Agency
National Institute of Health (NIH)
Institute
National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
Type
Research Project (R01)
Project #
5R01AR019626-18
Application #
2078438
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1977-03-01
Project End
1999-08-31
Budget Start
1996-09-01
Budget End
1997-08-31
Support Year
18
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Medicine & Dentistry of NJ
Department
Biochemistry
Type
Schools of Medicine
DUNS #
622146454
City
Piscataway
State
NJ
Country
United States
Zip Code
08854
Kramer, R Z; Bella, J; Brodsky, B et al. (2001) The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. J Mol Biol 311:131-47
Kramer, R Z; Venugopal, M G; Bella, J et al. (2000) Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair. J Mol Biol 301:1191-205
Ackerman, M S; Bhate, M; Shenoy, N et al. (1999) Sequence dependence of the folding of collagen-like peptides. Single amino acids affect the rate of triple-helix nucleation. J Biol Chem 274:7668-73
Shah, N K; Brodsky, B; Kirkpatrick, A et al. (1999) Structural consequences of D-amino acids in collagen triple-helical peptides. Biopolymers 49:297-302
Baum, J; Brodsky, B (1999) Folding of peptide models of collagen and misfolding in disease. Curr Opin Struct Biol 9:122-8
Ramshaw, J A; Shah, N K; Brodsky, B (1998) Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J Struct Biol 122:86-91
Beck, K; Brodsky, B (1998) Supercoiled protein motifs: the collagen triple-helix and the alpha-helical coiled coil. J Struct Biol 122:17-29
Kramer, R Z; Vitagliano, L; Bella, J et al. (1998) X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly). J Mol Biol 280:623-38
Liu, X; Kim, S; Dai, Q H et al. (1998) Nuclear magnetic resonance shows asymmetric loss of triple helix in peptides modeling a collagen mutation in brittle bone disease. Biochemistry 37:15528-33
Baum, J; Brodsky, B (1997) Real-time NMR investigations of triple-helix folding and collagen folding diseases. Fold Des 2:R53-60

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