相关实验视频

Updated: Jul 1, 2025

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
11:14

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

16.1K

无序的蛋白质与化学环境相互作用,在干燥过程中调整它们的保护功能

Shraddha Kc, Kenny H Nguyen, Vincent Nicholson

    bioRxiv : the preprint server for biology
    |March 11, 2024
    PubMed
    概括

    内在无序蛋白质 (IDP) 和溶解蛋白在干燥过程中保护生物体. 它们的保护协同作用是一个融合的策略,但蛋白质家族之间的机制不同,如LEA和CAHS.

    更多相关视频

    Methods for the Self-integration of Megamolecular Biopolymers on the Drying Air-LC Interface07:06

    Methods for the Self-integration of Megamolecular Biopolymers on the Drying Air-LC Interface

    Published on: April 7, 2017

    6.1K
    How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project07:22

    How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project

    Published on: February 11, 2019

    28.2K

    相关概念视频

    Protein Denaturation01:28

    Protein Denaturation

    The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
    4.2K
    Protein Folding01:25

    Protein Folding

    Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
    Protein Structure Is Critical to Its Biological Function
    Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
    8.0K
    Intrinsically Disordered Proteins02:18

    Intrinsically Disordered Proteins

    Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
    17.8K
    Molecular Chaperones and Protein Folding03:00

    Molecular Chaperones and Protein Folding

    The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
    The...
    17.9K
    Protein-protein Interfaces02:04

    Protein-protein Interfaces

    Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
    12.5K
    Protein Modifications in the RER01:26

    Protein Modifications in the RER

    Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
    Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
    5.2K