scholarly journals Ergodic pumping: A mechanism to drive biomolecular conformation changes

2006 ◽  
Vol 216 (1) ◽  
pp. 220-234 ◽  
Author(s):  
R.S. MacKay ◽  
D.J.C. MacKay
Keyword(s):  
Conformation Changes ◽  
Biomolecular Conformation

Kategorisierung der Schädelform des Cavalier King Charles Spaniels

2019 ◽  
Vol 47 (02) ◽  
pp. 133-133
Keyword(s):  
Pilot Study ◽  
Cavalier King Charles Spaniel ◽  
Conformation Changes ◽  
Veterinary Record ◽  
Changes Over Time ◽  
Over Time

Knowler SP, Gillstedt L, Mitchell TJ et al. Pilot study of head conformation changes over time in the Cavalier King Charles spaniel breed. Veterinary Record 2019. doi:10.1136/vr.105135.

scholarly journals Time-resolved detection of SDS-induced conformational changes in α-synuclein by a micro-stopped-flow system

RSC Advances ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 1086-1097
Author(s):  
Shunki Takaramoto ◽  
Yusuke Nakasone ◽  
Kei Sadakane ◽  
Shinsaku Maruta ◽  
Masahide Terazima
Keyword(s):  
Conformational Changes ◽  
Flow System ◽  
Stopped Flow ◽  
Time Resolved ◽  
Sds Micelles ◽  
Conformation Changes ◽  
System P

Dynamics of conformation changes of α-synuclein induced by the presence of SDS micelles are revealed using time-resolved diffusion, CD, and FRET measurements combined with a micro-stopped flow system.

scholarly journals Ligand-induced structural changes analysis of ribose-binding protein as studied by molecular dynamics simulations

2021 ◽  
pp. 1-12
Author(s):  
Haiyan Li ◽  
Zanxia Cao ◽  
Guodong Hu ◽  
Liling Zhao ◽  
Chunling Wang ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Structural Changes ◽  
Binding Protein ◽  
Network Models ◽  
Md Simulations ◽  
Protein Domain ◽  
Opening Angle ◽  
Conformation Changes ◽  
Wide Range ◽  
Ribose Binding Protein

BACKGROUND: The ribose-binding protein (RBP) from Escherichia coli is one of the representative structures of periplasmic binding proteins. Binding of ribose at the cleft between two domains causes a conformational change corresponding to a closure of two domains around the ligand. The RBP has been crystallized in the open and closed conformations. OBJECTIVE: With the complex trajectory as a control, our goal was to study the conformation changes induced by the detachment of the ligand, and the results have been revealed from two computational tools, MD simulations and elastic network models. METHODS: Molecular dynamics (MD) simulations were performed to study the conformation changes of RBP starting from the open-apo, closed-holo and closed-apo conformations. RESULTS: The evolution of the domain opening angle θ clearly indicates large structural changes. The simulations indicate that the closed states in the absence of ribose are inclined to transition to the open states and that ribose-free RBP exists in a wide range of conformations. The first three dominant principal motions derived from the closed-apo trajectories, consisting of rotating, bending and twisting motions, account for the major rearrangement of the domains from the closed to the open conformation. CONCLUSIONS: The motions showed a strong one-to-one correspondence with the slowest modes from our previous study of RBP with the anisotropic network model (ANM). The results obtained for RBP contribute to the generalization of robustness for protein domain motion studies using either the ANM or PCA for trajectories obtained from MD.

scholarly journals PSVIII-17 Assessment of conformational changes across three parities in sows

2020 ◽  
Vol 98 (Supplement_3) ◽  
pp. 221-222
Author(s):  
Melanie D Trenhaile-Grannemann ◽  
Ronald M Lewis ◽  
Stephen D Kachman ◽  
Kenneth J Stalder ◽  
Benny E Mote
Keyword(s):  
Body Size ◽  
Body Length ◽  
Conformational Changes ◽  
Repeated Measures ◽  
Fixed Effects ◽  
Random Effect ◽  
Joint Angles ◽  
Body Depth ◽  
Conformation Changes ◽  
Over Time

Abstract Conformation-based sow selection is performed prior to reaching mature size, yet little is known about how conformation changes as growth continues. To assess conformation changes, 9 conformational traits were objectively measured at 12 discrete time points between 112 d of age and parity 3 weaning on 622 sows in 5 cohorts. The 9 traits included 5 body size traits (body length, body depth at the shoulder and flank, and height at the shoulder and flank) and 4 joint angles (knee, hock, and front and rear pastern). Data were analyzed with a repeated measures model (SAS V 9.4) including cohort and time point as fixed effects, sire as a random effect, and heterogeneous compound symmetry as the covariance structure. Sire variance ranged from 0.16 (body depth shoulder) to 2.00 (body length) cm2 for body size traits and 2.28 (rear pastern) to 4.22 (front pastern) degrees2 for joint angles. Cohort had an effect on all traits (P < 0.05). All traits displayed changes over time (P < 0.001). Size traits increased between 112 d of age and parity 3 weaning (64.16 vs. 107.57 cm, 26.62 vs. 44.14 cm, 23.32 vs. 36.92 cm, 46.10 vs. 73.55 cm, 49.36 vs. 77.47 cm for body length, body depth shoulder and flank, and height shoulder and flank, respectively); however, they fluctuated within parity by increasing during gestation and decreasing at weaning. Knee angle decreased (164.12 vs. 150.72 degrees) while fluctuating within parity by decreasing in the second half of gestation and increasing after weaning. Front and rear pastern angles decreased over time (60.89 vs. 53.74 degrees and 64.64 vs. 55.50 degrees for front and rear pastern, respectively), while biologically negligible change was observed in hock angle (148.63 vs. 147.48 degrees). Sow conformation changes throughout life, and these changes may require consideration when making selection decisions.

Studies on calcium ion-induced conformation changes in the actin-tropomyosin-troponin system by fluorimetry

1974 ◽  
Vol 351 (2) ◽  
pp. 205-213 ◽  
Author(s):  
Takamitsu Sekine ◽  
Takao Ohyashiki ◽  
Minoru Machida ◽  
Yuichi Kanaoka
Keyword(s):  
Calcium Ion ◽  
Conformation Changes

Copper(II) complexes of peptide fragments of the prion protein. Conformation changes induced by copper(II) and the binding motif in C-terminal protein region

2004 ◽  
Vol 98 (1) ◽  
pp. 133-143 ◽  
Author(s):  
David R Brown ◽  
Valeria Guantieri ◽  
Giulia Grasso ◽  
Giuseppe Impellizzeri ◽  
Giuseppe Pappalardo ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Conformation ◽  
Binding Motif ◽  
Peptide Fragments ◽  
Terminal Protein ◽  
Conformation Changes

Space-filling models of kinase clefts and conformation changes

Science ◽  
1979 ◽  
Vol 204 (4391) ◽  
pp. 375-380 ◽  
Author(s):  
C. Anderson ◽  
F. Zucker ◽  
T. Steitz
Keyword(s):  
Space Filling ◽  
Conformation Changes
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