5 research outputs found
ΠΡΠ½ΠΎΠ²Π½Ρ ΠΏΡΠ΄Ρ ΠΎΠ΄ΠΈ Π΄ΠΎ ΡΠΎΠ·ΡΠΎΠ±Π»Π΅Π½Π½Ρ Π΄ΠΈΠ·Π°ΠΉΠ½Ρ ΡΠΏΠ°ΠΊΠΎΠ²ΠΊΠΈ
Π£ΠΏΠ°ΠΊΠΎΠ²ΠΊΠ° β ΠΎΡΡΠ°Π½Π½ΡΠΉ ΠΏΡΠΈΠ·ΠΎΠ², ΡΠΊΠΈΠΉ Π±Π°ΡΠΈΡΡ ΠΏΠΎΠΊΡΠΏΠ΅ΡΡ, Ρ ΠΎΡΡΠ°Π½Π½ΡΠΉ ΡΠ°Π½Ρ
ΠΏΠ΅ΡΠ΅ΠΊΠΎΠ½Π°ΡΠΈ ΠΉΠΎΠ³ΠΎ ΠΊΡΠΏΠΈΡΠΈ ΡΠΎΠ²Π°Ρ [1], ΡΠΎΠΌΡ Π½Π°Π΄ ΡΠΎΠ·ΡΠΎΠ±Π»Π΅Π½Π½ΡΠΌ ΡΡΠΊΠ°Π²ΠΎΠ³ΠΎ,
ΠΎΡΠΈΠ³ΡΠ½Π°Π»ΡΠ½ΠΎΠ³ΠΎ Π΄ΠΈΠ·Π°ΠΉΠ½Ρ ΡΠΏΠ°ΠΊΠΎΠ²ΠΊΠΈ ΠΏΡΠ°ΡΡΡ ΡΡΠ»Π° Π°ΡΠΌΡΡ ΠΏΡΠΎΡΠ΅ΡΡΠΎΠ½Π°Π»ΡΠ².
ΠΠΈΠ·Π°ΠΉΠ½ ΡΠΏΠ°ΠΊΠΎΠ²ΠΊΠΈ Π²ΠΊΠ»ΡΡΠ°Ρ Π³Π°ΡΠΌΠΎΠ½ΡΡΠ½Ρ ΡΡΠΊΡΠΏΠ½ΡΡΡΡ ΡΠ°ΠΊΠΈΡ
Π΅Π»Π΅ΠΌΠ΅Π½ΡΡΠ², ΡΠΊ:
ΡΠΎΡΠΌΠ°, ΠΌΠ°ΡΠ΅ΡΡΠ°Π», ΡΠΎΠ·ΠΌΡΡΠΈ, ΡΠΊΡΡΡΡ Π²ΠΈΠ³ΠΎΡΠΎΠ²Π»Π΅Π½Π½Ρ, Π²ΠΈΠ΄ Π΄ΡΡΠΊΡ, ΠΊΠΎΠ»ΡΠΎΡΠΈ
Disentangling the Coil: Modulation of Conformational and Dynamic Properties by Site-Directed Mutation in the Non-Native State of Hen Egg White Lysozyme
The conformational analysis of non-native states of proteins
remains one of the most difficult problems in structural biology,
because such states are represented by a superimposition of several
states that are rapidly interconverting. Hence, model building of
the conformational ensemble remains challenging, although many different
biophysical observables can be determined in non-native states of
proteins. Here, we present a comprehensive analysis of non-native
states of wild-type and mutant forms of the model protein lysozyme
by nuclear magnetic resonance spectroscopy. Relaxation rates, chemical
shifts, backbone and side chain coupling constants, residual dipolar
couplings, diffusion rate constants, and small-angle scattering data
merged with computational approaches, such as <i>flexible meccano</i> and ASTEROIDS, allow the description of the non-native state of
hen egg white lysozyme in unprecedented detail
Modulation of Structure and Dynamics by Disulfide Bond Formation in Unfolded States
During oxidative folding, the formation of disulfide
bonds has
profound effects on guiding the protein folding pathway. Until now,
comparatively little is known about the changes in the conformational
dynamics in folding intermediates of proteins that contain only a
subset of their native disulfide bonds. In this comprehensive study,
we probe the conformational landscape of non-native states of lysozyme
containing a single native disulfide bond utilizing nuclear magnetic
resonance (NMR) spectroscopy, small-angle X-ray scattering (SAXS),
circular dichroism (CD) data, and modeling approaches. The impact
on conformational dynamics varies widely depending on the loop size
of the single disulfide variants and deviates significantly from random
coil predictions for both NMR and SAXS data. From these experiments,
we conclude that the introduction of single disulfides spanning a
large portion of the polypeptide chain shifts the structure and dynamics
of hydrophobic core residues of the protein so that these regions
exhibit levels of order comparable to the native state on the nanosecond
time scale
Modulation of Structure and Dynamics by Disulfide Bond Formation in Unfolded States
During oxidative folding, the formation of disulfide
bonds has
profound effects on guiding the protein folding pathway. Until now,
comparatively little is known about the changes in the conformational
dynamics in folding intermediates of proteins that contain only a
subset of their native disulfide bonds. In this comprehensive study,
we probe the conformational landscape of non-native states of lysozyme
containing a single native disulfide bond utilizing nuclear magnetic
resonance (NMR) spectroscopy, small-angle X-ray scattering (SAXS),
circular dichroism (CD) data, and modeling approaches. The impact
on conformational dynamics varies widely depending on the loop size
of the single disulfide variants and deviates significantly from random
coil predictions for both NMR and SAXS data. From these experiments,
we conclude that the introduction of single disulfides spanning a
large portion of the polypeptide chain shifts the structure and dynamics
of hydrophobic core residues of the protein so that these regions
exhibit levels of order comparable to the native state on the nanosecond
time scale
Modulation of Structure and Dynamics by Disulfide Bond Formation in Unfolded States
During oxidative folding, the formation of disulfide
bonds has
profound effects on guiding the protein folding pathway. Until now,
comparatively little is known about the changes in the conformational
dynamics in folding intermediates of proteins that contain only a
subset of their native disulfide bonds. In this comprehensive study,
we probe the conformational landscape of non-native states of lysozyme
containing a single native disulfide bond utilizing nuclear magnetic
resonance (NMR) spectroscopy, small-angle X-ray scattering (SAXS),
circular dichroism (CD) data, and modeling approaches. The impact
on conformational dynamics varies widely depending on the loop size
of the single disulfide variants and deviates significantly from random
coil predictions for both NMR and SAXS data. From these experiments,
we conclude that the introduction of single disulfides spanning a
large portion of the polypeptide chain shifts the structure and dynamics
of hydrophobic core residues of the protein so that these regions
exhibit levels of order comparable to the native state on the nanosecond
time scale