{"id":21657,"date":"2023-09-14T10:48:34","date_gmt":"2023-09-14T14:48:34","guid":{"rendered":"http:\/\/www.bumc.bu.edu\/ppb\/?page_id=21657"},"modified":"2023-12-04T11:21:25","modified_gmt":"2023-12-04T16:21:25","slug":"the-mcknight-lab","status":"publish","type":"page","link":"https:\/\/www.bumc.bu.edu\/ppb\/the-mcknight-lab\/","title":{"rendered":"The McKnight Lab"},"content":{"rendered":"<h4 style=\"text-align: left;\"><a href=\"https:\/\/www.bumc.bu.edu\/ppb\/nmr-spectroscopy-lab\/\">Director, BUSM Core Facility for Structural NMR<\/a><\/h4>\n<h4><a id=\"research\" name=\"research\"><\/a>Research<\/h4>\n<figure id=\"attachment_20957\" aria-describedby=\"caption-attachment-20957\" style=\"width: 660px\" class=\"wp-caption aligncenter\"><img loading=\"lazy\" src=\"\/ppb\/files\/2023\/06\/cjm_hp35-650x581-1.png\" alt=\"\" width=\"650\" height=\"581\" class=\"wp-image-20957 size-full\" srcset=\"https:\/\/www.bumc.bu.edu\/ppb\/files\/2023\/06\/cjm_hp35-650x581-1.png 650w, https:\/\/www.bumc.bu.edu\/ppb\/files\/2023\/06\/cjm_hp35-650x581-1-336x300.png 336w\" sizes=\"(max-width: 650px) 100vw, 650px\" \/><figcaption id=\"caption-attachment-20957\" class=\"wp-caption-text\"><strong>The 35-residue villin headpiece subdomain, HP35. The sidechains of buried hydrophobic residues are shown as spheres. Other side chains are shown as sticks and colored by atom.<\/strong><\/figcaption><\/figure>\n<h5><\/h5>\n<p style=\"text-align: justify;\"><br style=\"clear: both;\" \/>The McKnight lab is interested in the folding, function and dynamics of proteins. A long-time favorite model system is the actin-binding \u201cheadpiece\u201d domain of the protein villin. The villin headpiece contains a subdomain of only 35-residues that folds to form a novel three helix structure (HP35). HP35 is one of the shortest amino acid sequences that folds to a monomeric native state in the absence of disulfide bonds or bound metals\/ligands. We use NMR, circular dichroism spectroscopy, and other methods, to investigate the stability and motions of proteins using the unique HP35 domain as well as other small protein domains.<\/p>\n<h4><a id=\"publications\" name=\"publications\"><\/a><strong>Recent Publications<\/strong><\/h4>\n<p><a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/?term=mcknight%2Bcj%5Bauthor%5D\">Full list of publications on PubMed<\/a><\/p>\n<p>Vugmeyster, L., Rodgers, A, Ostrovsky, D, McKnight, C.J. &amp; Fu, R. Deuteron off-resonance rotating frame relaxation for the characterization of slow motions in rotating and static solid-state proteins, Journal of Magnetic Resonance. 2023. 352, 107493:1-13. PMID: 37271094<\/p>\n<p>Vugmeyster L, Nichols PJ, Ostrovsky D, McKnight CJ, V\u00f6geli B, Slow methyl axes motions in perdeuterated villin headpiece subdomain probed by cross-correlated NMR relaxation measurements. Magnetochemistry. 2023. 9, 33:1-15. PMC9910280<\/p>\n<p>Nichols PJ, Falconer I, Griffin A, Mant C, Hodges R, McKnight CJ, V\u00f6geli B, Vugmeyster L. Deuteration of nonexchangeable protons on proteins affects their thermal stability, side-chain dynamics, and hydrophobicity. Protein Sci. 2020 07; 29(7):1641-1654. PMID: 32356390.<\/p>\n<p>Vugmeyster L, Griffin A, Ostrovsky D, Bhattacharya S, Nichols PJ, McKnight CJ, V\u00f6geli B. Correlated motions of C&#8217;-N and Ca-C\u00df pairs in protonated and per-deuterated GB3. J Biomol NMR. 2018 Oct; 72(1-2):39-54. PMID: 30121872.<\/p>\n<p>Miears HL, Gruber DR, Horvath NM, Antos JM, Young J, Sigurjonsson JP, Klem ML, Rosenkranz EA, Okon M, McKnight CJ, Vugmeyster L, Smirnov SL. Plant Villin Headpiece Domain Demonstrates a Novel Surface Charge Pattern and High Affinity for F-Actin. Biochemistry. 