Charles L. Brooks
| |
Professor (Adjunct)
(primary appointment in the Department of Veterinary Biosciences)
Phone: 614-292-9641
Fax: 614-292-9641
email: brooks.8@osu.edu
Webpage: None |
Research Interests:
The focus of Dr. Brooks' research is to identify and understand the
function of structural motifs that participate in initiating changes
in protein conformation and function. The mechanisms by which molecules
rearrange their constituent atoms and modulate their functions are not
well understood. Does each protein have a unique mechanisms to alter
its shape, or are there a discrete number of recognizable motifs/mechanisms
that are used in various proteins to alter shape and thereby modulate
function? Both post-translational modifications or protein/protein interactions
can initiate conformation changes that regulate function. Numerous post-translational
modifications affect protein shape and function, including: metal prosthetic
groups (such as zinc- binding in lactogenic hormones or calcium-binding
in calmodulin or alpha-lactalbumin), or phosphorylation (such as phosphorylation
of casein, prolactin, growth hormone or calmodulin). The binding of
hormones and receptors are protein/protein interacts that may induce
conformation changes that modulate function. The amino acids in proteins
that are directly affected by these interactions and pot translational
modifications have not been identified in most proteins and common motifs
that contain such residues have not been classified.
The mechanism by which local conformation changes are initiated and
transmitted to distal structural elements need to be identified. This
information is required in order to engineer enzymes for industrial
applications that may be regulated, design peptides and proteins with
pharmaceutical applications, understand the basis of diseases that are
associated with mutations and loss of functional regulation, and to
understand the relationship of conserved protein structures during the
evolution of species.
Currently, three groups of proteins are being investigated: somatotropic
and lactogenic hormones (functional motifs: protein/receptor binding,
zinc-binding and phosphorylation), alpha-lactalbumin (calcium-binding
and zinc-binding) and calmodulin (phosphorylation and calcium binding).
Publications
Selected publications from the last 5 years:
Pemlykov, S.E., Veprintsev, D.B., Brooks, C.L., Permykov, E.A. and
Berliner, L.J. Bovine alpha-lactalbumin: Searching for the Strong Zinc-binding
Site. Proteins: Structure, Function and Genetics 40: 106-111 (2000).
Peterson, F.C. and Brooks, C.L. The Species Specificity of Growth Hormone
Requires the Cooperative Interaction of Two Motifs. FEBS Letters 3.1276-282
(2000).
Veprintsev, D.B., Naryan, M, Perrnyakov, S.E., Uversky, V.N., Brooks,
C.L., Cherskaya, A.M., Perrnyakov, E.A. and Berliner, L.J. Fine Tuning
the N-terrninus of a Calcium Binding Protein alpha-lactalbumin. Proteins:
Structure, Function and Genetics 31: 65-72 (1999).
Wicks, J .R. and Brooks, C.L. Growth Hormone Kinase Activity in Bovine
Anterior Pituitary Subcellular Fractions. Endocrine 10: 77-82 (1999).
Duda, K.M. and Brooks, C.L. Human Growth Hormone Site 2 Lactogenic
Activity Requires a Distant Tyrosine 164. FEBS Letters, 442: 120-124
(1999).
Peterson, F.C. Anderson, P.l., Berliner, L.l. and Brooks,
C.L. Efficient
Expression, Folding and Characterization of Small Molecular Weight Proteins
with a pT7-7 -derived Phagemid. Protein Expression and Purification,
15: 16-23 (1999).
Wicks, J .R. and Brooks, C.L. Prolactin Kinase Activity in Bovine Anterior
Pituitary Subcellular Fractions. Molec. Cell. Endo. 141: 125-132 (1999).
Brooks, C.L. and Saiduddin, S. Phosphorylation of Bovine Prolactin
Eliminates Luteotrophic Activity in the Rat. Life Sciences 63: 1281-1287
(1998).
Anderson, P .J. , Brooks, C.L and L.1. Berliner. Functional Identification
of Calcium Binding Residues in Bovine alpha-Lactalbumin. Biochemistry
16: 11648-11643 (1997).
Peterson, F.C. and Brooks, C.L. Identification of a Lactogenic Motif
in Human Growth Hormone. Journal of Biological Chemistry 212: 21444-21448
(1997).
Permyakov, E.A., D.B. Veprintsev, G.Y. Deikus, S.E. Permyakov, L.P.
Kalinichenko, V.M. Grishchenko and Brooks, C.L. pH-Induced Transition
and Zn2+-binding Properties of Bovine Prolactin. FEBS Letters 405: 273-276
(1997).
Frazer, G.S., D.M. Bucci and Brooks, C.L. Two-Dimensional Polyacrylamide
Gel Electrophoresis of Bovine Semen After Cryopreservation in Half Milliliter
Straws. Theriogenology 46: 1103-1115 (1996).
Schenck, P.A., D.J. Chew, and Brooks, C.L. Effects of Storage on Serum
Ionized Calcium and pH from Horses with Normal and Abnormal Ionized
Calcium. Veterinary Clinical Pathology 25: 118-120 (1996).
Oglesbee, M. , Z. Liu, H. Kenney and Brooks, C.L. The Highly Inducible
Member of the 70kDa Family of Heat Shock Proteins Increases Canine Distemper
Virus Polymerase Activity. Journal General Virology 77: 2125-2135 (1996).
Schenck, P.A., D.J. Chew, and Brooks, C.L.
Fractionation of Canine Serum Calcium Using a Micropartition System.
American Journal of Veterinary Research 57: 268-271 (1996).
Maceijewski, P .M. , F .C. Peterson, P .J . Anderson, and Brooks,
C.L.
Mutation of Serine 90 to Glutamic Acid Mimics Phosphorylation of Bovine
Prolactin. Journal of Biological Chemistry 210: 27661-27665 (1995).
Wicks, J .R. and Brooks, C.L. Biological Activity of Phosphorylated
and Dephosphorylated Bovine Prolactin. Molecular and Cellular Endocrinology
112: 223-229 (1995).
Latendresse, J.R., Brooks, C.L, and C.C. Capen. Toxic Effects of Butylated
Triphenyl Phosphate-based Hydraulic Fluid and Tricrencyl Phosphate in
Female F344 rats. Veterinary Pathology 32: 394-402 (1995).
Schenck, P.A., D.J. Chew, and Brooks, C.L. Effects of Storage on Serum
Ionized Calcium and pH values in Clinically Normal Dogs. American Journal
of Veterinary Research 56 (3), 304-307 (1995).
