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L Serrano

Showing results (1-10 of 614) with videos related to

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Advances in Protein Chemistry|April 7, 2000
The relationship between sequence and structure in elementary folding unitsL Serrano
MLO: Medical Laboratory Observer|July 27, 2001
Laboratory automation: a case studyL Serrano
Journal of Molecular Biology|November 24, 1995
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformationL Serrano
American Journal of Hospital Pharmacy|November 1, 1989
Central American countries need drug products and medical suppliesJ L Serrano
Current Opinion in Structural Biology|February 17, 2001
Protein design based on folding modelsR Guerois, L Serrano
Protein Science : a Publication of the Protein Society|February 27, 1999
Molecular dynamics as a tool to detect protein foldability. A mutant of domain B1 of protein G with non-native secondary structure propensitiesD Cregut, L Serrano
Biochemistry|November 21, 1995
Analysis of i,i+5 and i,i+8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motifV Muñoz, L Serrano
Biopolymers|April 15, 1997
Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalismsV Muñoz, L Serrano
Anales Espanoles De Pediatria|March 1, 1979
[Cytological and bacteriological study of the vagina in newborn in a hospital environment (author's transl)]J L Serrano Luna
Journal of Molecular Biology|December 22, 2000
The SH3-fold family: experimental evidence and prediction of variations in the folding pathwaysR Guerois, L Serrano
Pageof 62

Showing results (1-10 of 614) with videos related to

Sort By:
Pageof 62
Advances in Protein Chemistry|April 7, 2000
The relationship between sequence and structure in elementary folding unitsL Serrano
MLO: Medical Laboratory Observer|July 27, 2001
Laboratory automation: a case studyL Serrano
Journal of Molecular Biology|November 24, 1995
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformationL Serrano
American Journal of Hospital Pharmacy|November 1, 1989
Central American countries need drug products and medical suppliesJ L Serrano
Current Opinion in Structural Biology|February 17, 2001
Protein design based on folding modelsR Guerois, L Serrano
Protein Science : a Publication of the Protein Society|February 27, 1999
Molecular dynamics as a tool to detect protein foldability. A mutant of domain B1 of protein G with non-native secondary structure propensitiesD Cregut, L Serrano
Biochemistry|November 21, 1995
Analysis of i,i+5 and i,i+8 hydrophobic interactions in a helical model peptide bearing the hydrophobic staple motifV Muñoz, L Serrano
Biopolymers|April 15, 1997
Development of the multiple sequence approximation within the AGADIR model of alpha-helix formation: comparison with Zimm-Bragg and Lifson-Roig formalismsV Muñoz, L Serrano
Anales Espanoles De Pediatria|March 1, 1979
[Cytological and bacteriological study of the vagina in newborn in a hospital environment (author's transl)]J L Serrano Luna
Journal of Molecular Biology|December 22, 2000
The SH3-fold family: experimental evidence and prediction of variations in the folding pathwaysR Guerois, L Serrano
Pageof 62