References

i.      Mande, Shekhar C.  "Crystal structure of recombinant human
                 triosephosphate isomerase at 2.8 A resolution.  TIM related
                 human genetic disorders and comparison with the trypanosomal
                 enzyme."  Protein Science May 1994:  810-820.

ii.     Knowles, J. R. and Albery, W. J.  "Evolution of enzyme function
                 and the development of catalytic efficiency."  Biochemistry
                 vol. 15 Nov. 1976:  5631-5639.

iii.     Knowles, J. R. and Albery, W. J.  "Perfection in enzyme catalysis:
                  The energetics of TIM."  Accounts of Chemical Research vol. 10
                  Apr. 1977:  105-111.

iv.     Radha, K.V.  "Comparison of the structures and the crystal contacts
                  of trypanosomal TIM in four different crystal forms."  Protein
                  Science May 1994:  779-786.

v.       http://www.jbc.org/cgi/content/full/271/17/10010#f1

vi.      http://www.chem.sunysb.edu/faculty/sampson/link3.html

vii.     http://www.biochem.ucl.ac.uk/bsm/pdbsum/3tim/main.html

viii.     Harris, T. K.   "NMR studies of the roll of hydrogen bonding in the
                   mechanism of TIM."  Biochemistry vol. 48 1997:  14661-14674.

ix.      Williams, J. C. and McDermott, A. E.  "Dynamics of the flexible loop
                  of TIM:  The loop motion is not ligand gated."  Biochemistry vol.
                  34 1995:  8309-8318.m

x.       Joseph, D. ;  Petsko, G. A. ; and Karplus, M.  "Anatomy of a
                   conformational change:  Hinged 'lid' motion of the TIM loop."
                   Science vol. 249 Sept. 1990:  1425-1428.



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Created by Jason Hadrath
hadratjm@UWEC.edu
Student of Dr. W. Gallagher
at the University of Wisconsin at Eau Claire
Chemistry Department


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