Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM040746-07
Application #
2180568
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1989-04-01
Project End
1997-11-30
Budget Start
1995-12-01
Budget End
1996-11-30
Support Year
7
Fiscal Year
1996
Total Cost
Indirect Cost
Name
New York University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
004514360
City
New York
State
NY
Country
United States
Zip Code
10012
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Wang, L; Kallenbach, N R (1998) Proteolysis as a measure of the free energy difference between cytochrome c and its derivatives. Protein Sci 7:2460-4
Wang, L; Chen, R X; Kallenbach, N R (1998) Proteolysis as a probe of thermal unfolding of cytochrome c. Proteins 30:435-41
Yang, J; Spek, E J; Gong, Y et al. (1997) The role of context on alpha-helix stabilization: host-guest analysis in a mixed background peptide model. Protein Sci 6:1264-72
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Gong, Y; Zhou, H X; Guo, M et al. (1995) Structural analysis of the N- and C-termini in a peptide with consensus sequence. Protein Sci 4:1446-56
Zhong, M; Lin, L; Kallenbach, N R (1995) A method for probing the topography and interactions of proteins: footprinting of myoglobin. Proc Natl Acad Sci U S A 92:2111-5
Zhou, H X; Lyu, P; Wemmer, D E et al. (1994) Alpha helix capping in synthetic model peptides by reciprocal side chain-main chain interactions: evidence for an N terminal ""capping box"". Proteins 18:1-7
Lin, L; Pinker, R J; Phillips, G N et al. (1994) Stabilization of myoglobin by multiple alanine substitutions in helical positions. Protein Sci 3:1430-5
Lyu, P C; Wemmer, D E; Zhou, H X et al. (1993) Capping interactions in isolated alpha helices: position-dependent substitution effects and structure of a serine-capped peptide helix. Biochemistry 32:421-5

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