Difference: ArthurPalmer (20 vs. 21)

Revision 2123 Jan 2009 - Main.DavidHirsh

 
META TOPICPARENT name="TWikiUsers"
Added:
>
>
  • Address: Black Building 507, 630 West 168th Street New York, NY 10032
 
  • Country: USA
Changed:
<
<
  • Comment: Hard to contact. Currently best to leave messages at Dept number NYSBC NMR Park Bldg 900 Magnet Black Building 507, 630 West 168th Street, Columbia email agp6@columbia.edu Professor and Acting Chair Department of Biochemistry Deparment Office: (212) 305-3669 and Molecular Biophysics Department FAX: (212) 305-7932 Columbia University Laboratory Office: (212) 305-8675 630 West 168th Street, Box 36 Laboratory FAX: (212) 305-6949 New York, NY 10032-3702 email: agp6@columbia.edu WWW: www.palmer.hs.columbia.edu
>
>
  • Comment: Hard to contact. Currently best to leave messages at Dept number NYSBC NMR Park Bldg 900 Magnet Columbia email agp6@columbia.edu Professor and Acting Chair Department of Biochemistry Deparment Office: (212) 305-3669 and Molecular Biophysics Department FAX: (212) 305-7932 Columbia University Laboratory Office: (212) 305-8675 630 West 168th Street, Box 36 Laboratory FAX: (212) 305-6949 New York, NY 10032-3702 email: agp6@columbia.edu
Added:
>
>
Assistant: Ed Johnson 212-305-3882 etj1@columbia.edu
 

Grants associated with NYSBC

GM59273

  1. GM 59273 5/1/02-4/30/06; 5/1/06-4/30/10 has been awarded CRISP UPDATE PENDING
National Institutes of Health Protein motions in recognition, regulation, and catalysis Development and application of methods for assessing the functional importance of large amplitude conformational dynamics on microsecond-millisecond time scales in proteins. Applications include protein folding, ligand-binding, and catalysis. Major foci include conformational dynamics in TIM barrel proteins and folding of small, fast-folding, model proteins.

GM50291

Grant Number: 2R01GM050291-12 PI Name: PALMER, ARTHUR G. PI Email: agp6@columbia.edu PI Title: PROFESSOR Project Title: Nuclear Magnetic Resonance Studies of Proteins

Abstract: DESCRIPTION (provided by applicant): Comprehensive experimental information on the essential contributions of intramolecular dynamics to biological functions of proteins is critical for biophysical theories of equilibrium properties, such as heat capacity and thermal stability; for mechanistic interpretations of kinetic processes, such as enzyme catalysis and ligand recognition; and for design of novel proteins and protein ligands, including pharmaceutical agents. This research project will use multidimensional NMR spectroscopy to address these fundamental issues. One long-term goal is to define the molecular determinants of stability and catalytic activity of the enzyme ribonuclease HI (RNase H) by comparing the structural, dynamical and enzymatic properties of homologous proteins derived from Escherichia coli and the extremely thermophilic bacterium Thermus thermophilus. The enzyme is distributed widely in prokaryotes and eukaryotes, and retroviral reverse transcriptase contains a C-terminal RNase H domain. Another long-term goal is to define the molecular determinants of ligand binding, including aspects of specificity, and allosterism, in DNA recognition by the yeast protein GCN4 and in nucleotide binding by the ATP-binding cassette (ABC) MJ1267 of the branched chain amino acid (LIV) transporter from Methanococcus jannaschii. GCN4 is the prototypical member of the bZip family of transcription activators. Motifs that recognize specific DNA sequences are ubiquitous components of proteins that regulate gene expression; consequently, explication of the molecular basis for recognition is critical for understanding normal biological function and pathology. GCN4 represents an example of induced fit molecular recognition through a disorder-order transition associated with DNA binding. The LIV transporter is a member of a diverse family of ABC transporters involved in numerous biological processes and diseases, including multidrug resistance and cystic fibrosis. ABC MJ1267 represents an example of selected-fit molecular recognition and allosteric transmission of conformational changes between remote sites in proteins.

Thesaurus Terms: bacterial protein, enzyme activity, intermolecular interaction, molecular dynamics, protein structure function, ribonuclease H, structural biology, thermostability adenosine diphosphate, adenosine triphosphate, biophysics, chemical kinetics, enzyme substrate complex, membrane transport protein, molecular site, nucleic acid, protein folding, species difference, temperature, transcription factor Archaea, Escherichia coli, nuclear magnetic resonance spectroscopy, site directed mutagenesis

Institution: COLUMBIA UNIVERSITY HEALTH SCIENCES PO Box 49 NEW YORK, NY 10032 Fiscal Year: 2005 Department: BIOCHEM & MOLECULAR BIOPHYSICS Project Start: 01-AUG-1994 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES IRG: MSFC

  • Short summary.
Characterization of the temperature dependence of conformational dynamics of ribonuclease H from mesophilic and thermophilic organisms using NMR spectroscopy. Conformational dynamics in the ATP-binding cassette MJ1267 from the branched chain amino acid transporter of Methanococcus jannaschii. Methods development is focused on experimental and theoretical aspects of picoseond-nanosecond time scale processes.

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)
    • Set ALLOWTOPICCHANGE =

Related topics

META FILEATTACHMENT attr="" comment="" date="1097786994" name="Palmer.jpg" path="Palmer.jpg" size="15233" user="DavidCowburn" version="1.1"
 
Copyright © by the contributing authors. All material on this collaboration platform is the property of the contributing authors.
Ideas, requests, problems regarding this intranet, Send feedback