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Water permeability of chloroplast envelope membranes
1985
FEBS Letters
Preserved Fulltext
previously [l] . ...
Table 1 1 Results of relaxation time and saturation transfer measurements of 8 L. tdipifera samples at 20°C. ...
., the time required for a water molecule to diffuse a distance half the mean diameter of a chloroplast [l] . ...
doi:10.1016/0014-5793(85)80809-7
pmid:3987894
fatcat:qdyprxswpzahhjp7w6phcvqobq
Databases and Software for NMR-Based Metabolomics
2012
Current Metabolomics
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L-alanine as an example of an interactive 1 H-NMR session in the MQMCD. ...
, specific information acquired from the literature and other databases such as tissue location, average concentrations and associated disorders (for an example of this compilation of information for L-alanine ...
doi:10.2174/2213235x11301010028
pmid:24260723
pmcid:PMC3832261
fatcat:umhinkhvavfsjeyhkpqylbjnly
Biomolecular NMR: Past and future
2017
Archives of Biochemistry and Biophysics
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We thank Eldon L. Ulrich for critical comments on the manuscript and the National Institutes of Health for continuous support over 46 years. ...
Bill Horsely, who worked with John Markley, is sitting at the NMR spectrometer. ...
Our early experience with NMR John Markley grew up in Colorado and was a chemistry major and member of the ski team at Carleton College (Northfield, Minnesota). ...
doi:10.1016/j.abb.2017.05.003
pmid:28495511
pmcid:PMC5701516
fatcat:2aw6oo3wcfa3peq3prb76ananq
Nuclear Magnetic Resonance Studies of Spherical Plant Viruses
1986
Biophysical Journal
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VIRUDACHALAM AND JOHN L. MARKLEY
Department ofBiochemistry, University of Wisconsin at Madison, Madison, Wisconsin 53706. ...
L. Markley, unpublished results; see reference 1.)
Sauer, R. T., and R. Anderegg. 1978. Primary structure of the X repressor. Biochemistry. 17:1092-1100. 8. Shih, H. H.-L., J. Brady, and M. ...
doi:10.1016/s0006-3495(86)83582-2
pmid:19431638
pmcid:PMC1329566
fatcat:b5kbpsozyjcflaxwcfasezzahy
Sliding mode control using modified Rodrigues parameters
1996
Journal of Guidance Control and Dynamics
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Solution structure of human sorting nexin 22
2007
Protein Science
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The sorting nexins (SNXs) constitute a large group of PX domain-containing proteins that play critical roles in protein trafficking. We report here the solution structure of human sorting nexin 22 (SNX22). Although SNX22 has <30% sequence identity with any PX domain protein of known structure, it was found to contain the a/b fold and compact structural core characteristic of PX domains. Analysis of the backbone dynamics of SNX22 by NMR relaxation measurements revealed that the two walls of the
doi:10.1110/ps.072752407
pmid:17400918
pmcid:PMC2206652
fatcat:5i35wn3tbndu3diflefxhjmgmi
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... igand binding cleft undergo internal motions: on the picosecond timescale for the b1/b2 loop and on the micro-to millisecond timescale for the loop between the polyproline motif and helix a2. Regions of the SNX22 structure that differ from those of other PX domains include the loop connecting strands b1 and b2 and the loop connecting helices a1 and a2, which appear to be more mobile than corresponding loops in other known structures. The interaction of dibutanoyl-phosphatidylinositol-3-phosphate (dibutanoyl-PtdIns(3)P) with SNX22 was investigated by an NMR titration experiment, which identified the binding site in a basic cleft and indicated that ligand binding leads only to a local structural rearrangement as has been found with other PX domains. Because motions in the loops are damped out when dibutanoyl-PtdIns(3)P binds, entropic effects could contribute to the lower affinity of SNX22 for this ligand compared to other PX domains.
NMR Solution Structure of ATTp, anArabidopsis thalianaTrypsin Inhibitor†,‡
2002
Biochemistry
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L. Markley, manuscript in preparation) . ...
L. Markley, manuscript in preparation). ...
doi:10.1021/bi025702a
pmid:12369816
fatcat:w3zaptk5tngtlpldum7ukyui5m
High Pressure Effects on Protein Structure
[chapter]
1998
Protein Dynamics, Function, and Design
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L. Markley, unpublished). ...
L. Markley, unpublished). ...
doi:10.1007/978-1-4615-4895-9_5
fatcat:fvb6a7ke5jbshopj6vxdwcsrqe
The future of the protein data bank
2012
Biopolymers
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The Worldwide Protein Data Bank (wwPDB) is the international collaboration that manages the deposition, processing and distribution of the PDB archive. The wwPDB's mission is to maintain a single archive of macromolecular structural data that are freely and publicly available to the global community. Its members [RCSB PDB (USA), PDBe (Europe), PDBj (Japan), and BMRB (USA)] host data-deposition sites and mirror the PDB ftp archive. To support future developments in structural biology, the wwPDB
doi:10.1002/bip.22132
pmid:23023942
pmcid:PMC3684242
fatcat:tkdo6ykibnhebfbavqjb55nhsq
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... artners are addressing organizational, scientific, and technical challenges.
