Biopolymers

Cover image for Vol. 103 Issue 4

Edited By: Gary D. Glick

Impact Factor: 2.288

ISI Journal Citation Reports © Ranking: 2013: 45/74 (Biophysics); 190/291 (Biochemistry & Molecular Biology)

Online ISSN: 1097-0282

Associated Title(s): Peptide Science

Featured

  • Polymorphic crystal structures of an all-AT DNA dodecamer

    Polymorphic crystal structures of an all‐AT DNA dodecamer

    Example of two crossovers in Form VI. In all cases, the pseudo TA base step between neighboring duplexes in a column is involved in the interaction. (a) Left handed; (b) right handed.

  • Stacking interactions in RNA and DNA: Roll-slide energy hyperspace for ten unique dinucleotide steps

    Stacking interactions in RNA and DNA: Roll‐slide energy hyperspace for ten unique dinucleotide steps

    Energy contours for the purine–pyrimidine steps at four different twists without solvent. Color-bar is given in kcal/mol. The contour lines are 1 kcal/mol apart.

  • Effect of a buried ion pair in the hydrophobic core of a protein: An insight from constant pH molecular dynamics study

    Effect of a buried ion pair in the hydrophobic core of a protein: An insight from constant pH molecular dynamics study

    Microenvironment of the V23E/L36K variant of Δ+PHS protein (PDB ID: 3NHH) showing several important core residues, Asp-21, Glu-23, Arg-35, and Lys-36.

  • Essential dynamics analysis captures the concerted motion of the integrin-binding site in jerdostatin, an RTS disintegrin

    Essential dynamics analysis captures the concerted motion of the integrin‐binding site in jerdostatin, an RTS disintegrin

    Ribbon drawings of representative models of R24K mutant during the MD simulation. The residues discussed in the text are represented as Connolly surfaces and K24 as sticks.

  • Biophysical properties and thermal stability of oligonucleotides of RNA containing 7,8-dihydro-8-hydroxyadenosine

    Biophysical properties and thermal stability of oligonucleotides of RNA containing 7,8‐dihydro‐8‐hydroxyadenosine

    Sequence and structure of RNA strands 18 and 19. Tm values were obtained from their CD spectra and were performed in triplicate.

  • Beaded nanofibers assembled from double-hydrophobic elastin-like block polypeptides: Effects of trifluoroethanol

    Beaded nanofibers assembled from double‐hydrophobic elastin‐like block polypeptides: Effects of trifluoroethanol

    (a) Domain structures in the elastin precursor, tropoelastin. Reprinted with permission from Tamburro, A. M.; Bochicchio, B.; Pepe, A. Biochemistry 2003, 42, 13347–13362. Copyright 2003, American Chemical Society. (b) Amino acid sequences of constructed triblock GPG and its block components P and G.

  • Polymorphic crystal structures of an all‐AT DNA dodecamer
  • Stacking interactions in RNA and DNA: Roll‐slide energy hyperspace for ten unique dinucleotide steps
  • Effect of a buried ion pair in the hydrophobic core of a protein: An insight from constant pH molecular dynamics study
  • Essential dynamics analysis captures the concerted motion of the integrin‐binding site in jerdostatin, an RTS disintegrin
  • Biophysical properties and thermal stability of oligonucleotides of RNA containing 7,8‐dihydro‐8‐hydroxyadenosine
  • Beaded nanofibers assembled from double‐hydrophobic elastin‐like block polypeptides: Effects of trifluoroethanol

Recently Published Issues

See all

Anniversary Special Issues

October 2013
Volume 99, Issue 10
Special Issue: Glycosciences

November 2013
Volume 99, Issue 11
Special Issue: Proteins

December 2013
Volume 99, Issue 12
Special Issue: Nucleic Acids

Going Green

BIOPOLYMERS PeptideBiopolymers became an Online Only journal in January, 2013. As you no longer receive Biopolymers in your mailbox, it's now more important than ever to sign up for email table-of-contents alerts. Be the first to know when Biopolymers publishes new research.

News

MG Prize winner

Announcing the 2014 Winner of the Biopolymers Murray Goodman Memorial Prize

Steven G. Boxer PhD
Camille and Henry Dreyfus Professor of Chemistry
Department of Chemistry
Stanford University

The prize recognizes Dr. Boxer's seminal contributions applying physical tools to the study of protein structure and function.

SEARCH

SEARCH BY CITATION