Karen N. Allen, PhD
Professor
Boston University College of Arts and Sciences
Dept of Chemistry

PhD, Brandeis University



Karen Allen investigates protein structure and function through X-ray diffraction and enzyme kinetic studies. Prior to joining the Department of Chemistry in 2008, she was Professor of Physiology and Biophysics at the Boston University School of Medicine. A leader in the American Chemical Society, she is currently an Associate Editor of the ACS journal, Biochemistry.

The Allen Research Group investigates the structure, function, and catalytic properties of enzymes. Their insights into these essential proteins guide the design of specialized molecules and enzymes to aid in drug discovery and in the development of tools that assist in protein studies. The Allen Group researchers conduct their studies using X-ray crystallography and spectroscopy, enzymology, and bioinformatics and routinely collaborate with leading laboratories at other universities.

Structure/Function/Catalytic Studies investigate the properties of specific enzymes in the haloalkanoic acid dehalogenase (HAD) Superfamily and the Hot Dog Thioesterase Superfamily. The HAD studies aim to develop an understanding of enzyme evolution. The Hot Dog thioestearse (found in eukaryotes, bacteria, and archea) studies focus on the biological functions of this pervasive domain (With the Dunaway-Mariano Group, University of New Mexico).

Drug Discovery Studies aim to develop inhibitors against the potent neurotoxin produced by the soil-dwelling bacterium Clostridium botulinum (BoNT). These inhibitors are crucial because these toxins have high potential for use in biological weapons (With the Tzipori Group, Tufts University).

Tool Discovery Studies develop multi-tasking, easy-to-use Lanthanide Binding Tags (LBTs). LBTs consist of 17 amino-acids which have minimal impact on the structures and functions of the proteins they help study (With the Imperiali Group, Massachusetts Institute of Technology).

Techniques & Resources include:

X-Ray Crystallography – the University runs a state-of-the-art X-ray crystallographic suite, including a rotating anode generator, with a CCD detector, capable of collecting data on both macro and small molecules. A dedicated X-Ray technician assists with data collection, processing, and troubleshooting.

The Crystal Farm - stores and visualizes 96-well trays of crystal, allowing automated tracking of crystal growth, remote viewing of crystals, optimized formulation of new crystal conditions, and enhanced temperature control.

Bioinformatics – lab utilizes the Scientific Computing and Visualization (SCV) supercomputers to create an approximation of the potential energy of molecules. These calculations are entered into CHARMM force fields in order to characterize the conformational changes of various members of the HAD superfamily.

Spectroscopy – lab performs Mass Spectrometry and CD Spectroscopy using CIC instrumentation.

Associate Professor
Boston University School of Medicine
Physiology & Biophysics




Collaborative research: Development of a platform enabling analysis of membrane protein interactions
08/01/2016 - 07/31/2018 (PI)
National Science Foundation
MCB-1614608

Trehalose-6-phosphate phosphatase inhibitors as anti-helminthics
09/12/2016 - 11/30/2017 (PI)
NIH/National Institute of Allergy & Infectious Diseases
1R21AI127623-01

A Multidisciplinary Approach for the Treatment of Botulinum Intoxication
08/26/2016 - 06/30/2017 (PI)
The Scripps Research Institute NIH NIAID
1R01AI19564-01A1

Molecular Mechanism of the NFkappaB Essential Modulator (NEMO) Scaffold Protein Mutated in Human Immunodeficiencies
08/15/2016 - 06/30/2017 (Co-PI)
PI: Adrian Whitty, PhD
NIH/National Institute of General Medical Sciences
1R01GM117350-01A1

Structure and Function of HAD Phosphatase Partners Dullard and Lipin
09/01/2012 - 05/31/2017 (PI)
NIH/National Institute of General Medical Sciences
5R01GM098760-04

COLLABORATIVE CENTER FOR AN ENZYME FUNCTION INITIATIVE
05/01/2010 - 04/30/2016 (PI)
University of Illinois NIH NIGMS
5U54GM093342-05

Trehalose-6-Phosphate Phosphatase: A Target for Anti-Onchocerciasis Therapeutics
01/18/2013 - 12/31/2015 (PI)
NIH/National Institute of Allergy & Infectious Diseases
5R21AI103484-02

PGT Inhibitors Mapped From A Tunicamycin Blueprint
02/01/2013 - 01/31/2015 (PI)
Massachusetts Institute of Technology NIH
1R21AI101807-01A1

MRI: Acquisition of Circular Dichroism (CD) Spectrometer
09/15/2011 - 08/31/2014 (PI)
National Science Foundation
CHE-1126545

Biochemical Studies of Oxalate Decarboxylase
07/01/2012 - 06/30/2014 (PI)
Trustees of Indiana University NIH
7R01DK061666-08

