Impact Factor
3.08
Journal Citation Impact
Estimated influence, citation density, publishing volume, and citation integrity from the analytics table.
Citation rate
2.27
293 total citations
h5-index
23
h5 depth signal
Cited share
59.5%
78 of 131
Total citations
293
Citation footprint
Metric signal
2.95
External metric anchor
Self-citation
2.7%
8 self-citations
Citations Trend
Monthly Publications Cadence
Citing Geographic Demographics
United States
128
India
65
China
60
Germany
36
United Kingdom
28
Citing Fields of Research
Polymer & Macromolecule Science
120
Protein Structure & Folding
98
Nucleic Acids Chemistry
85
Nanofibers, Scaffolds & Fabrication
80
Polymer Science
67
Publishing Activity & Reach
Volume, recency, access pattern, and citing-community signals from the journal analytics record.
All-time article footprint
10,018
Articles tracked across the journal lifetime
Indexed publication set
131
78 cited publications
Last 12 months
72
6.5 publications/month
Open access share
27.8%
20 OA publications in the last year
Leading citing country
United States
128 citing publications
Leading citing field
Polymer & Macromolecule Science
120 citing publications
Latest tracked publication
16 October 2026
10 recent records available
Coverage & Indexing History
v3n1, 1965-
v3n1, 1965-
Active Coverage
Research Focus & Classification
Indexed Subjects
Polymer & Macromolecule Science
Nanofibers, Scaffolds & Fabrication
Food Science & Technology
Drug Delivery Systems
Polymer Science
Issuing & Sponsoring Bodies
Contributor
American Peptide Society
Broad Categories
Biochemistry
Food Science & Technology
Nanofibers, Scaffolds & Fabrication
Paper & Wood Materials Science
Drug Delivery Systems
Polymer & Macromolecule Science
MeSH Descriptors
Nucleic Acids
Peptides
Polymers
Polysaccharides
Proteins
Latest Publications
Recent article records with DOI-first linking and condensed abstracts.
01
DOI 10.1002/bip.70127
Open DOI
Polyglycine Strands Within a Collagen Triple Helix
The collagen triple helix is the most abundant protein structural motif in animals. It tolerates any amino acid in its Xaa and Yaa positions but demands glycine (Gly) at every third position, where the residue packs into the sterically f...
02
DOI 10.1002/bip.70126
Open DOI
Molecular Interactions Between Bacteriorhodopsin Protein Embedded Within Purple Membrane and the Surfaces of Polyvinyl Alcohol ( PVA ) and Graphene
Bacteriorhodopsin (bR), the light‐driven proton pump of Halobacterium salinarum , is a promising candidate for bioelectronic and optoelectronic applications. Its utility in hybrid systems depends on how surrounding materials influence st...
03
DOI 10.1002/bip.70110
Open DOI
Issue Information
04
DOI 10.1002/bip.70125
Open DOI
Pre‐Esterification Dry Heat Treatment Enhances the Functional Properties of Starch Citrate: Enzyme Resistance and Water Absorption
This study investigates how pre‐esterification dry heat treatment (DHT) of corn starch at 170°C, 180°C, and 200°C influences the functional properties of subsequently synthesized starch citrates. Structural and morphological changes indu...
05
DOI 10.1002/bip.70123
Open DOI
Biogenic Silver Nanoparticles‐Loaded Collagen–L‐Lysine Matrices in Gel and Spray Formulations for Improved Skin Wound Repair
Biogenic silver nanoparticles (AgNPs) are emerging as valuable candidates in biomedical research, offering advantages such as cost‐effectiveness, eco‐friendly preparation methods, and superior biocompatibility. Owing to the challenges in...
06
DOI 10.1002/bip.70124
Open DOI
Bacterial Cellulose Membranes for Dye Removal: Adsorption Behavior, Thermodynamics, Regeneration, and Performance in Simulated Wastewater
Bacterial cellulose is a sustainable biopolymeric material with considerable potential for wastewater treatment due to its nanofibrous structure and abundance of hydroxyl groups. In this study, BC membranes were evaluated as adsorbents f...
07
DOI 10.1002/bip.70122
Open DOI
Unraveling the Asymmetric Hydration Dynamics and Water‐Mediated Stabilization in Collagen Heterotrimers
Collagen's triple helix structure is fundamental to the mechanical integrity of bodily tissues, and its stability is vital for optimal physiological function. While the stabilization mechanisms of simple, symmetric collagen homotrimers h...
08
DOI 10.1002/bip.70121
Open DOI
High‐Efficiency Carboxymethylation Achieved by Enhancing Hydroxyl Accessibility Through Glycerol Pretreatment of Bacterial Cellulose
Due to its dense crystalline structure and extensive hydrogen bonding network, cellulose exhibits limited reactive accessibility and reactivity, which severely restricts the reaction efficiency, degree of substitution, and uniformity of ...
09
DOI 10.1002/bip.70120
Open DOI
Inherent α‐Helix Around Tyrosine 183 in the Intrinsically Disordered Tail of the Multi‐Site Docking Platform Gab1
The biological function of intrinsically disordered proteins is frequently coupled to short linear motifs, which serve as protein binding sites. This goes often hand in hand with local transient structural element formation. The intrinsi...
10
DOI 10.1002/bip.70119
Open DOI
Role of Water in Starch Mechanical Treatment
The impact of initial moisture content (1.5%–20%) on the ball‐milling of pea starch was investigated across multiple structural levels. Scanning electron microscopy revealed moisture‐dependent deformation mechanisms: plastic flow and agg...
Bibliographical & Catalog Notes
Beginning in 1995, six issues per year constitute the section publication: Biopolymers. Peptide science, which is published in cooperation with the American Peptide Society. Beginning in 1997, four issues per year constitute the section publication: Biopolymers. Nucleic acid sciences. Beginning in 2000, six issues per year constitute the section publication: Biopolymers. Biospectroscopy. (Frequency varies for section issues.)
Volume numbering for the section publications: Biopolymers. Peptide science, Biopolymers. Nucleic acid sciences, and Biopolymers. Biospectroscopy are integrated as part of the parent title's regular publication numbering.
Also available online.
Peptide science issues published in cooperation with the American Peptide Society.
Vol. 25 (1986)19900917 Notice not published Printed on acid-free paper