{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T14:25:55Z","timestamp":1787063155992,"version":"build-2736575974"},"reference-count":38,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2010,11,29]],"date-time":"2010-11-29T00:00:00Z","timestamp":1290988800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2011,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The oligomerization and\/or aggregation of proteins is of critical importance in a wide variety of biomedical situations, ranging from abnormal disease states like Alzheimer's and Parkinson's disease to the production of inclusion bodies, stability, and delivery of protein drugs. In the case of eye\u2010lens proteins, oligomerization is implicated in cataract formation. In the present study, we have investigated the temperature driven oligomerization of M\u2010crystallin, a close homologue of eye\u2010lens proteins, using NMR spectroscopy and dynamic\u2010light scattering (DLS). The NMR data primarily included\n                    <jats:italic>R<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    ,\n                    <jats:italic>R<\/jats:italic>\n                    <jats:sub>2<\/jats:sub>\n                    relaxation rates and nOes of the backbone amide groups recorded at three different temperatures, 25, 20, and 15\u00b0 C. The major outcome of the study is the two fold increase in the overall tumbling time (\u03c4\n                    <jats:sub>c<\/jats:sub>\n                    ) of M\u2010crystallin on lowering the temperature from 25 to 15\u00b0 C. An extrapolation of \u03c4\n                    <jats:sub>c<\/jats:sub>\n                    to a further lower temperature (5\u00b0 C) may lead to a \u03c4\n                    <jats:sub>c<\/jats:sub>\n                    of \u223c19 ns that would correspond to a \u03c4\n                    <jats:sub>c<\/jats:sub>\n                    value of a tetrameric M\u2010crystallin. These results also validate the observed changes in the hydrodynamic radius of M\u2010crystallin, determined using DLS data. Further, the temperature\u2010dependent protein dynamics of M\u2010crystallin reveal considerable variation at\/near the Ca\n                    <jats:sup>2+<\/jats:sup>\n                    \u2010binding sites. A concerted analysis of the temperature dependent relaxation parameters and DLS data reveals that the self\u2010association of the protein is not only a monomer\u2010dimer equilibrium, but also goes to tetramers or other multimeric states. These higher states may co\u2010exist in fast exchange with the monomeric and dimeric M\u2010crystallin at milli\u2010molar to sub\u2010millimolar concentrations and at lower temperature. Proteins 2011. \u00a9 2010 Wiley\u2010Liss, Inc.\n                  <\/jats:p>","DOI":"10.1002\/prot.22905","type":"journal-article","created":{"date-parts":[[2010,10,11]],"date-time":"2010-10-11T16:26:54Z","timestamp":1286814414000},"page":"569-580","source":"Crossref","is-referenced-by-count":7,"title":["Temperature\u2010dependent oligomerization in M\u2010crystallin: Lead or lag toward cataract, an NMR perspective"],"prefix":"10.1002","volume":"79","author":[{"given":"Ravi P.","family":"Barnwal","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K. Manjula","family":"Devi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geetika","family":"Agarwal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yogendra","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kandala V. 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