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T Kortemme

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Journal of Molecular Biology|November 10, 1995
Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin familyT Kortemme, T E Creighton
Biochemistry|June 24, 1998
Ionization-reactivity relationships for cysteine thiols in polypeptidesG Bulaj, T Kortemme, D P Goldenberg
Science (New York, N.Y.)|July 10, 1998
Design of a 20-amino acid, three-stranded beta-sheet proteinT Kortemme, M Ramírez-Alvarado, L Serrano
Protein Science : a Publication of the Protein Society|May 1, 1994
Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactionsA Chakrabartty, T Kortemme, R L Baldwin
Biochemistry|November 19, 1996
Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomeraseT Kortemme, N J Darby, T E Creighton
Biochemistry|June 1, 1993
Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensitiesA Chakrabartty, T Kortemme, S Padmanabhan, et al.
Journal of Molecular Biology|March 22, 1996
Comparison of the (30-51, 14-38) two-disulphide folding intermediates of the homologous proteins dendrotoxin K and bovine pancreatic trypsin inhibitor by two-dimensional 1H nuclear magnetic resonanceT Kortemme, M Hollecker, J Kemmink, et al.
Bioorganic & Medicinal Chemistry|April 13, 1999
Beta-hairpin and beta-sheet formation in designed linear peptidesM Ramírez-Alvarado, T Kortemme, F J Blanco, et al.
Current Opinion in Structural Biology|August 17, 1999
The design of linear peptides that fold as monomeric beta-sheet structuresE Lacroix, T Kortemme, M Lopez de la Paz, et al.
Journal of Molecular Biology|April 15, 2000
Similarities between the spectrin SH3 domain denatured state and its folding transition stateT Kortemme, M J Kelly, L E Kay, et al.
Pageof 1

Showing results (1-10 of 10) with videos related to

Sort By:
Pageof 1
Journal of Molecular Biology|November 10, 1995
Ionisation of cysteine residues at the termini of model alpha-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin familyT Kortemme, T E Creighton
Biochemistry|June 24, 1998
Ionization-reactivity relationships for cysteine thiols in polypeptidesG Bulaj, T Kortemme, D P Goldenberg
Science (New York, N.Y.)|July 10, 1998
Design of a 20-amino acid, three-stranded beta-sheet proteinT Kortemme, M Ramírez-Alvarado, L Serrano
Protein Science : a Publication of the Protein Society|May 1, 1994
Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactionsA Chakrabartty, T Kortemme, R L Baldwin
Biochemistry|November 19, 1996
Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomeraseT Kortemme, N J Darby, T E Creighton
Biochemistry|June 1, 1993
Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensitiesA Chakrabartty, T Kortemme, S Padmanabhan, et al.
Journal of Molecular Biology|March 22, 1996
Comparison of the (30-51, 14-38) two-disulphide folding intermediates of the homologous proteins dendrotoxin K and bovine pancreatic trypsin inhibitor by two-dimensional 1H nuclear magnetic resonanceT Kortemme, M Hollecker, J Kemmink, et al.
Bioorganic & Medicinal Chemistry|April 13, 1999
Beta-hairpin and beta-sheet formation in designed linear peptidesM Ramírez-Alvarado, T Kortemme, F J Blanco, et al.
Current Opinion in Structural Biology|August 17, 1999
The design of linear peptides that fold as monomeric beta-sheet structuresE Lacroix, T Kortemme, M Lopez de la Paz, et al.
Journal of Molecular Biology|April 15, 2000
Similarities between the spectrin SH3 domain denatured state and its folding transition stateT Kortemme, M J Kelly, L E Kay, et al.
Pageof 1