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Wand, A. Joshua Short, James Howard 2015-09-25T22:28:24Z 2015-09-25T22:28:24Z 10000-01-01 1998 1998 The interaction of apocalmodulin with a peptide (Neurop ) derived from the calmodulin-binding domain of the neural-specific protein neuromodulin has been studied by nuclear magnetic resonance (NMR). This complex is in fast exchange with its components on the NMR timescale, and the dissociation constant for the complex is in the micromolar range. This thesis presents the solution structure of the apoCaM. Neurop complex. The 1H, 13C, and 15N resonance assignments for the calmodulin and Neurop components of the complex were determined using multidimensional, multinuclear and triple resonance NMR methods. NOE-derived distance restraints and angular restraints were likewise determined. A total of 1910 intraprotein, 108 intrapeptide, and 18 protein-peptide NOEs were used to generate a family of structures. In addition, 217 torsional restraints and 68 hydrogen bond restraints were used to refine the final generated structures. A family of 48 refined structures was chosen for analysis on the basis of lowest energy and violations. The atomic r. m. s. d. for this family was 1.3 A for main chain atoms and 1.78 A for all heavy atoms. The average structure differs from other known calmodulin-peptide structures in possessing protein domains in which the hydrophobic surfaces normally involved in protein-peptide interactions are either not present (N-terminal domain) or are reduced in size (C-terminal domain). The result is a complex in which the peptide is loosely held by a pair of salt links, one to each domain of the protein, and hydrophobic interactions with the C-terminal domain. Made available in DSpace on 2015-09-25T22:28:24Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 9912378.pdf: 5283943 bytes, checksum: 4d43feff5b8a9168d9fa8741b9ee2de7 (MD5) Previous issue date: 1998 Embargo set by: Seth Robbins for item 86180 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 177 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998. http://hdl.handle.net/2142/84899 (MiAaPQ)AAI9912378 eng Chemistry, Biochemistry Solution Structure of the Apocalmodulin/neuro-P Complex text Biochemistry Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.