Examining kinesin processivity within a general gating framework
Kinesin-1 is a dimeric motor that transports cargo along microtubules, taking 8.2-nm steps in
a hand-over-hand fashion. The ATP hydrolysis cycles of its two heads are maintained out of …
a hand-over-hand fashion. The ATP hydrolysis cycles of its two heads are maintained out of …
The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5
JS Waitzman, AG Larson, JC Cochran, N Naber… - Biophysical journal, 2011 - cell.com
Eg5 is a homotetrameric kinesin-5 motor protein that generates outward force on the
overlapping, antiparallel microtubules (MTs) of the mitotic spindle. Upon binding an MT, an …
overlapping, antiparallel microtubules (MTs) of the mitotic spindle. Upon binding an MT, an …
Bound ion effects: Using machine learning method to study the kinesin Ncd's binding with microtubule
W Guo, D Du, H Zhang, JE Sanchez, S Sun, W Xu… - Biophysical journal, 2024 - cell.com
Drosophila Ncd proteins are motor proteins that play important roles in spindle organization.
Ncd and the tubulin dimer are highly charged. Thus, it is crucial to investigate Ncd-tubulin …
Ncd and the tubulin dimer are highly charged. Thus, it is crucial to investigate Ncd-tubulin …
Probing the Structural and Energetic Basis of Kinesin–Microtubule Binding Using Computational Alanine-Scanning Mutagenesis
Kinesin–microtubule (MT) binding plays a critical role in facilitating and regulating the motor
function of kinesins. To obtain a detailed structural and energetic picture of kinesin–MT …
function of kinesins. To obtain a detailed structural and energetic picture of kinesin–MT …
Thermodynamic effects of multiple protein conformations on stability and DNA binding
The side-chain conformations of amino acids in the hydrophobic core are important for
protein folding and function. A previous NMR study has shown that a mutant protein of …
protein folding and function. A previous NMR study has shown that a mutant protein of …
All-atom structural investigation of kinesin–microtubule complex constrained by high-quality cryo-electron-microscopy maps
In this study, we have performed a comprehensive structural investigation of three major
biochemical states of a kinesin complexed with microtubule under the constraint of high …
biochemical states of a kinesin complexed with microtubule under the constraint of high …
Phosphazenes
FF Stewart - 2015 - books.rsc.org
Phosphazene chemistry continues to expand in its breadth and application. This article
discusses new research published in 2013 covering mono-and dimeric structures …
discusses new research published in 2013 covering mono-and dimeric structures …
Decrypting the structural, dynamic, and energetic basis of a monomeric kinesin interacting with a tubulin dimer in three ATPase states by all-atom molecular dynamics …
S Chakraborty, W Zheng - Biochemistry, 2015 - ACS Publications
We have employed molecular dynamics (MD) simulation to investigate, with atomic details,
the structural dynamics and energetics of three major ATPase states (ADP, APO, and ATP …
the structural dynamics and energetics of three major ATPase states (ADP, APO, and ATP …
[图书][B] Molecular motors in bionanotechnology
K Firman, J Youell - 2013 - books.google.com
Biological molecular motors provide most cells with the dynamic systems required for their
day-to-day existence. Examples occur in even the simplest organism (eg a bacteria virus) …
day-to-day existence. Examples occur in even the simplest organism (eg a bacteria virus) …
Plant kinesin-like calmodulin binding protein employs its regulatory domain for dimerization
MV Vinogradova, GG Malanina, JS Waitzman… - PLoS …, 2013 - journals.plos.org
Kinesin-like calmodulin binding protein (KCBP), a Kinesin-14 family motor protein, is
involved in the structural organization of microtubules during mitosis and trichome …
involved in the structural organization of microtubules during mitosis and trichome …