set of maximal Hausdorff dimension.
Communications in Mathematical Physics. Springer Nature. https://doi.org/10.1007/s00220-012-1532-x
chicago: Kaloshin, Vadim, and Maria Saprykina. “An Example of a Nearly Integrable
Hamiltonian System with a Trajectory Dense in a Set of Maximal Hausdorff Dimension.”
Communications in Mathematical Physics. Springer Nature, 2012. https://doi.org/10.1007/s00220-012-1532-x.
ieee: V. Kaloshin and M. Saprykina, “An example of a nearly integrable Hamiltonian
system with a trajectory dense in a set of maximal Hausdorff dimension,” Communications
in Mathematical Physics, vol. 315, no. 3. Springer Nature, pp. 643–697, 2012.
ista: Kaloshin V, Saprykina M. 2012. An example of a nearly integrable Hamiltonian
system with a trajectory dense in a set of maximal Hausdorff dimension. Communications
in Mathematical Physics. 315(3), 643–697.
mla: Kaloshin, Vadim, and Maria Saprykina. “An Example of a Nearly Integrable Hamiltonian
System with a Trajectory Dense in a Set of Maximal Hausdorff Dimension.” Communications
in Mathematical Physics, vol. 315, no. 3, Springer Nature, 2012, pp. 643–97,
doi:10.1007/s00220-012-1532-x.
short: V. Kaloshin, M. Saprykina, Communications in Mathematical Physics 315 (2012)
643–697.
date_created: 2020-09-18T10:47:16Z
date_published: 2012-11-01T00:00:00Z
date_updated: 2021-01-12T08:19:44Z
day: '01'
doi: 10.1007/s00220-012-1532-x
extern: '1'
intvolume: ' 315'
issue: '3'
keyword:
- Mathematical Physics
- Statistical and Nonlinear Physics
language:
- iso: eng
month: '11'
oa_version: None
page: 643-697
publication: Communications in Mathematical Physics
publication_identifier:
issn:
- 0010-3616
- 1432-0916
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: An example of a nearly integrable Hamiltonian system with a trajectory dense
in a set of maximal Hausdorff dimension
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 315
year: '2012'
...
---
_id: '858'
abstract:
- lang: eng
text: 'ackground: The evolution and genomic stop codon frequencies have not been
rigorously studied with the exception of coding of non-canonical amino acids.
Here we study the rate of evolution and frequency distribution of stop codons
in bacterial genomes.Results: We show that in bacteria stop codons evolve slower
than synonymous sites, suggesting the action of weak negative selection. However,
the frequency of stop codons relative to genomic nucleotide content indicated
that this selection regime is not straightforward. The frequency of TAA and TGA
stop codons is GC-content dependent, with TAA decreasing and TGA increasing with
GC-content, while TAG frequency is independent of GC-content. Applying a formal,
analytical model to these data we found that the relationship between stop codon
frequencies and nucleotide content cannot be explained by mutational biases or
selection on nucleotide content. However, with weak nucleotide content-dependent
selection on TAG, -0.5 < Nes < 1.5, the model fits all of the data and recapitulates
the relationship between TAG and nucleotide content. For biologically plausible
rates of mutations we show that, in bacteria, TAG stop codon is universally associated
with lower fitness, with TAA being the optimal for G-content < 16% while for G-content
> 16% TGA has a higher fitness than TAG.Conclusions: Our data indicate that TAG
codon is universally suboptimal in the bacterial lineage, such that TAA is likely
to be the preferred stop codon for low GC content while the TGA is the preferred
stop codon for high GC content. The optimization of stop codon usage may therefore
be useful in genome engineering or gene expression optimization applications.Reviewers:
This article was reviewed by Michail Gelfand, Arcady Mushegian and Shamil Sunyaev.
For the full reviews, please go to the Reviewers'' Comments section.'
acknowledgement: |
We thank Elena Alkalaeva and Peter Kolosov for insightful discussion and Brian Charlesworth for a critical reading of our manuscript. The work has been supported by a Plan Nacional grant from the Spanish Ministry of Science and Innovation, EMBO Young Investigator and Howard Hughes Medical Institute International Early Career Scientist awards.
author:
- first_name: Inna
full_name: Povolotskaya, Inna
last_name: Povolotskaya
- first_name: Fyodor
full_name: Fyodor Kondrashov
id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
last_name: Kondrashov
orcid: 0000-0001-8243-4694
- first_name: Alice
full_name: Ledda, Alice
last_name: Ledda
- first_name: Peter
full_name: Vlasov, Peter K
last_name: Vlasov
citation:
ama: Povolotskaya I, Kondrashov F, Ledda A, Vlasov P. Stop codons in bacteria are
not selectively equivalent. Biology Direct. 2012;7. doi:10.1186/1745-6150-7-30
apa: Povolotskaya, I., Kondrashov, F., Ledda, A., & Vlasov, P. (2012). Stop
codons in bacteria are not selectively equivalent. Biology Direct. BioMed
Central. https://doi.org/10.1186/1745-6150-7-30
chicago: Povolotskaya, Inna, Fyodor Kondrashov, Alice Ledda, and Peter Vlasov. “Stop
Codons in Bacteria Are Not Selectively Equivalent.” Biology Direct. BioMed
Central, 2012. https://doi.org/10.1186/1745-6150-7-30.
ieee: I. Povolotskaya, F. Kondrashov, A. Ledda, and P. Vlasov, “Stop codons in bacteria
are not selectively equivalent,” Biology Direct, vol. 7. BioMed Central,
2012.
ista: Povolotskaya I, Kondrashov F, Ledda A, Vlasov P. 2012. Stop codons in bacteria
are not selectively equivalent. Biology Direct. 7.
mla: Povolotskaya, Inna, et al. “Stop Codons in Bacteria Are Not Selectively Equivalent.”