Showing 10 of 23 results. Show All Results



Yr Title Project-Sub Proj Pubs
2017 Trehalose-6-phosphate phosphatase inhibitors as anti-helminthics 1R21AI127623-01
2014 Trehalose-6-phosphate phosphatase: a target for anti-onchocerciasis therapeutics 5R21AI103484-02 1
2014 Structure and Function of HAD Phosphatase Partners Dullard and Lipin 5R01GM098760-03 2
2013 Trehalose-6-phosphate phosphatase: a target for anti-onchocerciasis therapeutics 1R21AI103484-01 1
2013 Structure and Function of HAD Phosphatase Partners Dullard and Lipin 5R01GM098760-02 2
2012 Structure and Function of HAD Phosphatase Partners Dullard and Lipin 1R01GM098760-01A1 2
2009 2-KETO-3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE PHOSPHATASE 5P41RR012408-13-7497 122
2009 STRUCTURE-FUNCTION DETEMINATION OF THE TYPE III HALOACID DEHALOGENASE (HAD) SUPE 5P41RR012408-13-7534 122
2009 Mechanisms and Function in HAD Phosphotransferases 7R01GM061099-09 27
2008 X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN A 2P41RR012408-12-7786 122
Showing 10 of 31 results. Show All Results
Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.

  1. Tararina MA, Janda KD, Allen KN. Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida. Biochemistry. 2016 Dec 06; 55(48):6595-6598. PMID: 27933790.
  2. Allen KN, Dunaway-Mariano D. Catalytic scaffolds for phosphoryl group transfer. Curr Opin Struct Biol. 2016 Dec; 41:172-179. PMID: 27526404; DOI: 10.1016/j.sbi.2016.07.017;.
  3. Zhu W, Easthon LM, Reinhardt LA, Tu C, Cohen SE, Silverman DN, Allen KN, Richards NG. Substrate Binding Mode and Molecular Basis of a Specificity Switch in Oxalate Decarboxylase. Biochemistry. 2016 Apr 12; 55(14):2163-73. PMID: 27014926; PMCID: PMC4854488; DOI: 10.1021/acs.biochem.6b00043;.
  4. Lukose V, Luo L, Kozakov D, Vajda S, Allen KN, Imperiali B. Conservation and Covariance in Small Bacterial Phosphoglycosyltransferases Identify the Functional Catalytic Core. Biochemistry. 2015 Dec 22; 54(50):7326-34. PMID: 26600273; DOI: 10.1021/acs.biochem.5b01086;.
  5. Rago F, Saltzberg D, Allen KN, Tolan DR. Enzyme Substrate Specificity Conferred by Distinct Conformational Pathways. J Am Chem Soc. 2015 Nov 4; 137(43):13876-86.View Related Profiles. PMID: 26440863; DOI: 10.1021/jacs.5b08149;.
  6. Barthelmes D, Gränz M, Barthelmes K, Allen KN, Imperiali B, Prisner T, Schwalbe H. Encoded loop-lanthanide-binding tags for long-range distance measurements in proteins by NMR and EPR spectroscopy. J Biomol NMR. 2015 Nov; 63(3):275-82. PMID: 26341230; DOI: 10.1007/s10858-015-9984-x;.
  7. Xia B, Mamonov A, Leysen S, Allen KN, Strelkov SV, Paschalidis ICh, Vajda S, Kozakov D. Accounting for observed small angle X-ray scattering profile in the protein-protein docking server ClusPro. J Comput Chem. 2015 Jul 30; 36(20):1568-72. PMID: 26095982; PMCID: PMC4485579; DOI: 10.1002/jcc.23952;.
  8. Kozakov D, Hall DR, Jehle S, Jehle S, Luo L, Ochiana SO, Jones EV, Pollastri M, Allen KN, Whitty A, Vajda S. Ligand deconstruction: Why some fragment binding positions are conserved and others are not. Proc Natl Acad Sci U S A. 2015 May 19; 112(20):E2585-94.View Related Profiles. PMID: 25918377; PMCID: PMC4443342; DOI: 10.1073/pnas.1501567112;.
  9. Huang H, Pandya C, Liu C, Al-Obaidi NF, Wang M, Zheng L, Toews Keating S, Aono M, Love JD, Evans B, Seidel RD, Hillerich BS, Garforth SJ, Almo SC, Mariano PS, Dunaway-Mariano D, Allen KN, Farelli JD. Panoramic view of a superfamily of phosphatases through substrate profiling. Proc Natl Acad Sci U S A. 2015 Apr 21; 112(16):E1974-83. PMID: 25848029; PMCID: PMC4413258; DOI: 10.1073/pnas.1423570112;.
  10. London N, Farelli JD, Brown SD, Liu C, Huang H, Korczynska M, Al-Obaidi NF, Babbitt PC, Almo SC, Allen KN, Shoichet BK. Covalent docking predicts substrates for haloalkanoate dehalogenase superfamily phosphatases. Biochemistry. 2015 Jan 20; 54(2):528-37. PMID: 25513739; PMCID: PMC4303301; DOI: 10.1021/bi501140k;.
Showing 10 of 92 results. Show More

This graph shows the total number of publications by year, by first, middle/unknown, or last author.

Bar chart showing 92 publications over 21 distinct years, with a maximum of 8 publications in 2004 and 2014

YearPublications
19892
19943
19952
19992
20002
20011
20025
20034
20048
20055
20066
20075
20086
20093
20104
20117
20124
20135
20148
20157
20163
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Boston MA 02215
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