Coupling betweentrans/cisproline isomerization and protein stability in staphylococcal nuclease
1996
Protein Science
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In both P117G mutants, the loop formed by residues 112-1 17 is located closer to the adjacent loop formed by residues 77-85, and residues 115-1 18 adopt a type I' p-turn conformation with the L y~"~-G ...
l y "~ peptide bond in the trans configuration, as compared with the parent protein in which these residues have a typeVI, p-turn conformation with the Ly~"~-Pro'" peptide bond in the cis configuration ...
As expected, H124L+P1 17G exhibits only one peptide bond configuration at L y~l '~-P r o l '~ , but maintains heterogeneity at the peptide bond. ...
doi:10.1002/pro.5560050917
pmid:8880915
pmcid:PMC2143535
fatcat:xhzgbbyh25d3noculexxb32sgi
Predictive Filtering for Nonlinear Systems
1997
Journal of Guidance Control and Dynamics
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, , , , 1 2 (7) S x t m q ∈ × R is a matrix with each i th row given by s L L c L L c i m i g f p i g f p i i q i = = − − 1 1 1 1 2 , , , , , , (8) where the Lie derivative with respect to L g j in Equation ...
L t Q L y z f f f ≤ − + + − − + − − 2 4 4 1 2 2 2 2 2 ξ ξ ∆ ∆ (43) Substituting 4 1 z Q = − ξ leads to V Q V b ≤ − + − ξ 1 (44) where b Q y L L t Q L y f f f ≡ − − + − −1 2 2 2 2 1 ξ ξ ∆ ∆ (45)
Numerical ...
doi:10.2514/2.4078
fatcat:6qnpa4fycfaxnmtt6zmggo5fhm
Safeguarding the integrity of protein archive
2010
Nature
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Biophysical characterization of α-synuclein and its controversial structure
2013
Intrinsically Disordered Proteins
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In the crowded intracellular environment (~400 g of macromolecules/L), folded globular proteins experience the increased viscosity of the bacterial cytoplasm, which greatly affects rotational diffusion ...
doi:10.4161/idp.26255
pmid:24634806
pmcid:PMC3908606
fatcat:pnqfye3mvbfcdaj24tjcs6rlmq
Solution Structure and Backbone Dynamics of Component IVGlycera dibranchiataMonomeric Hemoglobin−CO†,‡
1998
Biochemistry
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73
-70
+60
16
H 72 -L 73
+60
+70
13
H 97 -I 98
+60
-70
22
H 97 -I 98
-80
+60
7
G 119 -G 120
-30
+120
24
G 119 -G 120
+110
-120
5
a
Table 4 : 4 Average Values for S 2 , Backbone ...
structures. b Number of structures out of 29 that contain the conformational subpopulation specified by ψi and φi+1. the 15 N-1 H HSQC spectrum prevented the determination of residues
ψi
φi+1
n b
H 72 -L ...
doi:10.1021/bi980810b
pmid:9692983
fatcat:a7sztpbb2fbl3pu4h4bs4lrqa4
PINE-SPARKY.2 for automated NMR-based protein structure research
2017
Bioinformatics
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Nuclear magnetic resonance (NMR) spectroscopy, along with X-ray crystallography and cryoelectron microscopy, is one of the three major tools that enable the determination of atomiclevel structural models of biological macromolecules. Of these, NMR has the unique ability to follow important processes in solution, including conformational changes, internal dynamics and protein-ligand interactions. As a means for facilitating the handling and analysis of spectra involved in these types of NMR
doi:10.1093/bioinformatics/btx785
pmid:29281006
pmcid:PMC5925765
fatcat:xxagdsyjarad7a577o2d34gsii
more »
... es, we have developed PINE-SPARKY.2, a software package that integrates and automates discrete tasks that previously required interaction with separate software packages. The graphical user interface of PINE-SPARKY.2 simplifies chemical shift assignment and verification, automated detection of secondary structural elements, predictions of flexibility and hydrophobic cores, and calculation of three-dimensional structural models. Availability and implementation: PINE-SPARKY.2 is available in the latest version of NMRFAM-SPARKY from the National Magnetic Resonance Facility at Madison (http://pine.nmrfam.wisc.edu/ download_packages.html), the NMRbox Project (https://nmrbox.org) and to subscribers to the SBGrid (https://sbgrid.org). For a detailed description of the program, see http://www.nmrfam.wisc. edu/pine-sparky2.htm.
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