السلام عليكم
 

ممكن اسأل سؤال؟ هو فيه ورق في المكتبة بتاع organic ولا مفيش؟اصلي مش بفهم حاجة من الدكتور كمال ده:angry2:..............

دلوقتى بالنسبة لسكشن الكيميا قبل ما يحصل تغيير فى السكاشن كانت بتدينا معيدة اسمها د.امل وكمان كان بيدينا د.سامح كانوا بتكلموا عن الاملاح 00000الى اخره
وكمان كتبوا لنا التفاعلات بالمعادلات وطبعا المفروض انها تتحفظ
لما تغيرت السكاشن دخل لنا معيد اسمه د.محمد ما كتبش ولا معادلة خالص إلا بس معادلتين قال انهم مهمين
ولما صاحبتى سالت د.امل عن المعادلات قالت لها انك لازم تطلعيهم من الكتاب العملى وتحفظيهم وقالت لها اننا_المعيدين _ مش بنكتب المعادلات كلها اللى موجودة فى الكتاب لأنه المفروض مسموح لنا بنص ساعة بس شرح وباقى الوقت عملى
فأنا مش عارفة احنا مطالبين باننا نحفظ المعادلات اللى الدكتور بيقولها واللى مش بيقولها مع العلم ان الدكتور اللى بيدينى مش بيكتب معادلات
وانتوا عندكوا نظام السكشن ايه؟؟؟!!!!:(

السلام عليكم
 

لا السكشن عندنا معيد كويس بس معرفش اسمه ايه؟..بس بيكتب كل حاجة علي السبورة بصي فيه ورق عملي كيمياء في المكتبة ابقي هاتيه:romarioxp6:

اتفضلوا يا جماعه شويه حاجات كده لقيتها عن enzymes

هى مش كلها علينا بس ممكن تقروها هتبقى كويسه باذن الله


Enzymes are biomolecules that catalyze (i.e. increase the rates of) chemical reactions.[1][2] Almost all enzymes are proteins. In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products. Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few reactions from among many possibilities, the set of enzymes made in a cell determines which metabolic pathways occur in that cell.
Like all catalysts, enzymes work by lowering the activation energy (Ea or ΔG‡) for a reaction, thus dramatically increasing the rate of the reaction. Most enzyme reaction rates are millions of times faster than those of comparable un-catalyzed reactions. As with all catalysts, enzymes are not consumed by the reactions they catalyze, nor do they alter the equilibrium of these reactions. However, enzymes do differ from most other catalysts by being much more specific. Enzymes are known to catalyze about 4,000 biochemical reactions.[3] A few RNA molecules called ribozymes catalyze reactions, with an important example being some parts of the ribosome.[4][5] Synthetic molecules called artificial enzymes also display enzyme-like catalysis.[6]
Enzyme activity can be affected by other molecules. Inhibitors are molecules that decrease enzyme activity; *********s are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. Activity is also affected by temperature, chemical environment (e.g. pH), and the concentration of substrate. Some enzymes are used commercially, for example, in the synthesis of antibiotics. In addition, some household products use enzymes to speed up biochemical reactions (e.g., enzymes in biological washing powders break down protein or fat stains on clothes; enzymes in meat tenderizers break down proteins, making the meat easier to chew)

وفيه صوره فى المرفقات للتوضيح

ولو عجبكم فيه الcofactors and co enzymes

السلام عليكم
 

شكرا يا د.جولييت على المجهود ده
بس كنت عايزة حد يفهمنى الجزء بتاع ال
allosteric site & regulation enzyme
وكمان د .عادل اتكلم عن poly peptide chain وقال انها تنقسم الى
(functional &nonfunctional)
معلش انا مش فهماهم:(

انا عايز اسال الجماعه اللى معايا فى مجموعه ب كام سؤال وياريت د/احمد يفيدنا

1- بتذاكروا ازاى محاضرات د/بسيونى(الله يسامحه)

2-د/عادل عبد العال شرح محاضرتين فهمتهم وبعد ما طلعت من المحاضره لقيت انى مش كاتب حاجه وده لانه بتكلم بسرعه و نادرا ما بيكتب

3- العملى اللى بناخده ونظرى العملى بنمتحن فيهم ازاى

4- لو ذاكرت المحاضرات و المذكرات بس كفايه ولا ايه؟







والف شكر.........................

