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#0 dbbase_sql->halt(Invalid SQL: select * from kra_comment where pid='82688' and iffb='1' order by id limit 0,10) called at [E:\phpweb\phpwebsite\1011kra\63965966\includes\] #1 dbbase_sql->query(select * from {P}_comment where pid='82688' and iffb='1' order by id limit 0,10) called at [E:\phpweb\phpwebsite\1011kra\63965966\comment\module\CommentContent.php:167] #2 CommentContent() called at [E:\phpweb\phpwebsite\1011kra\63965966\includes\] #3 printpage() called at [E:\phpweb\phpwebsite\1011kra\63965966\comment\html\index.php:13] 留言点评--晋红兵
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发布于:2019-7-3 15:53:08  访问:27 次 回复:0 篇
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Liu Y, Borbat P, Zweier JL, Freed JH, Hubbell WL. Pulsed
Measuring Cu2+-U0126-EtOH Purity & Documentation nitroxide distances applying double eNPe6 custom synthesis lectron lectron resonance and saturation restoration. Measuring Cu2+-nitroxide distances employing double electron lectron resonance and saturation restoration. Appl Magn Reson. 2012:ten. s00723-012-0422-x:1-12. The authors examine inter-spin distances among Cu+2 plus a nitroxide in a very peptide decided from T1 relaxometry (echo-detected saturation recovery) and static dipolar interactions (DEER), equally at small temperature. It‘s located the distances measured by relaxometry is usually predicted from the DEER distance distributions, and are strongly weighted toward the shortest distances. PubMed ID: Details from relaxometry and DEER attained at small temperature can in theory be when compared with relaxometry facts obtained with pulse SR at physiological temperatures to investigate the effect of freezing on structure. 53. Zhang Z, Fleissner MR, Tipikin DS, Liang Z, Moscicki JK, Earle KA, Hubbell WL, Freed JH. Multifrequency electron spin resonance review on the dynamics of spin labeled T4 lysozyme. J Phys Chem B. 2010; 114:5503?521. [PubMed: 20361789] 54. Nesmelov Y, Thomas D. Protein structural dynamics disclosed by site-directed spin labeling and multifrequency EPR. Biophys Rev. 2010; 2:91?nine. [PubMed: 21687819] 55. L ez CJ, Oga S, Hubbell WL. Mapping molecular versatility of proteins with site-directed spin labeling: a scenario analyze of myoglobin. Biochemistry. 2012; 51:6568?583. [PubMed: 22809279]NIH-PA Creator Manuscript NIH-PA Creator Manuscript NIH-PA Author ManuscriptCurr Opin Struct Biol. Writer manuscript; offered in PMC 2014 October 01.Hubbell et al.PageThis short article presents an extensive analyze in the holo-, PubMed ID: apo- as well as molten globule states of myoglobin that highlights the utility of continuous wave lineshape analysis combined with osmolyte perturbation and PD spectroscopy to recognize disordered locations, detect ns backbone fluctuation in requested sequences, and discover sequence-correlated conformational versatility about the microsecond and for a longer period time scales. Lineshape evaluation discovered a correlation among the speed and amplitude of R1 motion with extent of area packing (Determine 3a), which strongly supports a design wherein variation in R1 movement at floor web pages in requested helices reflects contributions from ns backbone fluctuations.Liu Y, Borbat P, Zweier JL, Freed JH, Hubbell WL. Pulsed ESR dipolar spectroscopy for length measurements in immobilized spin labeled proteins in liquid alternative. J Am Chem Soc. 2012; 134:9950?952. [PubMed: 22676043] ATAM radical is introduced as a novel spin label for proteins. Immobilization of a protein made up of two TAM facet chains on a strong aid prevented averaging of inter-spin dipolar interactions. Given the extended period memory time (Tm) of TAM, it had been then probable to evaluate inter-spin distances by using dipolar interactions at ambient alternatively when compared to the common cryogenic temperature working with PD spectroscopy (DQC). forty nine. J er H, Koch A, Maus V, Spiess HW, Jeschke G. Relaxation-based distance measurements involving a nitroxide and also a lanthanide spin label. J Magn Reson. 2008; 194:254?63. [PubMed: 18674941] fifty. Jun S, Becker JS, Yonkunas M, Coalson R, Saxena S. Unfolding of alanine-based peptides applying electron spin resonance length measurements. Biochemistry.
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