Unknown

Dataset Information

0

Microproteins: a 3D protein structure prediction analysis.


ABSTRACT: Microproteins are a novel and expanding group of small proteins encoded by less than 100-150 codons that are translated from small open reading frames (smORFs). It has been shown that smORFs and their corresponding microproteins make up a sizable fraction of the genome and proteome, but very little information on microproteins' structural features exists in the literature. In this paper, we present the results of analyzing the predicted structures of 44 microproteins. The results show that this set of microproteins have a different amino acid composition profiles, similar structural characteristics and fewer small-molecule ligand binding sites than regular proteins.Communicated by Ramaswamy H. Sarma.

SUBMITTER: Thambu K 

PROVIDER: S-EPMC9489054 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

altmetric image

Publications

Microproteins: a 3D protein structure prediction analysis.

Thambu Kishan K   Glomb Victoria V   Hernandez Trapero Rolando R   Facelli Julio C JC  

Journal of biomolecular structure & dynamics 20211027 24


Microproteins are a novel and expanding group of small proteins encoded by less than 100-150 codons that are translated from small open reading frames (smORFs). It has been shown that smORFs and their corresponding microproteins make up a sizable fraction of the genome and proteome, but very little information on microproteins' structural features exists in the literature. In this paper, we present the results of analyzing the predicted structures of 44 microproteins. The results show that this  ...[more]

Similar Datasets

| S-EPMC2880412 | biostudies-literature
| S-EPMC9791599 | biostudies-literature
| S-EPMC4304177 | biostudies-literature
| S-EPMC3024132 | biostudies-other
| S-EPMC11229186 | biostudies-literature
| S-EPMC8336827 | biostudies-literature
| S-EPMC3746096 | biostudies-literature
| S-EPMC11260495 | biostudies-literature
| S-EPMC3608176 | biostudies-other
| S-EPMC373465 | biostudies-literature