Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Method to Extend Research in Time (MERIT) Award (R37)
Project #
5R37GM013453-31
Application #
2168659
Study Section
Special Emphasis Panel (NSS)
Project Start
1976-12-01
Project End
1997-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
31
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Massachusetts Institute of Technology
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139
Moreau, Robert J; Schubert, Christian R; Nasr, Khaled A et al. (2009) Context-independent, temperature-dependent helical propensities for amino acid residues. J Am Chem Soc 131:13107-16
Nasr, Khaled A; Schubert, Christian R; Torok, Marianna et al. (2009) Helix-coil energetics for helix formers and breakers reflect context and temperature: mutants of helically robust, guest-sensitive homopeptide hosts. Biopolymers 91:311-20
Fotouhi, N; Kemp, D S (1993) Novel class of silicon-based protective groups for the side chain of tyrosine. Int J Pept Protein Res 41:153-61
Fotouhi, N; Bowen, B R; Kemp, D S (1992) Resolution of proline acylation problem for thiol capture strategy by use of a chloro-dibenzofuran template. Int J Pept Protein Res 40:141-7
Kemp, D S; Fotouhi, N; Boyd, J G et al. (1988) Practical preparation and deblocking conditions for N-alpha-(2-(p-biphenylyl)-2-propyloxycarbonyl)-amino acid (N-a-Bpoc-Xxx-OH) derivatives. Int J Pept Protein Res 31:359-72