والله انا مش عارف احنا خدنا ده ولا ايه؟؟؟؟

اصلي مش بفتحها ....مستني ربنا يفرجها

بس النهارده يمكن انزل جزء من كتاب السنة اللي فاتت بتاعه حوال 10 -15 صفحة
في الجزء اللي خدناه
ولو دورتي هنا في الموضوع حتلاقيني ملخصهم في 5 ورقات

:078111rg3::078111rg3:

اعتقد اسم حضرتك عبد الرحمن.صح؟؟انا فاكر كده...

انا مش في مجموعة ب عشان كده مش عارف د/بسيوني بيشرح ازاي
بس فيه ناس من ب بتيجي تحضر معانا يوم الاحد

........

بالنسبة لدكتور عادل ...انا مش بكتب وراه حاجة بصراحو ومش بفهم حاجة
بيبقى عندي شهور بالبهيمية.....بس بحاول والله

.......

امتحانات العملي

عندك الحيوان حيبقى يقولك شرح الضفدعة جهاز معين فيها وارسمه او اكتب بيانات على رسم جاهز

والنبات بتشوف عينات وبترسمها اوتكتب بيانات برضه وكمان تجارب الفسيولوجي

الفيزياء من التجارب اللي بناخدها

والكيمياء حييجي يديك ملح (مش حيقولك ده كربونات ولا بيكربونات) حيسيبك منك له وانت تتعرف عليه

وتبدا تحذف احتمالات لغاية ماتوصل للملح (فيه املاح ملهاش عملي زي السلفايد والنيتريت والايودين..)

اللي بتطلع روائح سيئة او سموم او انفجارات:(

احنا دلوقتي بناخد الشق الحامضي وبعد كده القاعدي ونركبهم على بعض يطلعوا الملح في اخر الترم

:078111rg3::078111rg3::078111rg3:

cofactors
 

cofactors
Some enzymes do not need any additional components to show full activity. However, others require
non-protein molecules called cofactors to be bound for activity.[41] Cofactors can be either inorganic (e.g., metal ions and iron-sulfur clusters) or organic compounds, (e.g., flavin and heme). Organic cofactors can be either prosthetic groups, which are tightly bound to an enzyme, or coenzymes, which are released from the enzyme's active site during the reaction. Coenzymes include NADH, NADPH and adenosine triphosphate. These molecules act to transfer chemical groups between enzymes.[42]
An example of an enzyme that contains a cofactor is carbonic anhydrase, and is shown in the ribbon diagram above with a zinc cofactor bound as part of its active site.[43] These tightly-bound molecules are usually found in the active site and are involved in catalysis. For example, flavin and heme cofactors are often involved in redox reactions.
Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An apoenzyme together with its cofactor(s) is called a holoenzyme (this is the active form). Most cofactors are not covalently attached to an enzyme, but are very tightly bound. However, organic prosthetic groups can be covalently bound (e.g., thiamine pyrophosphate in the enzyme pyruvate dehydrogenase). The term "holoenzyme" can also be applied to enzymes that contain multiple protein subunits, such as the DNA polymerases, here the holoenzyme is the complete complex containing all the subunits needed for activity.

للأسف مش عارفه الحاجات دى فين:(
بس اللى انا فاكراه من السنه اللى اللى فاتت ان الريجولاشن انزيمز دى بتنظم عمليات معينه فى الجسم زى مثلا انزيمات الهضم اللى بتفرز فى المعده والحاجات دى برضه اكييد بينظموا العمليات فى النبات
بس ممكن اشوفهالك او ممكن تبقى تسأليه بعد المحاضره

على فكرة واحنا كمان فى السكشن بتعنا بيدينا د.محمد ومبيكتبش معادلات برضة :mad::mad:
وعلى فكرة د.سامح اللى كان بيديكى دة هو اللى بينزل ورق inorganic,phisical
ودة دكتور كويس اوى :av4056bb7jp3::av4056bb7jp3:
واكيد حنمشى على نظام المذكرات اللى هو بينزلها
علشان نضمن العملى:078111rg3::078111rg3:

coenzymes
 

Coenzymes are small organic molecules that transport chemical groups from one enzyme to another.[44] Some of these chemicals such as riboflavin, thiamine and folic acid are vitamins, this is when these compounds cannot be made in the body and must be acquired from the diet. The chemical groups carried include the hydride ion (H-) carried by NAD or NADP+, the acetyl group carried by coenzyme A, formyl, methenyl or methyl groups carried by folic acid and the methyl group carried by S-adenosylmethionine.
Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates, which are common to many different enzymes. For example, about 700 enzymes are known to use the coenzyme NADH.[45]
Coenzymes are usually regenerated and their concentrations maintained at a steady level inside the cell: for example, NADPH is regenerated through the pentose phosphate pathway and S-adenosylmethionine by methionine adenosyltransferase.