2018 03 20; 57(11):1690-1701. PMID: 29444403.<\/p>\n<p>Xiao R, Dane EL, Zeng J, McKnight CJ, Grinstaff MW. Synthesis of Altrose Poly-amido-saccharides with \u00df-N-(1&gt;2)-d-amide Linkages: A Right-Handed Helical Conformation Engineered in at the Monomer Level. J Am Chem Soc. 2017 10 11; 139(40):14217-14223. PMID: 28902504.<\/p>\n<p>Falconer IB, Mant CT, McKnight CJ, Vugmeyster L, Hodges R. Optimized purification of a fusion protein by reversed-phase high performance liquid chromatography informed by the linear solvent strength model. J Chromatogr A. 2017 Oct 27; 1521:44-52. PMID: 28942999.<\/p>\n<p>Chin SL, Lu Q, Dane EL, Dominguez L, McKnight CJ, Straub JE, Grinstaff MW. Combined Molecular Dynamics Simulations and Experimental Studies of the Structure and Dynamics of Poly-Amido-Saccharides. J Am Chem Soc. 2016 05 25; 138(20):6532-40. PMID: 27119983.<\/p>\n<p>Harpole KW, O&#8217;Brien ES, Clark MA, McKnight CJ, Vugmeyster L, Wand AJ. The unusual internal motion of the villin headpiece subdomain. Protein Sci. 2016 Feb; 25(2):423-32. PMID: 26473993.<\/p>\n<p>Raina D, Agarwal P, Lee J, Bharti A, McKnight CJ, Sharma P, Kharbanda S, Kufe D. Characterization of the MUC1-C Cytoplasmic Domain as a Cancer Target. PLoS One. 2015; 10(8):e0135156. PMID: 26267657.<\/p>\n<p>Chen L, Brown JW, Mok YF, Hatters DM, McKnight CJ. The allosteric mechanism induced by protein kinase A (PKA) phosphorylation of dematin (band 4.9). J Biol Chem. 2015 Jul 17; 290(29):17808. PMID: 26188045.<\/p>\n<p>Brown JW, Bullitt E, Sriswasdi S, Harper S, Speicher DW, McKnight CJ. The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap. PLoS Comput Biol. 2015 Jun; 11(6):e1004302. PMID: 26067675.<\/p>\n<h4>Links<\/h4>\n<p><a href=\"https:\/\/profiles.bu.edu\/C.McKnight\">BU Profile<\/a><br \/>\n<a href=\"https:\/\/www.researchgate.net\/profile\/Christopher-Mcknight-2\">ResearchGate<\/a><br \/>\n<a href=\"https:\/\/www.linkedin.com\/in\/christopher-james-mcknight-bbb7a69\/\">LinkedIn<\/a><br \/>\n<a href=\"https:\/\/www.bumc.bu.edu\/ppb\/nmr-spectroscopy-lab\/\">Facility for Structural NMR<\/a><\/p>\n<h4><a id=\"contact\" name=\"contact\"><\/a>Contact Us<\/h4>\n<p>Department of Pharmacology, Physiology &amp; Biophysics<br \/>\nChobanian &amp; Avedisian School of Medicine<br \/>\n72 East Concord Street, L317<br \/>\nBoston MA 02118-2526<\/p>\n<p>Phone: (617) 358-9553<br \/>\ne-mail: <a href=\"mailto:cjmck@bu.edu\">cjmck@bu.edu<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Director, BUSM Core Facility for Structural NMR Research The McKnight lab is interested in the folding, function and dynamics of proteins. A long-time favorite model system is the actin-binding \u201cheadpiece\u201d domain of the protein villin. The villin headpiece contains a subdomain of only 35-residues that folds to form a novel three helix structure (HP35). HP35 [&hellip;]<\/p>\n","protected":false},"author":1811,"featured_media":0,"parent":0,"menu_order":47,"comment_status":"closed","ping_status":"closed","template":"page-templates\/no-sidebars.php","meta":[],"_links":{"self":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages\/21657"}],"collection":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/users\/1811"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/comments?post=21657"}],"version-history":[{"count":7,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages\/21657\/revisions"}],"predecessor-version":[{"id":22539,"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/pages\/21657\/revisions\/22539"}],"wp:attachment":[{"href":"https:\/\/www.bumc.bu.edu\/ppb\/wp-json\/wp\/v2\/media?parent=21657"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}