Biology Direct, vol. 7, BioMed Central, 2012, doi:10.1186/1745-6150-7-30.
short: I. Povolotskaya, F. Kondrashov, A. Ledda, P. Vlasov, Biology Direct 7 (2012).
date_created: 2018-12-11T11:48:52Z
date_published: 2012-09-01T00:00:00Z
date_updated: 2021-01-12T08:20:08Z
day: '01'
doi: 10.1186/1745-6150-7-30
extern: 1
intvolume: ' 7'
license: https://creativecommons.org/licenses/by/4.0/
month: '09'
publication: Biology Direct
publication_status: published
publisher: BioMed Central
publist_id: '6792'
quality_controlled: 0
status: public
title: Stop codons in bacteria are not selectively equivalent
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
volume: 7
year: '2012'
...
---
_id: '900'
abstract:
- lang: eng
text: 'The main forces directing long-term molecular evolution remain obscure. A
sizable fraction of amino-acid substitutions seem to be fixed by positive selection,
but it is unclear to what degree long-term protein evolution is constrained by
epistasis, that is, instances when substitutions that are accepted in one genotype
are deleterious in another. Here we obtain a quantitative estimate of the prevalence
of epistasis in long-term protein evolution by relating data on amino-acid usage
in 14 organelle proteins and 2 nuclear-encoded proteins to their rates of short-term
evolution. We studied multiple alignments of at least 1,000 orthologues for each
of these 16 proteins from species from a diverse phylogenetic background and found
that an average site contained approximately eight different amino acids. Thus,
without epistasis an average site should accept two-fifths of all possible amino
acids, and the average rate of amino-acid substitutions should therefore be about
three-fifths lower than the rate of neutral evolution. However, we found that
the measured rate of amino-acid substitution in recent evolution is 20 times lower
than the rate of neutral evolution and an order of magnitude lower than that expected
in the absence of epistasis. These data indicate that epistasis is pervasive throughout
protein evolution: about 90 per cent of all amino-acid substitutions have a neutral
or beneficial impact only in the genetic backgrounds in which they occur, and
must therefore be deleterious in a different background of other species. Our
findings show that most amino-acid substitutions have different fitness effects
in different species and that epistasis provides the primary conceptual framework
to describe the tempo and mode of long-term protein evolution.'
acknowledgement: |
The work was supported by Plan Nacional grants from the Spanish Ministry of Science and Innovation, to F.A.K. and C.N. C.K. was supported by the European Union FP7 project Quantomics (KBBE2A222664). F.A.K. is a European Molecular Biology Organization Young Investigator and Howard Hughes Medical Institute International Early Career Scientist. We thank B. Lehner and T. Warnecke for input and a critical reading of the manuscript.
author:
- first_name: Michael
full_name: Breen, Michael S
last_name: Breen
- first_name: Carsten
full_name: Kemena, Carsten
last_name: Kemena
- first_name: Peter
full_name: Vlasov, Peter K
last_name: Vlasov
- first_name: Cédric
full_name: Notredame, Cédric
last_name: Notredame
- first_name: Fyodor
full_name: Fyodor Kondrashov
id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
last_name: Kondrashov
orcid: 0000-0001-8243-4694
citation:
ama: Breen M, Kemena C, Vlasov P, Notredame C, Kondrashov F. Epistasis as the primary
factor in molecular evolution. Nature. 2012;490(7421):535-538. doi:10.1038/nature11510
apa: Breen, M., Kemena, C., Vlasov, P., Notredame, C., & Kondrashov, F. (2012).
Epistasis as the primary factor in molecular evolution. Nature. Nature
Publishing Group. https://doi.org/10.1038/nature11510
chicago: Breen, Michael, Carsten Kemena, Peter Vlasov, Cédric Notredame, and Fyodor
Kondrashov. “Epistasis as the Primary Factor in Molecular Evolution.” Nature.
Nature Publishing Group, 2012. https://doi.org/10.1038/nature11510.
ieee: M. Breen, C. Kemena, P. Vlasov, C. Notredame, and F. Kondrashov, “Epistasis
as the primary factor in molecular evolution,” Nature, vol. 490, no. 7421.
Nature Publishing Group, pp. 535–538, 2012.
ista: Breen M, Kemena C, Vlasov P, Notredame C, Kondrashov F. 2012. Epistasis as
the primary factor in molecular evolution. Nature. 490(7421), 535–538.
mla: Breen, Michael, et al. “Epistasis as the Primary Factor in Molecular Evolution.”
Nature, vol. 490, no. 7421, Nature Publishing Group, 2012, pp. 535–38,
doi:10.1038/nature11510.
short: M. Breen, C. Kemena, P. Vlasov, C. Notredame, F. Kondrashov, Nature 490 (2012)
535–538.
date_created: 2018-12-11T11:49:06Z
date_published: 2012-10-25T00:00:00Z
date_updated: 2021-01-12T08:21:45Z
day: '25'
doi: 10.1038/nature11510
extern: 1
intvolume: ' 490'
issue: '7421'
month: '10'
page: 535 - 538
publication: Nature
publication_status: published
publisher: Nature Publishing Group
publist_id: '6748'
quality_controlled: 0
status: public
title: Epistasis as the primary factor in molecular evolution
type: journal_article
volume: 490
year: '2012'
...